serratus and Procambarus clarkii. Contact Dermatitis. 2015;73(1):53-54.

1052. Lopata AL, Jeebhay MF. Airborne seafood allergens as a cause of occupational allergy and asthma. *Curr Allergy Asthma Rep.* 2013;13(3):288-297.

1053. Calleja Algarra A, Aragón Miguel R, Ortiz de Frutos FJ, Tous Romero F. Hand Lesions After Contact With Shellfish: Beyond Patch Testing. *Actas Dermosifiliogr (Engl Ed).* 2021;112(3):274-275.

1054. Jeebhay MF, Moscato G, Bang BE, et al. Food processing and occupational respiratory allergy- An EAACI position paper. *Allergy*. 2019;74(10):1852-1871.

1055. Nieuwenhuizen NE, Lopata AL. Anisakis-a food-borne parasite that triggers allergic host defences. *Int J Parasitol.* 2013;43(12-13):1047-1057.

1056. Shanti KN, Martin BM, Nagpal S, Metcalfe DD, Rao PV. Identification of tropomyosin as the major shrimp allergen and characterization of its IgE-binding epitopes. *J Immunol.* 1993;151(10):5354-5363.

1057. Kamath SD, Scheiblhofer S, Johnson CM, et al. Effect of structural stability on endolysosomal degradation and T-cell reactivity of major shrimp allergen tropomyosin. *Allergy*. 2020;75(11):2909-2919.

1058. Guillen D, Fiandor A, Del Pozo V, et al. Anaphylaxis caused by hemocyanin contained in shrimp cephalothorax. *Ann Allergy Asthma Immunol.* 2014;113(6):674-675.e672.

1059. Yang S, Huang H, Wang F, Aweya JJ, Zheng Z, Zhang Y. Prediction and characterization of a novel hemocyanin-derived antimicrobial peptide from shrimp Litopenaeus vannamei. *Amino Acids.* 2018;50(8):995-1005.

1060. Mendoza-Porras O, Kamath S, Harris JO, et al. Resolving hemocyanin isoform complexity in haemolymph of black tiger shrimp Penaeus monodon - implications in aquaculture, medicine and food safety. *J Proteomics.* 2020;218:103689.

1061. Nugraha R, Kamath SD, Johnston E, et al. Rapid and comprehensive discovery of unreported shellfish allergens using large-scale transcriptomic and proteomic resources. *J Allergy Clin Immunol.* 2018;141(4):1501-1504.e1508.

1062. Rona RJ, Keil T, Summers C, et al. The prevalence of food allergy: a meta-analysis. *J Allergy Clin Immunol.* 2007;120(3):638-646.

1063. Wang HT, Warren CM, Gupta RS, Davis CM. Prevalence and Characteristics of Shellfish Allergy in the Pediatric Population of the United States. *J Allergy Clin Immunol Pract.* 2020;8(4):1359-1370.e1352.

1064. Gámez C, Sánchez-García S, Ibáñez MD, et al. Tropomyosin IgE-positive results are a good predictor of shrimp allergy. *Allergy*. 2011;66(10):1375-1383.

1065. Yang AC, Arruda LK, Santos AB, et al. Measurement of IgE antibodies to shrimp tropomyosin is superior to skin prick testing with commercial extract and measurement of IgE to shrimp for predicting clinically relevant allergic reactions after shrimp ingestion. *J Allergy Clin Immunol.* 2010;125(4):872-878.

1066. Pascal MKS, Faber M. Diagnosis and management of shellfish allergy: current approach and future needs. *Curr Treat Options Allergy.* 2018;1-17. doi:10.1007/s40521-018-0186-0

1067. Wai CYY, Leung NYH, Leung ASY, Wong GWK, Leung TF. Seafood Allergy in Asia: Geographical Specificity and Beyond. *Front Allergy.* 2021;2:676903.

1068. Abramovitch JB, Kamath S, Varese N, et al. IgE Reactivity of Blue Swimmer Crab (Portunus pelagicus) Tropomyosin, Por p 1, and Other Allergens; Cross-Reactivity with Black Tiger Prawn and Effects of Heating. *PLoS One.* 2013;8(6):e67487.

1069. Vidal C, Bartolomé B, Rodríguez V, Armisén M, Linneberg A, González-Quintela A. Sensitization pattern of crustacean-allergic individuals can indicate allergy to molluscs. *Allergy*. 2015;70(11):1493-1496.

1070. Giuffrida MG, Villalta D, Mistrello G, Amato S, Asero R. Shrimp allergy beyond Tropomyosin in Italy: clinical relevance of Arginine

Kinase, Sarcoplasmic calcium binding protein and Hemocyanin. *Eur Ann Allergy Clin Immunol.* 2014;46(5):172-177.

1071. Thomassen MR, Kamath SD, Bang BE, et al. Occupational Allergic Sensitization Among Workers Processing King Crab (Paralithodes camtschaticus) and Edible Crab (Cancer pagurus) in Norway and Identification of Novel Putative Allergenic Proteins. *Front Allergy.* 2021;2:718824.

1072. Cox AL, Eigenmann PA, Sicherer SH. Clinical Relevance of Cross-Reactivity in Food Allergy. *J Allergy Clin Immunol Pract.* 2021;9(1):82-99.

1073. Wang J, Calatroni A, Visness CM, Sampson HA. Correlation of specific IgE to shrimp with cockroach and dust mite exposure and sensitization in an inner-city population. *J Allergy Clin Immunol.* 2011;128(4):834-837.

1074. Nowak-Wegrzyn A, Berin MC, Mehr S. Food Protein-Induced Enterocolitis Syndrome. *J Allergy Clin Immunol Pract.* 2020;8(1):24-35.

1075. Asaumi T, Yanagida N, Sato S, Shukuya A, Nishino M, Ebisawa M. Provocation tests for the diagnosis of food-dependent exercise-induced anaphylaxis. *Pediatr Allergy Immunol.* 2016;27(1):44-49.

1076. Caubet JC, Cianferoni A, Groetch M, Nowak-Wegrzyn A. Food protein-induced enterocolitis syndrome. *Clin Exp Allergy.* 2019;49(9):1178-1190.

1077. Warren CM, Aktas ON, Gupta RS, Davis CM. Prevalence and characteristics of adult shellfish allergy in the United States. *J Allergy Clin Immunol.* 2019;144(5):1435-1438.e1435.

1078. Morgan JE, O'Neil CE, Daul CB, Lehrer SB. Species-specific shrimp allergens: RAST and RAST-inhibition studies. *J Allergy Clin Immunol.* 1989;83(6):1112-1117.

1079. Jirapongsananuruk O, Sripramong C, Pacharn P, et al. Specific allergy to Penaeus monodon (seawater shrimp) or Macrobrachium rosenbergii (freshwater shrimp) in shrimp-allergic children. *Clin Exp Allergy.* 2008;38(6):1038-1047.

1080. Liu GY, Mei XJ, Hu MJ, et al. Analysis of the Allergenic Epitopes of Tropomyosin from Mud Crab Using Phage Display and Site-Directed Mutagenesis. *J Agric Food Chem.* 2018;66(34):9127-9137.

1081. Wong L, Tham EH, Lee BW. An update on shellfish allergy. *Curr Opin Allergy Clin Immunol.* 2019;19(3):236-242.

1082. Nugraha R, Kamath SD, Johnston E, Karnaneedi S, Ruethers T, Lopata AL. Conservation Analysis of B-Cell Allergen Epitopes to Predict Clinical Cross-Reactivity Between Shellfish and Inhalant Invertebrate Allergens. *Front Immunol.* 2019;10:2676.

1083. Ayuso R, Lehrer SB, Lopez M, et al. Identification of bovine IgG as a major cross-reactive vertebrate meat allergen. *Allergy*. 2000;55(4):348-354.

1084. Mahdavinia M, Tobin MC, Fierstein JL, et al. African American Children Are More Likely to Be Allergic to Shellfish and Finfish: Findings from FORWARD, a Multisite Cohort Study. *J Allergy Clin Immunol Pract.* 2021;9(7):2867-2872.e2861.

1085. Ayuso RS-GS, Lin J, et al. Greater epitope recognition of shrimp allergens by children than by adults suggests that shrimp sensitization decreases with age. *J Allergy Clin Immunol.* 2010;125(6):1286-1293.e3. doi:10.1016/j.jaci.2010.03.010

1086. Thalayasingam M, Gerez IF, Yap GC, et al. Clinical and immunochemical profiles of food challenge proven or anaphylactic shrimp allergy in tropical Singapore. *Clin Exp Allergy.* 2015;45(3):687-697.

1087. Teo SL, Gerez IF, Ang EY, Shek LP. Food-dependent exercise-induced anaphylaxis - a review of 5 cases. *Ann Acad Med Singapore.* 2009;38(10):905-909.

1088. Kandyil RM, Davis CM. Shellfish allergy in children. *Pediatr Allergy Immunol.* 2009;20(5):408-414. quiz 414.

1089. Fiocchi A, Restani P, Riva E. Beef allergy in children. *Nutrition.* 2000;16(6):454-457.
1090. Restani P, Fiocchi A, Beretta B, Velonà T, Giovannini M, Galli CL. Meat allergy: III-Proteins involved and cross-reactivity between different animal species. *J Am Coll Nutr.* 1997;16(4):383-389.

1091. Chandra RK, Puri S, Suraiya C, Cheema PS. Influence of maternal food antigen avoidance during pregnancy and lactation on incidence of atopic eczema in infants. *Clin Allergy.* 1986;16(6):563-569.

1092. Spitzauer S. Allergy to mammalian proteins: at the borderline between foreign and self? *Int Arch Allergy Immunol.* 1999;120(4):259-269.

1093. Posthumus J, James HR, Lane CJ, Matos LA, Platts-Mills TA, Commins SP. Initial description of pork-cat syndrome in the United States. *J Allergy Clin Immunol.* 2013;131(3):923-925.

1094. Chung CH, Mirakhur B, Chan E, et al. Cetuximab-induced anaphylaxis and IgE specific for galactose-alpha-1,3-galactose. *N Engl J Med.* 2008;358(11):1109-1117.

1095. Takahashi H, Chinuki Y, Tanaka A, Morita E. Laminin γ-1 and collagen α-1 (VI) chain are galactose-α-1,3-galactose-bound allergens in beef. *Allergy.* 2014;69(2):199-207.

1096. Fischer J, Hebsaker J, Caponetto P, Platts-Mills TA, Biedermann T. Galactose-alpha-1,3-galactose sensitization is a prerequisite for pork-kidney allergy and cofactor-related mammalian meat anaphylaxis. *J Allergy Clin Immunol.* 2014;134(3):755-759.e751.

1097. Mullins RJ, James H, Platts-Mills TA, Commins S. Relationship between red meat allergy and sensitization to gelatin and galactose-α-1,3-galactose. *J Allergy Clin Immunol.* 2012;129(5):1334-1342. e1331.

1098. Grönlund H, Adédoyin J, Commins SP, Platts-Mills TA, van Hage M. The carbohydrate galactose-alpha-1,3-galactose is a major IgE-binding epitope on cat IgA. *J Allergy Clin Immunol.* 2009;123:1189-1191.

1099. Hilger C, Fischer J, Wölbing F, Biedermann T. Role and Mechanism of Galactose-Alpha-1,3-Galactose in the Elicitation of Delayed Anaphylactic Reactions to Red Meat. *Curr Allergy Asthma Rep.* 2019;19(1):3.

1100. Platts-Mills TAECS, Biedermann T, et al. On the cause and consequences of IgE to galactose-α-1,3- galactose: A report from the National Institute of Allergy and Infectious Diseases Workshop on Understanding IgE- Mediated Mammalian Meat Allergy. *J Allergy Clin Immunol.* 2020;145(4):1061-1071. doi:10.1016/j.jaci.2020.01.047

1101. Apostolovic D, Tran TA, Starkhammar M, Sánchez-Vidaurre S, Hamsten C, van Hage M. The red meat allergy syndrome in Sweden. *Allergo J Int.* 2016;25(2):49-54.

1102. Mabelane T, Basera W, Botha M, Thomas HF, Ramjith J, Levin ME. Predictive values of alpha-gal IgE levels and alpha-gal IgE: Total IgE ratio and oral food challenge-proven meat allergy in a population with a high prevalence of reported red meat allergy. *Pediatr Allergy Immunol.* 2018;29(8):841-849.

1103. Wilson JM, Schuyler AJ, Workman L, et al. Investigation into the α-Gal Syndrome: Characteristics of 261 Children and Adults Reporting Red Meat Allergy. *J Allergy Clin Immunol Pract.* 2019;7(7):2348-2358.e2344.

1104. Kiewiet MBG, Apostolovic D, Starkhammar M, Grundström J, Hamsten C, van Hage M. Clinical and Serological Characterization of the α-Gal Syndrome-Importance of Atopy for Symptom Severity in a European Cohort. *J Allergy Clin Immunol Pract.* 2020;8(6):2027-2034.e2022.

1105. Hamsten C, Starkhammar M, Tran TA, et al. Identification of galactose-α-1,3-galactose in the gastrointestinal tract of the tick Ixodes ricinus; possible relationship with red meat allergy. *Allergy.* 2013;68(4):549-552.

1106. Fischer J, Riel S, Fehrenbacher B, et al. Spatial distribution of alpha-gal in Ixodes ricinus - A histological study. *Ticks Tick Borne Dis.* 2020;11(5):101506.

1107. Mateos-Hernández L, Villar M, Moral A, et al. Tick-host conflict: immunoglobulin E antibodies to tick proteins in patients with anaphylaxis to tick bite. *Oncotarget.* 2017;8(13):20630-20644.

1108. Apostolovic D, Mihailovic J, Commins SP, et al. Allergenomics of the tick Ixodes ricinus reveals important α-Gal-carrying IgE-binding proteins in red meat allergy. *Allergy.* 2020;75(1):217-220.

1109. Commins SP, James HR, Kelly LA, et al. The relevance of tick bites to the production of IgE antibodies to the mammalian oligosaccharide galactose-α-1,3-galactose. *J Allergy Clin Immunol.* 2011;127(5):1286-1293.e1286.

1110. Stoltz LPCL, Dowling APG, et al. Could chiggers be contributing to the prevalence of galactose- alpha-1,3-galactose sensitization and mammalian meat allergy? *J Allergy Clin Immunol Pract.* 2019;7(2):664-666. doi:10.1016/j.jaip.2018.07.014

1111. Van Nunen SA, O'Connor KS, Clarke LR, Boyle RX, Fernando SL. An association between tick bite reactions and red meat allergy in humans. *Med J Aust.* 2009;190(9):510-511.

1112. Hamsten C, Tran TAT, Starkhammar M, et al. Red meat allergy in Sweden: association with tick sensitization and B-negative blood groups. *J Allergy Clin Immunol.* 2013;132:1431-1434.

1113. Jappe U, Minge S, Kreft B, et al. Meat allergy associated with galactosyl-α-(1,3)-galactose (α-Gal)-Closing diagnostic gaps by anti-α-Gal IgE immune profiling. *Allergy.* 2018;73(1):93-105.

1114. Kiewiet MBG, Grundström J, Apostolovic D, et al. Elucidating the α-Gal syndrome at the molecular allergen level. *Allergy.* 2021;76:1576-1578.

1115. Apostolovic D, Rodrigues R, Thomas P, Starkhammar M, Hamsten C, van Hage M. Immunoprofile of α-Gal- and B-antigen-specific responses differentiates red meat-allergic patients from healthy individuals. *Allergy.* 2018;73(7):1525-1531.

1116. Wilson JM, Nguyen AT, Schuyler AJ, et al. IgE to the Mammalian Oligosaccharide Galactose-α-1,3-Galactose Is Associated With Increased Atheroma Volume and Plaques With Unstable Characteristics-Brief Report. *Arterioscler Thromb Vasc Biol.* 2018;38(7):1665-1669.

1117. Anemüller WMM, Brans R, et al. Alpha-Gal-assoziierte verzögerte Anaphylaxie gegen rotes Fleisch als Berufskrankheit [Alpha-Gal-associated delayed red meat anaphylaxis as an occupational disease]. *Hautarzt.* 2018;69(10):848-852. doi:10.1007/s00105-018-4224-4

1118. Perusko M, Apostolovic D, Kiewiet MBG, et al. Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome. *Allergy.* 2021;76(12):3766-3775.

1119. Swiontek K, Morisset M, Codreanu-Morel F, et al. Drugs of porcine origin-A risk for patients with α-gal syndrome? *J Allergy Clin Immunol Pract.* 2019;7(5):1687-1690.e1683.

1120. Hashizume H, Fujiyama T, Umayahara T, Kageyama R, Walls AF, Satoh T. Repeated Amblyomma testudinarium tick bites are associated with increased galactose-α-1,3-galactose carbohydrate IgE antibody levels: A retrospective cohort study in a single institution. *J Am Acad Dermatol.* 2018;78(6):1135-1141.e1133.

1121. Kim MS, Straesser MD, Keshavarz B, et al. IgE to galactose-α-1,3-galactose wanes over time in patients who avoid tick bites. *J Allergy Clin Immunol Pract.* 2020;8(1):364-367.e362.

1122. Bolhaar ST, van de Weg WE, van Ree R, et al. In vivo assessment with prick-to-prick testing and double-blind, placebo-controlled food challenge of allergenicity of apple cultivars. *J Allergy Clin Immunol.* 2005;116(5):1080-1086.

1123. Sancho AI, van Ree R, van Leeuwen A, et al. Measurement of lipid transfer protein in 88 apple cultivars. *Int Arch Allergy Immunol.* 2008;146(1):19-26.

1124. Sancho AIFR, Browne T, et al. Effect of postharvest storage on the expression of the apple allergen Mal d 1. *J Agric Food Chem.* 2006;54(16):5917-5923. doi:10.1021/jf060880m

1125. Bässler OY, Weiss J, Wienkoop S, et al. Evidence for novel tomato seed allergens: IgE-reactive legumin and vicilin proteins identified by multidimensional protein fractionation-mass spectrometry and in silico epitope modeling. *J Proteome Res.* 2009;8(3):1111-1122.
1090. Restani P, Fiocchi A, Beretta B, Velonà T, Giovannini M, Galli CL. Meat allergy: III-Proteins involved and cross-reactivity between different animal species. *J Am Coll Nutr.* 1997;16(4):383-389.

1091. Chandra RK, Puri S, Suraiya C, Cheema PS. Influence of maternal food antigen avoidance during pregnancy and lactation on incidence of atopic eczema in infants. *Clin Allergy.* 1986;16(6):563-569.

1092. Spitzauer S. Allergy to mammalian proteins: at the borderline between foreign and self? *Int Arch Allergy Immunol.* 1999;120(4):259-269.

1093. Posthumus J, James HR, Lane CJ, Matos LA, Platts-Mills TA, Commins SP. Initial description of pork-cat syndrome in the United States. *J Allergy Clin Immunol.* 2013;131(3):923-925.

1094. Chung CH, Mirakhur B, Chan E, et al. Cetuximab-induced anaphylaxis and IgE specific for galactose-alpha-1,3-galactose. *N Engl J Med.* 2008;358(11):1109-1117.

1095. Takahashi H, Chinuki Y, Tanaka A, Morita E. Laminin γ-1 and collagen α-1 (VI) chain are galactose-α-1,3-galactose-bound allergens in beef. *Allergy.* 2014;69(2):199-207.

1096. Fischer J, Hebsaker J, Caponetto P, Platts-Mills TA, Biedermann T. Galactose-alpha-1,3-galactose sensitization is a prerequisite for pork-kidney allergy and cofactor-related mammalian meat anaphylaxis. *J Allergy Clin Immunol.* 2014;134(3):755-759.e751.

1097. Mullins RJ, James H, Platts-Mills TA, Commins S. Relationship between red meat allergy and sensitization to gelatin and galactose-α-1,3-galactose. *J Allergy Clin Immunol.* 2012;129(5):1334-1342. e1331.

1098. Grönlund H, Adédoyin J, Commins SP, Platts-Mills TA, van Hage M. The carbohydrate galactose-alpha-1,3-galactose is a major IgE-binding epitope on cat IgA. *J Allergy Clin Immunol.* 2009;123:1189-1191.

1099. Hilger C, Fischer J, Wölbing F, Biedermann T. Role and Mechanism of Galactose-Alpha-1,3-Galactose in the Elicitation of Delayed Anaphylactic Reactions to Red Meat. *Curr Allergy Asthma Rep.* 2019;19(1):3.

1100. Platts-Mills TAECS, Biedermann T, et al. On the cause and consequences of IgE to galactose-α-1,3- galactose: A report from the National Institute of Allergy and Infectious Diseases Workshop on Understanding IgE- Mediated Mammalian Meat Allergy. *J Allergy Clin Immunol.* 2020;145(4):1061-1071. doi:10.1016/j.jaci.2020.01.047

1101. Apostolovic D, Tran TA, Starkhammar M, Sánchez-Vidaurre S, Hamsten C, van Hage M. The red meat allergy syndrome in Sweden. *Allergo J Int.* 2016;25(2):49-54.

1102. Mabelane T, Basera W, Botha M, Thomas HF, Ramjith J, Levin ME. Predictive values of alpha-gal IgE levels and alpha-gal IgE: Total IgE ratio and oral food challenge-proven meat allergy in a population with a high prevalence of reported red meat allergy. *Pediatr Allergy Immunol.* 2018;29(8):841-849.

1103. Wilson JM, Schuyler AJ, Workman L, et al. Investigation into the α-Gal Syndrome: Characteristics of 261 Children and Adults Reporting Red Meat Allergy. *J Allergy Clin Immunol Pract.* 2019;7(7):2348-2358.e2344.

1104. Kiewiet MBG, Apostolovic D, Starkhammar M, Grundström J, Hamsten C, van Hage M. Clinical and Serological Characterization of the α-Gal Syndrome-Importance of Atopy for Symptom Severity in a European Cohort. *J Allergy Clin Immunol Pract.* 2020;8(6):2027-2034.e2022.

1105. Hamsten C, Starkhammar M, Tran TA, et al. Identification of galactose-α-1,3-galactose in the gastrointestinal tract of the tick Ixodes ricinus; possible relationship with red meat allergy. *Allergy.* 2013;68(4):549-552.

1106. Fischer J, Riel S, Fehrenbacher B, et al. Spatial distribution of alpha-gal in Ixodes ricinus - A histological study. *Ticks Tick Borne Dis.* 2020;11(5):101506.

1107. Mateos-Hernández L, Villar M, Moral A, et al. Tick-host conflict: immunoglobulin E antibodies to tick proteins in patients with anaphylaxis to tick bite. *Oncotarget.* 2017;8(13):20630-20644.

1108. Apostolovic D, Mihailovic J, Commins SP, et al. Allergenomics of the tick Ixodes ricinus reveals important α-Gal-carrying IgE-binding proteins in red meat allergy. *Allergy.* 2020;75(1):217-220.

1109. Commins SP, James HR, Kelly LA, et al. The relevance of tick bites to the production of IgE antibodies to the mammalian oligosaccharide galactose-α-1,3-galactose. *J Allergy Clin Immunol.* 2011;127(5):1286-1293.e1286.

1110. Stoltz LPCL, Dowling APG, et al. Could chiggers be contributing to the prevalence of galactose- alpha-1,3-galactose sensitization and mammalian meat allergy? *J Allergy Clin Immunol Pract.* 2019;7(2):664-666. doi:10.1016/j.jaip.2018.07.014

1111. Van Nunen SA, O'Connor KS, Clarke LR, Boyle RX, Fernando SL. An association between tick bite reactions and red meat allergy in humans. *Med J Aust.* 2009;190(9):510-511.

1112. Hamsten C, Tran TAT, Starkhammar M, et al. Red meat allergy in Sweden: association with tick sensitization and B-negative blood groups. *J Allergy Clin Immunol.* 2013;132:1431-1434.

1113. Jappe U, Minge S, Kreft B, et al. Meat allergy associated with galactosyl-α-(1,3)-galactose (α-Gal)-Closing diagnostic gaps by anti-α-Gal IgE immune profiling. *Allergy.* 2018;73(1):93-105.

1114. Kiewiet MBG, Grundström J, Apostolovic D, et al. Elucidating the α-Gal syndrome at the molecular allergen level. *Allergy.* 2021;76:1576-1578.

1115. Apostolovic D, Rodrigues R, Thomas P, Starkhammar M, Hamsten C, van Hage M. Immunoprofile of α-Gal- and B-antigen-specific responses differentiates red meat-allergic patients from healthy individuals. *Allergy.* 2018;73(7):1525-1531.

1116. Wilson JM, Nguyen AT, Schuyler AJ, et al. IgE to the Mammalian Oligosaccharide Galactose-α-1,3-Galactose Is Associated With Increased Atheroma Volume and Plaques With Unstable Characteristics-Brief Report. *Arterioscler Thromb Vasc Biol.* 2018;38(7):1665-1669.

1117. Anemüller WMM, Brans R, et al. Alpha-Gal-assoziierte verzögerte Anaphylaxie gegen rotes Fleisch als Berufskrankheit [Alpha-Gal-associated delayed red meat anaphylaxis as an occupational disease]. *Hautarzt.* 2018;69(10):848-852. doi:10.1007/s00105-018-4224-4

1118. Perusko M, Apostolovic D, Kiewiet MBG, et al. Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome. *Allergy.* 2021;76(12):3766-3775.

1119. Swiontek K, Morisset M, Codreanu-Morel F, et al. Drugs of porcine origin-A risk for patients with α-gal syndrome? *J Allergy Clin Immunol Pract.* 2019;7(5):1687-1690.e1683.

1120. Hashizume H, Fujiyama T, Umayahara T, Kageyama R, Walls AF, Satoh T. Repeated Amblyomma testudinarium tick bites are associated with increased galactose-α-1,3-galactose carbohydrate IgE antibody levels: A retrospective cohort study in a single institution. *J Am Acad Dermatol.* 2018;78(6):1135-1141.e1133.

1121. Kim MS, Straesser MD, Keshavarz B, et al. IgE to galactose-α-1,3-galactose wanes over time in patients who avoid tick bites. *J Allergy Clin Immunol Pract.* 2020;8(1):364-367.e362.

1122. Bolhaar ST, van de Weg WE, van Ree R, et al. In vivo assessment with prick-to-prick testing and double-blind, placebo-controlled food challenge of allergenicity of apple cultivars. *J Allergy Clin Immunol.* 2005;116(5):1080-1086.

1123. Sancho AI, van Ree R, van Leeuwen A, et al. Measurement of lipid transfer protein in 88 apple cultivars. *Int Arch Allergy Immunol.* 2008;146(1):19-26.

1124. Sancho AIFR, Browne T, et al. Effect of postharvest storage on the expression of the apple allergen Mal d 1. *J Agric Food Chem.* 2006;54(16):5917-5923. doi:10.1021/jf060880m

1125. Bässler OY, Weiss J, Wienkoop S, et al. Evidence for novel tomato seed allergens: IgE-reactive legumin and vicilin proteins identified by multidimensional protein fractionation-mass spectrometry and in silico epitope modeling. *J Proteome Res.* 2009;8(3):1111-1122.
1126. Kschonsek J, Wiegand C, Hipler UC, Böhm V. Influence of polyphenolic content on the *in vitro* allergenicity of old and new apple cultivars: A pilot study. *Nutrition*. 2019;58:30-35.

1127. Gaier S, Marsh J, Oberhuber C, et al. Purification and structural stability of the peach allergens Pru p 1 and Pru p 3. *Mol Nutr Food Res*. 2008;52(Suppl 2):S220-S229.

1128. Bogas G, Muñoz-Cano R, Mayorga C, et al. Phenotyping peach-allergic patients sensitized to lipid transfer protein and analysing severity biomarkers. *Allergy*. 2020;75(12):3228-3236.

1129. Fernández-Rivas M, González-Mancebo E, Rodríguez-Pérez R, et al. Clinically relevant peach allergy is related to peach lipid transfer protein, Pru p 3, in the Spanish population. *J Allergy Clin Immunol*. 2003;112(4):789-795.

1130. Inomata N. Gibberellin-regulated protein allergy: Clinical features and cross-reactivity. *Allergol Int*. 2020;69(1):11-18.

1131. Karamloo F, Wangorsch A, Kasahara H, et al. Phenylcoumaran benzylic ether and isoflavonoid reductases are a new class of cross-reactive allergens in birch pollen, fruits and vegetables. *Eur J Biochem*. 2001;268(20):5310-5320.

1132. Sirvent S, Cantó B, Gómez F, et al. Detailed characterization of Act d 12 and Act d 13 from kiwi seeds: implication in IgE cross-reactivity with peanut and tree nuts. *Allergy*. 2014;69(11):1481-1488.

1133. Publin M, Mari A, Ebner C, et al. IgE sensitization profiles toward green and gold kiwifruits differ among patients allergic to kiwifruit from 3 European countries. *J Allergy Clin Immunol*. 2004;114(5):1169-1175.

1134. Le TM, Fritsche P, Publin M, et al. Differences in the allergenicity of 6 different kiwifruit cultivars analyzed by prick-to-prick testing, open food challenges, and ELISA. *J Allergy Clin Immunol*. 2011;127:677-679.

1135. Asero R, Mistrello G, Roncarolo D, et al. Detection of clinical markers of sensitization to profilin in patients allergic to plant-derived foods. *J Allergy Clin Immunol*. 2003;112(2):427-432.

1136. Sankian M, Varasteh A, Pazouki N, Mahmoudi M. Sequence homology: a poor predictive value for profilins cross-reactivity. *Clin Mol Allergy*. 2005;3:13.

1137. Cuesta-Herranz J, Pastor C, Figueredo E, et al. Identification of Cucumisin (Cuc m 1), a subtilisin-like endopeptidase, as the major allergen of melon fruit. *Clin Exp Allergy*. 2003;33(6):827-833.

1138. Asensio T, Crespo JF, Sanchez-Monge R, et al. Novel plant pathogenesis-related protein family involved in food allergy. *J Allergy Clin Immunol*. 2004;114(4):896-899.

1139. Sarkar MB, Sircar G, Ghosh N, et al. Cari p 1, a Novel Polygalacturonase Allergen From Papaya Acting as Respiratory and Food Sensitizer. *Front Plant Sci*. 2018;9:823.

1140. Bhowmik M, Biswas Sarkar M, Kanti Sarkar R, et al. Cloning and immunobiochemical analyses on recombinant chymopapain allergen Cari p 2 showing pollen-fruit cross-reaction. *Mol Immunol*. 2021;137:42-51.

1141. Publin M, Radauer C, Wilson IB, et al. Cross-reactive N-glycans of Api g 5, a high molecular weight glycoprotein allergen from celery, are required for immunoglobulin E binding and activation of effector cells from allergic patients. *FASEB J*. 2003;17(12):1697-1699.

1142. Gadermaier G, Hauser M, Egger M, et al. Sensitization prevalence, antibody cross-reactivity and immunogenic peptide profile of Api g 2, the non-specific lipid transfer protein 1 of celery. *PLoS One*. 2011;6(8):e24150.

1143. Vejvar E, Himly M, Briza P, et al. Allergenic relevance of non-specific lipid transfer proteins 2: Identification and characterization of Api g 6 from celery tuber as representative of a novel IgE-binding protein family. *Mol Nutr Food Res*. 2013;57(11):2061-2070.

1144. Wangorsch A, Lidholm J, Mattsson LA, et al. Identification of a defensin as novel allergen in celery root: Api g 7 as a missing link in the diagnosis of celery allergy? *Allergy*. 2022;77(4):1294-1296.

1145. Zuidmeer L, Goldhahn K, Rona RJ, et al. The prevalence of plant food allergies: a systematic review. *J Allergy Clin Immunol*. 2008;121(5):1210-1218.e1214.

1146. Burney PG, Potts J, Kummeling I, et al. The prevalence and distribution of food sensitization in European adults. *Allergy*. 2014;69(3):365-371.

1147. Boyano-Martínez T, Pedrosa M, Belver T, Quirce S, García-Ara C. Peach allergy in Spanish children: tolerance to the pulp and molecular sensitization profile. *Pediatr Allergy Immunol*. 2013;24(2):168-172.

1148. Pastorello EA, Farioli L, Stafylaraki C, et al. Anti-rPru p 3 IgE levels are inversely related to the age at onset of peach-induced severe symptoms reported by peach-allergic adults. *Int Arch Allergy Immunol*. 2013;162(1):45-49.

1149. Le TM, Publin M, Breiteneder H, et al. Kiwifruit allergy across Europe: clinical manifestation and IgE recognition patterns to kiwifruit allergens. *J Allergy Clin Immunol*. 2013;131(1):164-171.

1150. Publin M, Pfister M, Radauer C, et al. Component-resolved diagnosis of kiwifruit allergy with purified natural and recombinant kiwifruit allergens. *J Allergy Clin Immunol*. 2010;125(3):687-694. 694. e681.

1151. Burney P, Summers C, Chinn S, Hooper R, van Ree R, Lidholm J. Prevalence and distribution of sensitization to foods in the European Community Respiratory Health Survey: a EuroPrevall analysis. *Allergy*. 2010;65(9):1182-1188.

1152. Bauermeister K, Ballmer-Weber BK, Publin M, et al. Assessment of component-resolved *in vitro* diagnosis of celeriac allergy. *J Allergy Clin Immunol*. 2009;124(6):1273-1281.e1272.

1153. Ballmer-Weber BK, Skamstrup Hansen K, Sastre J, et al. Component-resolved *in vitro* diagnosis of carrot allergy in three different regions of Europe. *Allergy*. 2012;67(6):758-766.

1154. Ballmer-Weber BK, Hoffmann-Sommergruber K. Molecular diagnosis of fruit and vegetable allergy. *Curr Opin Allergy Clin Immunol*. 2011;11(3):229-235.

1155. Vera-Berrios RN, Freund-Serpa NP, Fernández-Rivas M. Medical algorithm: Diagnosis of plant food allergy. *Allergy*. 2022;77(2):698-704.

1156. Ballmer-Weber BK, Scheurer S, Fritsche P, et al. Component-resolved diagnosis with recombinant allergens in patients with cherry allergy. *J Allergy Clin Immunol*. 2002;110(1):167-173.

1157. Ehrenberg AE, Klingebiel C, Östling J, et al. Characterization of a 7 kDa pollen allergen belonging to the gibberellin-regulated protein family from three Cupressaceae species. *Clin Exp Allergy*. 2020;50(8):964-972.

1158. Lidholm J, Ballmer-Weber BK, Mari A, Vieths S. Component-resolved diagnostics in food allergy. *Curr Opin Allergy Clin Immunol*. 2006;6(3):234-240.

1159. González-Mancebo E, González-de-Olano D, Trujillo MJ, et al. Prevalence of sensitization to lipid transfer proteins and profilins in a population of 430 patients in the south of Madrid. *J Investig Allergol Clin Immunol*. 2011;21(4):278-282.

1160. Le TM, van Hoffen E, Lebens AF, Bruijnzeel-Koomen CA, Knulst AC. Anaphylactic versus mild reactions to hazelnut and apple in a birch-endemic area: different sensitization profiles? *Int Arch Allergy Immunol*. 2013;160(1):56-62.

1161. Schulten V, Lauer I, Scheurer S, Thalhammer T, Bohle B. A food matrix reduces digestion and absorption of food allergens *in vivo*. *Mol Nutr Food Res*. 2011;55(10):1484-1491.

1162. Romano A, Scala E, Rumi G, et al. Lipid transfer proteins: the most frequent sensitizer in Italian subjects with food-dependent exercise-induced anaphylaxis. *Clin Exp Allergy*. 2012;42(11):1643-1653.

1163. Oberhuber C, Bulley SM, Ballmer-Weber BK, et al. Characterization of Bet v 1-related allergens from kiwifruit relevant for patients with combined kiwifruit and birch pollen allergy. *Mol Nutr Food Res*. 2008;52(Suppl 2):S230-S240.
1126. Kschonsek J, Wiegand C, Hipler UC, Böhm V. Influence of polyphenolic content on the *in vitro* allergenicity of old and new apple cultivars: A pilot study. *Nutrition*. 2019;58:30-35.

1127. Gaier S, Marsh J, Oberhuber C, et al. Purification and structural stability of the peach allergens Pru p 1 and Pru p 3. *Mol Nutr Food Res*. 2008;52(Suppl 2):S220-S229.

1128. Bogas G, Muñoz-Cano R, Mayorga C, et al. Phenotyping peach-allergic patients sensitized to lipid transfer protein and analysing severity biomarkers. *Allergy*. 2020;75(12):3228-3236.

1129. Fernández-Rivas M, González-Mancebo E, Rodríguez-Pérez R, et al. Clinically relevant peach allergy is related to peach lipid transfer protein, Pru p 3, in the Spanish population. *J Allergy Clin Immunol*. 2003;112(4):789-795.

1130. Inomata N. Gibberellin-regulated protein allergy: Clinical features and cross-reactivity. *Allergol Int*. 2020;69(1):11-18.

1131. Karamloo F, Wangorsch A, Kasahara H, et al. Phenylcoumaran benzylic ether and isoflavonoid reductases are a new class of cross-reactive allergens in birch pollen, fruits and vegetables. *Eur J Biochem*. 2001;268(20):5310-5320.

1132. Sirvent S, Cantó B, Gómez F, et al. Detailed characterization of Act d 12 and Act d 13 from kiwi seeds: implication in IgE cross-reactivity with peanut and tree nuts. *Allergy*. 2014;69(11):1481-1488.

1133. Publin M, Mari A, Ebner C, et al. IgE sensitization profiles toward green and gold kiwifruits differ among patients allergic to kiwifruit from 3 European countries. *J Allergy Clin Immunol*. 2004;114(5):1169-1175.

1134. Le TM, Fritsche P, Publin M, et al. Differences in the allergenicity of 6 different kiwifruit cultivars analyzed by prick-to-prick testing, open food challenges, and ELISA. *J Allergy Clin Immunol*. 2011;127:677-679.

1135. Asero R, Mistrello G, Roncarolo D, et al. Detection of clinical markers of sensitization to profilin in patients allergic to plant-derived foods. *J Allergy Clin Immunol*. 2003;112(2):427-432.

1136. Sankian M, Varasteh A, Pazouki N, Mahmoudi M. Sequence homology: a poor predictive value for profilins cross-reactivity. *Clin Mol Allergy*. 2005;3:13.

1137. Cuesta-Herranz J, Pastor C, Figueredo E, et al. Identification of Cucumisin (Cuc m 1), a subtilisin-like endopeptidase, as the major allergen of melon fruit. *Clin Exp Allergy*. 2003;33(6):827-833.

1138. Asensio T, Crespo JF, Sanchez-Monge R, et al. Novel plant pathogenesis-related protein family involved in food allergy. *J Allergy Clin Immunol*. 2004;114(4):896-899.

1139. Sarkar MB, Sircar G, Ghosh N, et al. Cari p 1, a Novel Polygalacturonase Allergen From Papaya Acting as Respiratory and Food Sensitizer. *Front Plant Sci*. 2018;9:823.

1140. Bhowmik M, Biswas Sarkar M, Kanti Sarkar R, et al. Cloning and immunobiochemical analyses on recombinant chymopapain allergen Cari p 2 showing pollen-fruit cross-reaction. *Mol Immunol*. 2021;137:42-51.

1141. Publin M, Radauer C, Wilson IB, et al. Cross-reactive N-glycans of Api g 5, a high molecular weight glycoprotein allergen from celery, are required for immunoglobulin E binding and activation of effector cells from allergic patients. *FASEB J*. 2003;17(12):1697-1699.

1142. Gadermaier G, Hauser M, Egger M, et al. Sensitization prevalence, antibody cross-reactivity and immunogenic peptide profile of Api g 2, the non-specific lipid transfer protein 1 of celery. *PLoS One*. 2011;6(8):e24150.

1143. Vejvar E, Himly M, Briza P, et al. Allergenic relevance of non-specific lipid transfer proteins 2: Identification and characterization of Api g 6 from celery tuber as representative of a novel IgE-binding protein family. *Mol Nutr Food Res*. 2013;57(11):2061-2070.

1144. Wangorsch A, Lidholm J, Mattsson LA, et al. Identification of a defensin as novel allergen in celery root: Api g 7 as a missing link in the diagnosis of celery allergy? *Allergy*. 2022;77(4):1294-1296.

1145. Zuidmeer L, Goldhahn K, Rona RJ, et al. The prevalence of plant food allergies: a systematic review. *J Allergy Clin Immunol*. 2008;121(5):1210-1218.e1214.

1146. Burney PG, Potts J, Kummeling I, et al. The prevalence and distribution of food sensitization in European adults. *Allergy*. 2014;69(3):365-371.

1147. Boyano-Martínez T, Pedrosa M, Belver T, Quirce S, García-Ara C. Peach allergy in Spanish children: tolerance to the pulp and molecular sensitization profile. *Pediatr Allergy Immunol*. 2013;24(2):168-172.

1148. Pastorello EA, Farioli L, Stafylaraki C, et al. Anti-rPru p 3 IgE levels are inversely related to the age at onset of peach-induced severe symptoms reported by peach-allergic adults. *Int Arch Allergy Immunol*. 2013;162(1):45-49.

1149. Le TM, Publin M, Breiteneder H, et al. Kiwifruit allergy across Europe: clinical manifestation and IgE recognition patterns to kiwifruit allergens. *J Allergy Clin Immunol*. 2013;131(1):164-171.

1150. Publin M, Pfister M, Radauer C, et al. Component-resolved diagnosis of kiwifruit allergy with purified natural and recombinant kiwifruit allergens. *J Allergy Clin Immunol*. 2010;125(3):687-694. 694. e681.

1151. Burney P, Summers C, Chinn S, Hooper R, van Ree R, Lidholm J. Prevalence and distribution of sensitization to foods in the European Community Respiratory Health Survey: a EuroPrevall analysis. *Allergy*. 2010;65(9):1182-1188.

1152. Bauermeister K, Ballmer-Weber BK, Publin M, et al. Assessment of component-resolved *in vitro* diagnosis of celeriac allergy. *J Allergy Clin Immunol*. 2009;124(6):1273-1281.e1272.

1153. Ballmer-Weber BK, Skamstrup Hansen K, Sastre J, et al. Component-resolved *in vitro* diagnosis of carrot allergy in three different regions of Europe. *Allergy*. 2012;67(6):758-766.

1154. Ballmer-Weber BK, Hoffmann-Sommergruber K. Molecular diagnosis of fruit and vegetable allergy. *Curr Opin Allergy Clin Immunol*. 2011;11(3):229-235.

1155. Vera-Berrios RN, Freund-Serpa NP, Fernández-Rivas M. Medical algorithm: Diagnosis of plant food allergy. *Allergy*. 2022;77(2):698-704.

1156. Ballmer-Weber BK, Scheurer S, Fritsche P, et al. Component-resolved diagnosis with recombinant allergens in patients with cherry allergy. *J Allergy Clin Immunol*. 2002;110(1):167-173.

1157. Ehrenberg AE, Klingebiel C, Östling J, et al. Characterization of a 7 kDa pollen allergen belonging to the gibberellin-regulated protein family from three Cupressaceae species. *Clin Exp Allergy*. 2020;50(8):964-972.

1158. Lidholm J, Ballmer-Weber BK, Mari A, Vieths S. Component-resolved diagnostics in food allergy. *Curr Opin Allergy Clin Immunol*. 2006;6(3):234-240.

1159. González-Mancebo E, González-de-Olano D, Trujillo MJ, et al. Prevalence of sensitization to lipid transfer proteins and profilins in a population of 430 patients in the south of Madrid. *J Investig Allergol Clin Immunol*. 2011;21(4):278-282.

1160. Le TM, van Hoffen E, Lebens AF, Bruijnzeel-Koomen CA, Knulst AC. Anaphylactic versus mild reactions to hazelnut and apple in a birch-endemic area: different sensitization profiles? *Int Arch Allergy Immunol*. 2013;160(1):56-62.

1161. Schulten V, Lauer I, Scheurer S, Thalhammer T, Bohle B. A food matrix reduces digestion and absorption of food allergens *in vivo*. *Mol Nutr Food Res*. 2011;55(10):1484-1491.

1162. Romano A, Scala E, Rumi G, et al. Lipid transfer proteins: the most frequent sensitizer in Italian subjects with food-dependent exercise-induced anaphylaxis. *Clin Exp Allergy*. 2012;42(11):1643-1653.

1163. Oberhuber C, Bulley SM, Ballmer-Weber BK, et al. Characterization of Bet v 1-related allergens from kiwifruit relevant for patients with combined kiwifruit and birch pollen allergy. *Mol Nutr Food Res*. 2008;52(Suppl 2):S230-S240.
1164. Palacin A, Rodriguez J, Blanco C, et al. Immunoglobulin E recognition patterns to purified Kiwifruit (Actinidinia deliciosa) allergens in patients sensitized to Kiwi with different clinical symptoms. *Clin Exp Allergy*. 2008;38(7):1220-1228.

1165. Ballmer-Weber BK, Vieths S, Lütkopf D, Heuschmann P, Wüthrich B. Celery allergy confirmed by double-blind, placebo-controlled food challenge: a clinical study in 32 subjects with a history of adverse reactions to celery root. *J Allergy Clin Immunol*. 2000;106(2):373-378.

1166. Ballmer-Weber BK, Hoffmann A, Wüthrich B, et al. Influence of food processing on the allergenicity of celery: DBPCFC with celery spice and cooked celery in patients with celery allergy. *Allergy*. 2002;57(3):228-235.

1167. Brehler R, Theissen U, Mohr C, Luger T. "Latex-fruit syndrome": frequency of cross-reacting IgE antibodies. *Allergy*. 1997;52(4):404-410.

1168. García Ortiz JC, Moyano JC, Alvarez M, Bellido J. Latex allergy in fruit-allergic patients. *Allergy*. 1998;53(5):532-536.

1169. Radauer C, Adhami F, Fürtler I, et al. Latex-allergic patients sensitized to the major allergen hevein and hevein-like domains of class I chitinases show no increased frequency of latex-associated plant food allergy. *Mol Immunol*. 2011;48(4):600-609.

1170. Decuyper II, Van Gasse AL, Faber MA, et al. Exploring the Diagnosis and Profile of Cannabis Allergy. *J Allergy Clin Immunol Pract*. 2019;7(3):983-989.e985.

1171. Alkhammash S, Tsui H, Thomson DMP. Cannabis and hemp seed allergy. *J Allergy Clin Immunol Pract*. 2019;7(7):2429-2430.e2421.

1172. Decuyper II, Armentia A, Martín-Armentia B, Almuzara AC, Ebo DG, Brucker HA. Adverse Reactions to Illicit Drugs (Marijuana, Opioids, Cocaine) and Alcohol. *J Allergy Clin Immunol Pract*. 2021;9(8):3006-3014.

1173. Decuyper II, Green BJ, Sussman GL, et al. Occupational Allergies to Cannabis. *J Allergy Clin Immunol Pract*. 2020;8(10):3331-3338.

1174. Gamboa P, Sanchez-Monge R, Sanz ML, Palacín A, Salcedo G, Diaz-Perales A. Sensitization to *Cannabis sativa* caused by a novel allergenic lipid transfer protein, Can s 3. *J Allergy Clin Immunol*. 2007;120:1459-1460.

1175. Ebo DG, Decuyper II, Rihs HP, et al. IgE-binding and mast cell-activating capacity of the homologue of the major birch pollen allergen and profilin from Cannabis sativa. *J Allergy Clin Immunol Pract*. 2021;9(6):2509-2512.e2503.

1176. Decuyper II, Rihs HP, Mertens CH, et al. A new cannabis allergen in Northwestern Europe: The oxygen-evolving enhancer protein 2 (OEEP2). *J Allergy Clin Immunol Pract*. 2020;8(7):2421-2424.e2422.

1177. Bolhaar ST, Tiemessen MM, Zuidmeer L, et al. Efficacy of birch-pollen immunotherapy on cross-reactive food allergy confirmed by skin tests and double-blind food challenges. *Clin Exp Allergy*. 2004;34(5):761-769.

1178. Hansen KS, Khinchi MS, Skov PS, Bindslev-Jensen C, Poulsen LK, Malling HJ. Food allergy to apple and specific immunotherapy with birch pollen. *Mol Nutr Food Res*. 2004;48(6):441-448.

1179. Gevaert P, De Craemer J, De Ruyck N, et al. Novel antibody cocktail targeting Bet v 1 rapidly and sustainably treats birch allergy symptoms in a phase 1 study. *J Allergy Clin Immunol*. 2022;149(1):189-199.

1180. Kopac P, Rudin M, Gentinetta T, et al. Continuous apple consumption induces oral tolerance in birch-pollen-associated apple allergy. *Allergy*. 2012;67(2):280-285.

1181. Gomez F, Bogas G, Gonzalez M, et al. The clinical and immunological effects of Pru p 3 sublingual immunotherapy on peach and peanut allergy in patients with systemic reactions. *Clin Exp Allergy*. 2017;47(3):339-350.

1182. Sapone A, Bai JC, Ciacci C, et al. Spectrum of gluten-related disorders: consensus on new nomenclature and classification. *BMC Med*. 2012;10:13.

1183. Longo G, Berti I, Burks AW, Krauss B, Barbi E. IgE-mediated food allergy in children. *Lancet*. 2013;382(9905):1656-1664.

1184. Ostblom E, Lilja G, Pershagen G, van Hage M, Wickman M. Phenotypes of food hypersensitivity and development of allergic diseases during the first 8 years of life. *Clin Exp Allergy*. 2008;38(8):1325-1332.

1185. Constantin C, Quirce S, Poorafshar M, et al. Micro-arrayed wheat seed and grass pollen allergens for component-resolved diagnosis. *Allergy*. 2009;64(7):1030-1037.

1186. Mäkelä MJ, Eriksson C, Kotaniemi-Syrjänen A, et al. Wheat allergy in children - new tools for diagnostics. *Clin Exp Allergy*. 2014;44(11):1420-1430.

1187. Venter C, Pereira B, Grundy J, Clayton CB, Arshad SH, Dean T. Prevalence of sensitization reported and objectively assessed food hypersensitivity amongst six-year-old children: a population-based study. *Pediatr Allergy Immunol*. 2006;17(5):356-363.

1188. Burman J, Palosuo K, Kukkonen K, Pelkonen A, Mäkelä MJ. Children with wheat allergy usually tolerate oats. *Pediatr Allergy Immunol*. 2019;30(8):855-857.

1189. Palosuo K, Alenius H, Varjonen E, Kalkkinen N, Reunala T. Rye gamma-70 and gamma-35 secalins and barley gamma-3 hordein cross-react with omega-5 gliadin, a major allergen in wheat-dependent, exercise-induced anaphylaxis. *Clin Exp Allergy*. 2001;31(3):466-473.

1190. Pahr S, Constantin C, Papadopoulos NG, et al. α-Purothionin, a new wheat allergen associated with severe allergy. *J Allergy Clin Immunol*. 2013;132(4):1000-1003.e1001-1004.

1191. Sander I, Rihs HP, Doekes G, et al. Component-resolved diagnosis of baker's allergy based on specific IgE to recombinant wheat flour proteins. *J Allergy Clin Immunol*. 2015;135(6):1529-1537.

1192. Palosuo K, Varjonen E, Kekki OM, et al. Wheat omega-5 gliadin is a major allergen in children with immediate allergy to ingested wheat. *J Allergy Clin Immunol*. 2001;108(4):634-638.

1193. Ito K, Futamura M, Borres MP, et al. IgE antibodies to omega-5 gliadin associate with immediate symptoms on oral wheat challenge in Japanese children. *Allergy*. 2008;63(11):1536-1542.

1194. Nilsson N, Sjölander S, Baar A, et al. Wheat allergy in children evaluated with challenge and IgE antibodies to wheat components. *Pediatr Allergy Immunol*. 2015;26(2):119-125.

1195. Palacin A, Quirce S, Armentia A, et al. Wheat lipid transfer protein is a major allergen associated with baker's asthma. *J Allergy Clin Immunol*. 2007;120(5):1132-1138.

1196. Pastorello EA, Farioli L, Conti A, et al. Wheat IgE-mediated food allergy in European patients: alpha-amylase inhibitors, lipid transfer proteins and low-molecular-weight glutenins. Allergenic molecules recognized by double-blind, placebo-controlled food challenge. *Int Arch Allergy Immunol*. 2007;144(1):10-22.

1197. Scibilia J, Pastorello EA, Zisa G, et al. Wheat allergy: a double-blind, placebo-controlled study in adults. *J Allergy Clin Immunol*. 2006;117(2):433-439.

1198. Brockow K, Kneissl D, Valentini L, et al. Using a gluten oral food challenge protocol to improve diagnosis of wheat-dependent exercise-induced anaphylaxis. *J Allergy Clin Immunol*. 2015;135(4):977-984.e974.

1199. Tomsitz D, Biedermann T, Brockow K. Sublingual immunotherapy reduces reaction threshold in three patients with wheat-dependent exercise-induced anaphylaxis. *Allergy*. 2021;76(12):3804-3806.

1200. Kotaniemi-Syrjänen A, Palosuo K, Jartti T, Kuitunen M, Pelkonen AS, Mäkelä MJ. The prognosis of wheat hypersensitivity in children. *Pediatr Allergy Immunol*. 2010;21(2 Pt 2):e421-e428.

1201. Koike Y, Yanagida N, Sato S, et al. Predictors of Persistent Wheat Allergy in Children: A Retrospective Cohort Study. *Int Arch Allergy Immunol*. 2018;176(3-4):249-254.

1202. Giménez-Bastida JA, Zieliński H. Buckwheat as a Functional Food and Its Effects on Health. *J Agric Food Chem*. 2015;63(36):7896-7913.

1203. Heffler E, Nebiolo F, Asero R, et al. Clinical manifestations, sensitizations, and immunoblotting profiles of buckwheat-allergic patients. *Allergy*. 2011;66(2):264-270.
1164. Palacin A, Rodriguez J, Blanco C, et al. Immunoglobulin E recognition patterns to purified Kiwifruit (Actinidinia deliciosa) allergens in patients sensitized to Kiwi with different clinical symptoms. *Clin Exp Allergy*. 2008;38(7):1220-1228.

1165. Ballmer-Weber BK, Vieths S, Lütkopf D, Heuschmann P, Wüthrich B. Celery allergy confirmed by double-blind, placebo-controlled food challenge: a clinical study in 32 subjects with a history of adverse reactions to celery root. *J Allergy Clin Immunol*. 2000;106(2):373-378.

1166. Ballmer-Weber BK, Hoffmann A, Wüthrich B, et al. Influence of food processing on the allergenicity of celery: DBPCFC with celery spice and cooked celery in patients with celery allergy. *Allergy*. 2002;57(3):228-235.

1167. Brehler R, Theissen U, Mohr C, Luger T. "Latex-fruit syndrome": frequency of cross-reacting IgE antibodies. *Allergy*. 1997;52(4):404-410.

1168. García Ortiz JC, Moyano JC, Alvarez M, Bellido J. Latex allergy in fruit-allergic patients. *Allergy*. 1998;53(5):532-536.

1169. Radauer C, Adhami F, Fürtler I, et al. Latex-allergic patients sensitized to the major allergen hevein and hevein-like domains of class I chitinases show no increased frequency of latex-associated plant food allergy. *Mol Immunol*. 2011;48(4):600-609.

1170. Decuyper II, Van Gasse AL, Faber MA, et al. Exploring the Diagnosis and Profile of Cannabis Allergy. *J Allergy Clin Immunol Pract*. 2019;7(3):983-989.e985.

1171. Alkhammash S, Tsui H, Thomson DMP. Cannabis and hemp seed allergy. *J Allergy Clin Immunol Pract*. 2019;7(7):2429-2430.e2421.

1172. Decuyper II, Armentia A, Martín-Armentia B, Almuzara AC, Ebo DG, Brucker HA. Adverse Reactions to Illicit Drugs (Marijuana, Opioids, Cocaine) and Alcohol. *J Allergy Clin Immunol Pract*. 2021;9(8):3006-3014.

1173. Decuyper II, Green BJ, Sussman GL, et al. Occupational Allergies to Cannabis. *J Allergy Clin Immunol Pract*. 2020;8(10):3331-3338.

1174. Gamboa P, Sanchez-Monge R, Sanz ML, Palacín A, Salcedo G, Diaz-Perales A. Sensitization to *Cannabis sativa* caused by a novel allergenic lipid transfer protein, Can s 3. *J Allergy Clin Immunol*. 2007;120:1459-1460.

1175. Ebo DG, Decuyper II, Rihs HP, et al. IgE-binding and mast cell-activating capacity of the homologue of the major birch pollen allergen and profilin from Cannabis sativa. *J Allergy Clin Immunol Pract*. 2021;9(6):2509-2512.e2503.

1176. Decuyper II, Rihs HP, Mertens CH, et al. A new cannabis allergen in Northwestern Europe: The oxygen-evolving enhancer protein 2 (OEEP2). *J Allergy Clin Immunol Pract*. 2020;8(7):2421-2424.e2422.

1177. Bolhaar ST, Tiemessen MM, Zuidmeer L, et al. Efficacy of birch-pollen immunotherapy on cross-reactive food allergy confirmed by skin tests and double-blind food challenges. *Clin Exp Allergy*. 2004;34(5):761-769.

1178. Hansen KS, Khinchi MS, Skov PS, Bindslev-Jensen C, Poulsen LK, Malling HJ. Food allergy to apple and specific immunotherapy with birch pollen. *Mol Nutr Food Res*. 2004;48(6):441-448.

1179. Gevaert P, De Craemer J, De Ruyck N, et al. Novel antibody cocktail targeting Bet v 1 rapidly and sustainably treats birch allergy symptoms in a phase 1 study. *J Allergy Clin Immunol*. 2022;149(1):189-199.

1180. Kopac P, Rudin M, Gentinetta T, et al. Continuous apple consumption induces oral tolerance in birch-pollen-associated apple allergy. *Allergy*. 2012;67(2):280-285.

1181. Gomez F, Bogas G, Gonzalez M, et al. The clinical and immunological effects of Pru p 3 sublingual immunotherapy on peach and peanut allergy in patients with systemic reactions. *Clin Exp Allergy*. 2017;47(3):339-350.

1182. Sapone A, Bai JC, Ciacci C, et al. Spectrum of gluten-related disorders: consensus on new nomenclature and classification. *BMC Med*. 2012;10:13.

1183. Longo G, Berti I, Burks AW, Krauss B, Barbi E. IgE-mediated food allergy in children. *Lancet*. 2013;382(9905):1656-1664.

1184. Ostblom E, Lilja G, Pershagen G, van Hage M, Wickman M. Phenotypes of food hypersensitivity and development of allergic diseases during the first 8 years of life. *Clin Exp Allergy*. 2008;38(8):1325-1332.

1185. Constantin C, Quirce S, Poorafshar M, et al. Micro-arrayed wheat seed and grass pollen allergens for component-resolved diagnosis. *Allergy*. 2009;64(7):1030-1037.

1186. Mäkelä MJ, Eriksson C, Kotaniemi-Syrjänen A, et al. Wheat allergy in children - new tools for diagnostics. *Clin Exp Allergy*. 2014;44(11):1420-1430.

1187. Venter C, Pereira B, Grundy J, Clayton CB, Arshad SH, Dean T. Prevalence of sensitization reported and objectively assessed food hypersensitivity amongst six-year-old children: a population-based study. *Pediatr Allergy Immunol*. 2006;17(5):356-363.

1188. Burman J, Palosuo K, Kukkonen K, Pelkonen A, Mäkelä MJ. Children with wheat allergy usually tolerate oats. *Pediatr Allergy Immunol*. 2019;30(8):855-857.

1189. Palosuo K, Alenius H, Varjonen E, Kalkkinen N, Reunala T. Rye gamma-70 and gamma-35 secalins and barley gamma-3 hordein cross-react with omega-5 gliadin, a major allergen in wheat-dependent, exercise-induced anaphylaxis. *Clin Exp Allergy*. 2001;31(3):466-473.

1190. Pahr S, Constantin C, Papadopoulos NG, et al. α-Purothionin, a new wheat allergen associated with severe allergy. *J Allergy Clin Immunol*. 2013;132(4):1000-1003.e1001-1004.

1191. Sander I, Rihs HP, Doekes G, et al. Component-resolved diagnosis of baker's allergy based on specific IgE to recombinant wheat flour proteins. *J Allergy Clin Immunol*. 2015;135(6):1529-1537.

1192. Palosuo K, Varjonen E, Kekki OM, et al. Wheat omega-5 gliadin is a major allergen in children with immediate allergy to ingested wheat. *J Allergy Clin Immunol*. 2001;108(4):634-638.

1193. Ito K, Futamura M, Borres MP, et al. IgE antibodies to omega-5 gliadin associate with immediate symptoms on oral wheat challenge in Japanese children. *Allergy*. 2008;63(11):1536-1542.

1194. Nilsson N, Sjölander S, Baar A, et al. Wheat allergy in children evaluated with challenge and IgE antibodies to wheat components. *Pediatr Allergy Immunol*. 2015;26(2):119-125.

1195. Palacin A, Quirce S, Armentia A, et al. Wheat lipid transfer protein is a major allergen associated with baker's asthma. *J Allergy Clin Immunol*. 2007;120(5):1132-1138.

1196. Pastorello EA, Farioli L, Conti A, et al. Wheat IgE-mediated food allergy in European patients: alpha-amylase inhibitors, lipid transfer proteins and low-molecular-weight glutenins. Allergenic molecules recognized by double-blind, placebo-controlled food challenge. *Int Arch Allergy Immunol*. 2007;144(1):10-22.

1197. Scibilia J, Pastorello EA, Zisa G, et al. Wheat allergy: a double-blind, placebo-controlled study in adults. *J Allergy Clin Immunol*. 2006;117(2):433-439.

1198. Brockow K, Kneissl D, Valentini L, et al. Using a gluten oral food challenge protocol to improve diagnosis of wheat-dependent exercise-induced anaphylaxis. *J Allergy Clin Immunol*. 2015;135(4):977-984.e974.

1199. Tomsitz D, Biedermann T, Brockow K. Sublingual immunotherapy reduces reaction threshold in three patients with wheat-dependent exercise-induced anaphylaxis. *Allergy*. 2021;76(12):3804-3806.

1200. Kotaniemi-Syrjänen A, Palosuo K, Jartti T, Kuitunen M, Pelkonen AS, Mäkelä MJ. The prognosis of wheat hypersensitivity in children. *Pediatr Allergy Immunol*. 2010;21(2 Pt 2):e421-e428.

1201. Koike Y, Yanagida N, Sato S, et al. Predictors of Persistent Wheat Allergy in Children: A Retrospective Cohort Study. *Int Arch Allergy Immunol*. 2018;176(3-4):249-254.

1202. Giménez-Bastida JA, Zieliński H. Buckwheat as a Functional Food and Its Effects on Health. *J Agric Food Chem*. 2015;63(36):7896-7913.

1203. Heffler E, Nebiolo F, Asero R, et al. Clinical manifestations, sensitizations, and immunoblotting profiles of buckwheat-allergic patients. *Allergy*. 2011;66(2):264-270.
1204. Norbäck D, Wieslander G. A Review on Epidemiological and Clinical Studies on Buckwheat Allergy. *Plants* (Basel). 2021;10(3).

1205. Jungewelter S, Airaksinen L, Pesonen M. Occupational buckwheat allergy as a cause of allergic rhinitis, asthma, contact urticaria and anaphylaxis-An emerging problem in food-handling occupations? *Am J Ind Med*. 2020;63(11):1047-1053.

1206. Breiteneder H, Radauer C. A classification of plant food allergens. *J Allergy Clin Immunol*. 2004;113(5):821-830. quiz 831.

1207. Maruyama N, Sato S, Yanagida N, et al. Clinical utility of recombinant allergen components in diagnosing buckwheat allergy. *J Allergy Clin Immunol Pract*. 2016;4(2):322-323.e323.

1208. Imamura T, Kanagawa Y, Ebisawa M. A survey of patients with self-reported severe food allergies in Japan. *Pediatr Allergy Immunol*. 2008;19(3):270-274.

1209. Yanagida N, Sato S, Takahashi K, et al. Reactions of Buckwheat-Hypersensitive Patients during Oral Food Challenge Are Rare, but Often Anaphylactic. *Int Arch Allergy Immunol*. 2017;172(2):116-122.

1210. Badiu I, Olivieri E, Montagni M, et al. Italian study on buckwheat allergy: prevalence and clinical features of buckwheat-sensitized patients in Italy. *Int J Immunopathol Pharmacol*. 2013;26:801-806.

1211. Urisu AKY, Morita Y, et al. Identification of a major allergen of buckwheat seeds by immunoblotting methods. *Allergy Clin Immunol News*. 1994;6:151-155. doi:10.1034/j.1398-9995.2000.00763.x

1212. Geiselhart S, Nagl C, Dubiela P, et al. Concomitant sensitization to legumin, Fag e 2 and Fag e 5 predicts buckwheat allergy. *Clin Exp Allergy*. 2018;48(2):217-224.

1213. Tanaka K, Matsumoto K, Akasawa A, et al. Pepsin-resistant 16-kD buckwheat protein is associated with immediate hypersensitivity reaction in patients with buckwheat allergy. *Int Arch Allergy Immunol*. 2002;129(1):49-56.

1214. Tohgi K, Kohno K, Takahashi H, Matsuo H, Nakayama S, Morita E. Usability of Fag e 2 ImmunoCAP in the diagnosis of buckwheat allergy. *Arch Dermatol Res*. 2011;303(9):635-642.

1215. Fok JS, Kette F, Smith WB, et al. Buckwheat allergy in Australia. *Intern Med J*. 2019;49(12):1552-1553.

1216. L'Hocine L, Boye JI. Allergenicity of soybean: new developments in identification of allergenic proteins, cross-reactivities and hypoallergenization technologies. *Crit Rev Food Sci Nutr*. 2007;47(2):127-143.

1217. Besler M, Helm RM, Ogawa T. Allergen data collection - update: soybean (*Glycine max*). *Int Symp Food Allerg*. 2000;2:1-35.

1218. Mittag D, Vieths S, Vogel L, et al. Soybean allergy in patients allergic to birch pollen: clinical investigation and molecular characterization of allergens. *J Allergy Clin Immunol*. 2004;113(1):148-154.

1219. Ballmer-Weber BK, Vieths S. Soy allergy in perspective. *Curr Opin Allergy Clin Immunol*. 2008;8(3):270-275.

1220. Katz Y, Gutierrez-Castrellon P, Gonzalez MG, Rivas R, Lee BW, Alarcon P. A comprehensive review of sensitization and allergy to soy-based products. *Clin Rev Allergy Immunol*. 2014;46(3):272-281.

1221. Sato M, Shukuya A, Sato S, et al. Oral challenge tests for soybean allergies in Japan: A summary of 142 cases. *Allergol Int*. 2016;65(1):68-73.

1222. Kleine-Tebbe J, Vogel L, Crowell DN, Haustein UF, Vieths S. Severe oral allergy syndrome and anaphylactic reactions caused by a Bet v 1- related PR-10 protein in soybean, SAM22. *J Allergy Clin Immunol*. 2002;110(5):797-804.

1223. Ballmer-Weber BK, Holzhauser T, Scibilia J, et al. Clinical characteristics of soybean allergy in Europe: a double-blind, placebo-controlled food challenge study. *J Allergy Clin Immunol*. 2007;119(6):1489-1496.

1224. Holzhauser T, Wackermann O, Ballmer-Weber BK, et al. Soybean (Glycine max) allergy in Europe: Gly m 5 (beta-conglycinin) and Gly m 6 (glycinin) are potential diagnostic markers for severe allergic reactions to soy. *J Allergy Clin Immunol*. 2009;123(2):452-458.

1225. Yagami A, Inaba Y, Kuno Y, et al. Two cases of pollen-food allergy syndrome to soy milk diagnosed by skin prick test, specific serum immunoglobulin E and microarray analysis. *J Dermatol*. 2009;36(1):50-55.

1226. Fukutomi Y, Sjolander S, Nakazawa T, et al. Clinical relevance of IgE to recombinant Gly m 4 in the diagnosis of adult soybean allergy. *J Allergy Clin Immunol*. 2012;129(3):860-863. e863.

1227. Anto JM, Sunyer J, Rodriguez-Roisin R, Suarez-Cervera M, Vazquez L. Community outbreaks of asthma associated with inhalation of soybean dust. *N Engl J Med*. 1989;320(17):1097-1102.

1228. Rodrigo MJ, Morel F, Helm RM, et al. Identification and partial characterization of the soybean-dust allergens involved in the Barcelona asthma epidemic. *J Allergy Clin Immunol*. 1990;85(4):778-784.

1229. Codina R, Lockey RF, Fernandez-Caldas E, Rama R. Identification of the soybean hull allergens responsible for the Barcelona asthma outbreaks. *Int Arch Allergy Immunol*. 1999;119(1):69-71.

1230. Thom de Souza CC, Rosario Filho NA, Camargo JF, RHM G. Levels of Airborne Soybean Allergen (Gly m 1) in a Brazilian Soybean Production City: A Pilot Study. *Int J Environ Res Public Health*. 2020;17(15).

1231. Haftenberger M, Laussmann D, Ellert U, et al. Prevalence of sensitization to aeroallergens and food allergens: results of the German Health Interview and Examination Survey for Adults (DEGS1). *Bundesgesundheitsblatt* Gesundheitsforschung Gesundheitsschutz. 2013;56(5-6):687-697.

1232. Ito K, Sjolander S, Sato S, et al. IgE to Gly m 5 and Gly m 6 is associated with severe allergic reactions to soybean in Japanese children. *J Allergy Clin Immunol*. 2011;128(3):673-675.

1233. Micardi PM, Bockelbrink A, Beyer K, et al. Primary versus secondary immunoglobulin E sensitization to soy and wheat in the Multi-Centre Allergy Study cohort. *Clin Exp Allergy*. 2008;38(3):493-500.

1234. Ebisawa M, Brostedt P, Sjolander S, Sato S, Borres MP, Ito K. Gly m 2S albumin is a major allergen with a high diagnostic value in soybean-allergic children. *J Allergy Clin Immunol*. 2013;132(4):976-978. e971-975.

1235. Ruiz Segura LT, Figueroa Perez E, Nowak-Wegrzyn A, Siepmann T, Larenas-Linnemann D. Food allergen sensitization patterns in a large allergic population in Mexico. *Allergol Immunopathol (Madr)*. 2020;48(6):553-559.

1236. Yamamoto-Hanada K, Borres MP, Aberg MK, et al. IgE responses to multiple allergen components among school-aged children in a general population birth cohort in Tokyo. *World Allergy Organ J*. 2020;13(2):100105.

1237. Klemans RJ, Knol EF, Michelsen-Huisman A, et al. Components in soy allergy diagnostics: Gly m 2S albumin has the best diagnostic value in adults. *Allergy*. 2013;68(11):1396-1402.

1238. Anto JM, Soriano JB, Sunyer J, et al. Long term outcome of soybean epidemic asthma after an allergen reduction intervention. *Thorax*. 1999;54(8):670-674.

1239. Maruyama N, Sato S, Cabanos C, Tanaka A, Ito K, Ebisawa M. Gly m 5/Gly m 8 fusion component as a potential novel candidate molecule for diagnosing soya bean allergy in Japanese children. *Clin Exp Allergy*. 2018;48(12):1726-1734.

1240. Ballmer-Weber BK, Lidholm J, Fernández-Rivas M, et al. IgE recognition patterns in peanut allergy are age dependent: perspectives of the EuroPrevall study. *Allergy*. 2015;70(4):391-407.

1241. Schwager C, Kull S, Behrends J, et al. Peanut oleosins associated with severe peanut allergy-importance of lipophilic allergens for comprehensive allergy diagnostics. *J Allergy Clin Immunol*. 2017;140(5):1331-1338. e1338.

1242. Lauer I, Dueringer N, Pokoj S, et al. The non-specific lipid transfer protein, Ara h 9, is an important allergen in peanut. *Clin Exp Allergy*. 2009;39(9):1427-1437.

1243. Greenhawt M, Shaker M, Wang J, et al. Peanut allergy diagnosis: A 2020 practice parameter update, systematic review, and GRADE analysis. *J Allergy Clin Immunol*. 2020;146(6):1302-1334.
1204. Norbäck D, Wieslander G. A Review on Epidemiological and Clinical Studies on Buckwheat Allergy. *Plants* (Basel). 2021;10(3).

1205. Jungewelter S, Airaksinen L, Pesonen M. Occupational buckwheat allergy as a cause of allergic rhinitis, asthma, contact urticaria and anaphylaxis-An emerging problem in food-handling occupations? *Am J Ind Med*. 2020;63(11):1047-1053.

1206. Breiteneder H, Radauer C. A classification of plant food allergens. *J Allergy Clin Immunol*. 2004;113(5):821-830. quiz 831.

1207. Maruyama N, Sato S, Yanagida N, et al. Clinical utility of recombinant allergen components in diagnosing buckwheat allergy. *J Allergy Clin Immunol Pract*. 2016;4(2):322-323.e323.

1208. Imamura T, Kanagawa Y, Ebisawa M. A survey of patients with self-reported severe food allergies in Japan. *Pediatr Allergy Immunol*. 2008;19(3):270-274.

1209. Yanagida N, Sato S, Takahashi K, et al. Reactions of Buckwheat-Hypersensitive Patients during Oral Food Challenge Are Rare, but Often Anaphylactic. *Int Arch Allergy Immunol*. 2017;172(2):116-122.

1210. Badiu I, Olivieri E, Montagni M, et al. Italian study on buckwheat allergy: prevalence and clinical features of buckwheat-sensitized patients in Italy. *Int J Immunopathol Pharmacol*. 2013;26:801-806.

1211. Urisu AKY, Morita Y, et al. Identification of a major allergen of buckwheat seeds by immunoblotting methods. *Allergy Clin Immunol News*. 1994;6:151-155. doi:10.1034/j.1398-9995.2000.00763.x

1212. Geiselhart S, Nagl C, Dubiela P, et al. Concomitant sensitization to legumin, Fag e 2 and Fag e 5 predicts buckwheat allergy. *Clin Exp Allergy*. 2018;48(2):217-224.

1213. Tanaka K, Matsumoto K, Akasawa A, et al. Pepsin-resistant 16-kD buckwheat protein is associated with immediate hypersensitivity reaction in patients with buckwheat allergy. *Int Arch Allergy Immunol*. 2002;129(1):49-56.

1214. Tohgi K, Kohno K, Takahashi H, Matsuo H, Nakayama S, Morita E. Usability of Fag e 2 ImmunoCAP in the diagnosis of buckwheat allergy. *Arch Dermatol Res*. 2011;303(9):635-642.

1215. Fok JS, Kette F, Smith WB, et al. Buckwheat allergy in Australia. *Intern Med J*. 2019;49(12):1552-1553.

1216. L'Hocine L, Boye JI. Allergenicity of soybean: new developments in identification of allergenic proteins, cross-reactivities and hypoallergenization technologies. *Crit Rev Food Sci Nutr*. 2007;47(2):127-143.

1217. Besler M, Helm RM, Ogawa T. Allergen data collection - update: soybean (*Glycine max*). *Int Symp Food Allerg*. 2000;2:1-35.

1218. Mittag D, Vieths S, Vogel L, et al. Soybean allergy in patients allergic to birch pollen: clinical investigation and molecular characterization of allergens. *J Allergy Clin Immunol*. 2004;113(1):148-154.

1219. Ballmer-Weber BK, Vieths S. Soy allergy in perspective. *Curr Opin Allergy Clin Immunol*. 2008;8(3):270-275.

1220. Katz Y, Gutierrez-Castrellon P, Gonzalez MG, Rivas R, Lee BW, Alarcon P. A comprehensive review of sensitization and allergy to soy-based products. *Clin Rev Allergy Immunol*. 2014;46(3):272-281.

1221. Sato M, Shukuya A, Sato S, et al. Oral challenge tests for soybean allergies in Japan: A summary of 142 cases. *Allergol Int*. 2016;65(1):68-73.

1222. Kleine-Tebbe J, Vogel L, Crowell DN, Haustein UF, Vieths S. Severe oral allergy syndrome and anaphylactic reactions caused by a Bet v 1- related PR-10 protein in soybean, SAM22. *J Allergy Clin Immunol*. 2002;110(5):797-804.

1223. Ballmer-Weber BK, Holzhauser T, Scibilia J, et al. Clinical characteristics of soybean allergy in Europe: a double-blind, placebo-controlled food challenge study. *J Allergy Clin Immunol*. 2007;119(6):1489-1496.

1224. Holzhauser T, Wackermann O, Ballmer-Weber BK, et al. Soybean (Glycine max) allergy in Europe: Gly m 5 (beta-conglycinin) and Gly m 6 (glycinin) are potential diagnostic markers for severe allergic reactions to soy. *J Allergy Clin Immunol*. 2009;123(2):452-458.

1225. Yagami A, Inaba Y, Kuno Y, et al. Two cases of pollen-food allergy syndrome to soy milk diagnosed by skin prick test, specific serum immunoglobulin E and microarray analysis. *J Dermatol*. 2009;36(1):50-55.

1226. Fukutomi Y, Sjolander S, Nakazawa T, et al. Clinical relevance of IgE to recombinant Gly m 4 in the diagnosis of adult soybean allergy. *J Allergy Clin Immunol*. 2012;129(3):860-863. e863.

1227. Anto JM, Sunyer J, Rodriguez-Roisin R, Suarez-Cervera M, Vazquez L. Community outbreaks of asthma associated with inhalation of soybean dust. *N Engl J Med*. 1989;320(17):1097-1102.

1228. Rodrigo MJ, Morel F, Helm RM, et al. Identification and partial characterization of the soybean-dust allergens involved in the Barcelona asthma epidemic. *J Allergy Clin Immunol*. 1990;85(4):778-784.

1229. Codina R, Lockey RF, Fernandez-Caldas E, Rama R. Identification of the soybean hull allergens responsible for the Barcelona asthma outbreaks. *Int Arch Allergy Immunol*. 1999;119(1):69-71.

1230. Thom de Souza CC, Rosario Filho NA, Camargo JF, RHM G. Levels of Airborne Soybean Allergen (Gly m 1) in a Brazilian Soybean Production City: A Pilot Study. *Int J Environ Res Public Health*. 2020;17(15).

1231. Haftenberger M, Laussmann D, Ellert U, et al. Prevalence of sensitization to aeroallergens and food allergens: results of the German Health Interview and Examination Survey for Adults (DEGS1). *Bundesgesundheitsblatt* Gesundheitsforschung Gesundheitsschutz. 2013;56(5-6):687-697.

1232. Ito K, Sjolander S, Sato S, et al. IgE to Gly m 5 and Gly m 6 is associated with severe allergic reactions to soybean in Japanese children. *J Allergy Clin Immunol*. 2011;128(3):673-675.

1233. Micardi PM, Bockelbrink A, Beyer K, et al. Primary versus secondary immunoglobulin E sensitization to soy and wheat in the Multi-Centre Allergy Study cohort. *Clin Exp Allergy*. 2008;38(3):493-500.

1234. Ebisawa M, Brostedt P, Sjolander S, Sato S, Borres MP, Ito K. Gly m 2S albumin is a major allergen with a high diagnostic value in soybean-allergic children. *J Allergy Clin Immunol*. 2013;132(4):976-978. e971-975.

1235. Ruiz Segura LT, Figueroa Perez E, Nowak-Wegrzyn A, Siepmann T, Larenas-Linnemann D. Food allergen sensitization patterns in a large allergic population in Mexico. *Allergol Immunopathol (Madr)*. 2020;48(6):553-559.

1236. Yamamoto-Hanada K, Borres MP, Aberg MK, et al. IgE responses to multiple allergen components among school-aged children in a general population birth cohort in Tokyo. *World Allergy Organ J*. 2020;13(2):100105.

1237. Klemans RJ, Knol EF, Michelsen-Huisman A, et al. Components in soy allergy diagnostics: Gly m 2S albumin has the best diagnostic value in adults. *Allergy*. 2013;68(11):1396-1402.

1238. Anto JM, Soriano JB, Sunyer J, et al. Long term outcome of soybean epidemic asthma after an allergen reduction intervention. *Thorax*. 1999;54(8):670-674.

1239. Maruyama N, Sato S, Cabanos C, Tanaka A, Ito K, Ebisawa M. Gly m 5/Gly m 8 fusion component as a potential novel candidate molecule for diagnosing soya bean allergy in Japanese children. *Clin Exp Allergy*. 2018;48(12):1726-1734.

1240. Ballmer-Weber BK, Lidholm J, Fernández-Rivas M, et al. IgE recognition patterns in peanut allergy are age dependent: perspectives of the EuroPrevall study. *Allergy*. 2015;70(4):391-407.

1241. Schwager C, Kull S, Behrends J, et al. Peanut oleosins associated with severe peanut allergy-importance of lipophilic allergens for comprehensive allergy diagnostics. *J Allergy Clin Immunol*. 2017;140(5):1331-1338. e1338.

1242. Lauer I, Dueringer N, Pokoj S, et al. The non-specific lipid transfer protein, Ara h 9, is an important allergen in peanut. *Clin Exp Allergy*. 2009;39(9):1427-1437.

1243. Greenhawt M, Shaker M, Wang J, et al. Peanut allergy diagnosis: A 2020 practice parameter update, systematic review, and GRADE analysis. *J Allergy Clin Immunol*. 2020;146(6):1302-1334.
1244. Uotila R, Kukkonen AK, Blom WM, et al. Component-resolved diagnostics demonstrates that most peanut-allergic individuals could potentially introduce tree nuts to their diet. *Clin Exp Allergy*. 2018;48(6):712-721.

1245. Vickery BP, Vereda A, Nilsson C, et al. Continuous and Daily Oral Immunotherapy for Peanut Allergy: Results from a 2-Year Open-Label Follow-On Study. *J Allergy Clin Immunol Pract*. 2021;9(5):1879-1889. e1814.

1246. Chen G, Shrock EL, Li MZ, et al. High-resolution epitope mapping by AllerScan reveals relationships between IgE and IgG repertoires during peanut oral immunotherapy. *Cell Rep Med*. 2021;2(10):100410.

1247. Turner PJ, Jerschow E, Umasunthar T, Lin R, Campbell DE, Boyle RJ. Fatal Anaphylaxis: Mortality Rate and Risk Factors. *J Allergy Clin Immunol Pract*. 2017;5(5):1169-1178.

1248. Umasunthar T, Leonardi-Bee J, Hodes M, et al. Incidence of fatal food anaphylaxis in people with food allergy: a systematic review and meta-analysis. *Clin Exp Allergy*. 2013;43(12):1333-1341.

1249. Bueno-Diaz C, Biserni C, Martín-Pedraza L, et al. Seed storage proteins, 2S albumin and 11S globulin, associated to severe allergic reactions after flaxseed intake. *J Investig Allergol Clin Immunol*. 2022;32:375-382.

1250. García Jiménez S, Pastor Vargas C. de las Heras M, Sanz Maroto A, Vivanco F, Sastre J. Allergen characterization of chia seeds (Salvia hispanica), a new allergenic food. *J Investig Allergol Clin Immunol*. 2015;25(1):55-56.

1251. American College of Astma Al. *Tree nut*. 2021 20-10-2021. https://acaii.org/allergies/allergic-conditions/food/tree-nut/

1252. Blom WM, van Dijk LM, Michelsen-Huisman A, et al. Allergen labeling: Current practice and improvement from a communication perspective. *Clin Exp Allergy*. 2021;51(4):574-584.

1253. Crevel RW. Kerkhoff MA, Koning MM. Allergenicity of refined vegetable oils. *Food Chem Toxicol*. 2000;38(4):385-393.

1254. Caffarelli C, Mastrorilli C, Santoro A, Criscione M, Procaccianti M. Component-Resolved Diagnosis of Hazelnut Allergy in Children. *Nutrients*. 2021;13(2).

1255. Scheurer S, van Ree R, Vieths S. The Role of Lipid Transfer Proteins as Food and Pollen Allergens Outside the Mediterranean Area. *Curr Allergy Asthma Rep*. 2021;21(2):7.

1256. Li J, Ogorodova LM, Mahesh PA, et al. Comparative Study of Food Allergies in Children from China, India, and Russia: The EuroPrevALLINCO Surveys. *J Allergy Clin Immunol Pract*. 2020;8(4):1349-1358. e1316.

1257. Sasaki M, Koplin JJ, Dharmage SC, et al. Prevalence of clinic-defined food allergy in early adolescence: The SchoolNuts study. *J Allergy Clin Immunol*. 2018;141(1):391-398.e394.

1258. McWilliam V, Peters R, Tang MLK, et al. Patterns of tree nut sensitization and allergy in the first 6 years of life in a population-based cohort. *J Allergy Clin Immunol*. 2019;143(2):644-650.e645.

1259. Sirvent S, Akotenou M, Cuesta-Herranz J, et al. The 11S globulin Sin a 2 from yellow mustard seeds shows IgE cross-reactivity with homologous counterparts from tree nuts and peanut. *Clin Transl Allergy*. 2012;2(1):23.

1260. van der Valk JP, Dubois AE. Gerth van Wijk R, Wichers HJ, de Jong NW. Systematic review on cashew nut allergy. *Allergy*. 2014;69(6):692-698.

1261. Vetander M, Helander D, Flodström C, et al. Anaphylaxis and reactions to foods in children-a population-based case study of emergency department visits. *Clin Exp Allergy*. 2012;42(4):568-577.

1262. Andersson K, Ballmer-Weber BK, Cistero-Bahima A, et al. Enhancement of hazelnut extract for IgE testing by recombinant allergen spiking. *Allergy*. 2007;62(8):897-904.

1263. Blankestijn MA, Blom WM, Otten HG, et al. Specific IgE to Jug r 1 has no additional value compared with extract-based

testing in diagnosing walnut allergy in adults. *J Allergy Clin Immunol*. 2017;139(2):688-690.e684.

1264. Maruyama N, Nakagawa T, Ito K, et al. Measurement of specific IgE antibodies to Ses i 1 improves the diagnosis of sesame allergy. *Clin Exp Allergy*. 2016;46(1):163-171.

1265. Elizur A, Appel MY, Nachshon L, et al. NUT Co Reactivity - ACquiring Knowledge for Elimination Recommendations (NUT CRACKER) study. *Allergy*. 2018;73(3):593-601.

1266. Brough HA, Caubet JC, Mazon A, et al. Defining challenge-proven coexistent nut and sesame seed allergy: A prospective multicenter European study. *J Allergy Clin Immunol*. 2020;145(4):1231-1239.

1267. Varga EM, Kollmann D, Zach M, Bohle B. Anaphylaxis to buckwheat in an atopic child: a risk factor for severe allergy to nuts and seeds? *Int Arch Allergy Immunol*. 2011;156(1):112-116.

1268. De Maat-Bleeker F, Stapel SO. Cross-reactivity between buckwheat and latex. *Allergy*. 1998;53(5):538-539.

1269. Masthoff LJN, Pasmans S, van Doorn H, et al. Major hazelnut and peanut allergens are potent in basophil activation and cross-react at T-cell level. *Allergy*. 2018;73(10):2080-2082.

1270. Sampson HA. Gerth van Wijk R, Bindslev-Jensen C, et al. Standardizing double-blind, placebo-controlled oral food challenges: American Academy of Allergy, Asthma & Immunology-European Academy of Allergy and Clinical Immunology PRACTALL consensus report. *J Allergy Clin Immunol*. 2012;130(6):1260-1274.

1271. Muraro A, Worm M, Alviani C, et al. EAACI guidelines: Anaphylaxis (2021 update). *Allergy*. 2022;77(2):357-377.

1272. van Hoffen E, Peeters KA, van Neerven RJ, et al. Effect of birch pollen-specific immunotherapy on birch pollen-related hazelnut allergy. *J Allergy Clin Immunol*. 2011;127:100-101.

1273. Worm M, Moneret-Vautrin A, Scherer K, et al. First European data from the network of severe allergic reactions (NORA). *Allergy*. 2014;69(10):1397-1404.

1274. Bucher C, Korner P, Wüthrich B. Allergy to bumblebee venom. *Curr Opin Allergy Clin Immunol*. 2001;1(4):361-365.

1275. Biló BMRF, Mosbech H. et al., EAACI Interest Group on Insect Venom Hypersensitivity. Diagnosis of Hymenoptera venom allergy. *Allergy*. 2005;60(11):1339-1349. doi:10.1111/j.1398-9995.2005.00963.x

1276. Arzt L, Bokanovic D, Schrautzer C, et al. Immunological differences between insect venom-allergic patients with and without immunotherapy and asymptomatically sensitized subjects. *Allergy*. 2018;73(6):1223-1231.

1277. Golden DB. Insect sting allergy and venom immunotherapy: a model and a mystery. *J Allergy Clin Immunol*. 2005;115(3):439-447. quiz 448.

1278. Antonicelli L, Bilò MB, Bonifazi F. Epidemiology of Hymenoptera allergy. *Curr Opin Allergy Clin Immunol*. 2002;2(4):341-346.

1279. Blank S, Bilò MB, Ollert M. Component-resolved diagnostics to direct in venom immunotherapy: Important steps towards precision medicine. *Clin Exp Allergy*. 2018;48(4):354-364.

1280. Blank SBM, Grosch J, et al. Marker allergens in Hymenoptera venom allergy — Characteristics and potential use in precision medicine. *Allergo J Int*. 2021;30(1):26-38. doi:10.1007/s40629-020-00151-5

1281. Ruiz B, Serrano P, Verdú M, Moreno C. Sensitization to Api m 1, Api m 2, and Api m 4: association with safety of bee venom immunotherapy. *Ann Allergy Asthma Immunol*. 2015;114(4):350-352.

1282. Hamilton RG, Williams PB. Human IgE antibody serology: a primer for the practicing North American allergist/immunologist. *J Allergy Clin Immunol*. 2010;126(1):33-38.

1283. Cifuentes L, Vosseler S, Blank S, et al. Identification of Hymenoptera venom-allergic patients with negative specific IgE to venom extract by using recombinant allergens. *J Allergy Clin Immunol*. 2014;133(3):909-910.

1284. Rafei-Shamsabadi D, Müller S, Pfützner W, Spillner E, Ruëff F, Jakob T. Recombinant allergens rarely allow identification of Hymenoptera venom-allergic patients with negative
1244. Uotila R, Kukkonen AK, Blom WM, et al. Component-resolved diagnostics demonstrates that most peanut-allergic individuals could potentially introduce tree nuts to their diet. *Clin Exp Allergy*. 2018;48(6):712-721.

1245. Vickery BP, Vereda A, Nilsson C, et al. Continuous and Daily Oral Immunotherapy for Peanut Allergy: Results from a 2-Year Open-Label Follow-On Study. *J Allergy Clin Immunol Pract*. 2021;9(5):1879-1889. e1814.

1246. Chen G, Shrock EL, Li MZ, et al. High-resolution epitope mapping by AllerScan reveals relationships between IgE and IgG repertoires during peanut oral immunotherapy. *Cell Rep Med*. 2021;2(10):100410.

1247. Turner PJ, Jerschow E, Umasunthar T, Lin R, Campbell DE, Boyle RJ. Fatal Anaphylaxis: Mortality Rate and Risk Factors. *J Allergy Clin Immunol Pract*. 2017;5(5):1169-1178.

1248. Umasunthar T, Leonardi-Bee J, Hodes M, et al. Incidence of fatal food anaphylaxis in people with food allergy: a systematic review and meta-analysis. *Clin Exp Allergy*. 2013;43(12):1333-1341.

1249. Bueno-Diaz C, Biserni C, Martín-Pedraza L, et al. Seed storage proteins, 2S albumin and 11S globulin, associated to severe allergic reactions after flaxseed intake. *J Investig Allergol Clin Immunol*. 2022;32:375-382.

1250. García Jiménez S, Pastor Vargas C. de las Heras M, Sanz Maroto A, Vivanco F, Sastre J. Allergen characterization of chia seeds (Salvia hispanica), a new allergenic food. *J Investig Allergol Clin Immunol*. 2015;25(1):55-56.

1251. American College of Astma Al. *Tree nut*. 2021 20-10-2021. https://acaii.org/allergies/allergic-conditions/food/tree-nut/

1252. Blom WM, van Dijk LM, Michelsen-Huisman A, et al. Allergen labeling: Current practice and improvement from a communication perspective. *Clin Exp Allergy*. 2021;51(4):574-584.

1253. Crevel RW. Kerkhoff MA, Koning MM. Allergenicity of refined vegetable oils. *Food Chem Toxicol*. 2000;38(4):385-393.

1254. Caffarelli C, Mastrorilli C, Santoro A, Criscione M, Procaccianti M. Component-Resolved Diagnosis of Hazelnut Allergy in Children. *Nutrients*. 2021;13(2).

1255. Scheurer S, van Ree R, Vieths S. The Role of Lipid Transfer Proteins as Food and Pollen Allergens Outside the Mediterranean Area. *Curr Allergy Asthma Rep*. 2021;21(2):7.

1256. Li J, Ogorodova LM, Mahesh PA, et al. Comparative Study of Food Allergies in Children from China, India, and Russia: The EuroPrevALLINCO Surveys. *J Allergy Clin Immunol Pract*. 2020;8(4):1349-1358. e1316.

1257. Sasaki M, Koplin JJ, Dharmage SC, et al. Prevalence of clinic-defined food allergy in early adolescence: The SchoolNuts study. *J Allergy Clin Immunol*. 2018;141(1):391-398.e394.

1258. McWilliam V, Peters R, Tang MLK, et al. Patterns of tree nut sensitization and allergy in the first 6 years of life in a population-based cohort. *J Allergy Clin Immunol*. 2019;143(2):644-650.e645.

1259. Sirvent S, Akotenou M, Cuesta-Herranz J, et al. The 11S globulin Sin a 2 from yellow mustard seeds shows IgE cross-reactivity with homologous counterparts from tree nuts and peanut. *Clin Transl Allergy*. 2012;2(1):23.

1260. van der Valk JP, Dubois AE. Gerth van Wijk R, Wichers HJ, de Jong NW. Systematic review on cashew nut allergy. *Allergy*. 2014;69(6):692-698.

1261. Vetander M, Helander D, Flodström C, et al. Anaphylaxis and reactions to foods in children-a population-based case study of emergency department visits. *Clin Exp Allergy*. 2012;42(4):568-577.

1262. Andersson K, Ballmer-Weber BK, Cistero-Bahima A, et al. Enhancement of hazelnut extract for IgE testing by recombinant allergen spiking. *Allergy*. 2007;62(8):897-904.

1263. Blankestijn MA, Blom WM, Otten HG, et al. Specific IgE to Jug r 1 has no additional value compared with extract-based

testing in diagnosing walnut allergy in adults. *J Allergy Clin Immunol*. 2017;139(2):688-690.e684.

1264. Maruyama N, Nakagawa T, Ito K, et al. Measurement of specific IgE antibodies to Ses i 1 improves the diagnosis of sesame allergy. *Clin Exp Allergy*. 2016;46(1):163-171.

1265. Elizur A, Appel MY, Nachshon L, et al. NUT Co Reactivity - ACquiring Knowledge for Elimination Recommendations (NUT CRACKER) study. *Allergy*. 2018;73(3):593-601.

1266. Brough HA, Caubet JC, Mazon A, et al. Defining challenge-proven coexistent nut and sesame seed allergy: A prospective multicenter European study. *J Allergy Clin Immunol*. 2020;145(4):1231-1239.

1267. Varga EM, Kollmann D, Zach M, Bohle B. Anaphylaxis to buckwheat in an atopic child: a risk factor for severe allergy to nuts and seeds? *Int Arch Allergy Immunol*. 2011;156(1):112-116.

1268. De Maat-Bleeker F, Stapel SO. Cross-reactivity between buckwheat and latex. *Allergy*. 1998;53(5):538-539.

1269. Masthoff LJN, Pasmans S, van Doorn H, et al. Major hazelnut and peanut allergens are potent in basophil activation and cross-react at T-cell level. *Allergy*. 2018;73(10):2080-2082.

1270. Sampson HA. Gerth van Wijk R, Bindslev-Jensen C, et al. Standardizing double-blind, placebo-controlled oral food challenges: American Academy of Allergy, Asthma & Immunology-European Academy of Allergy and Clinical Immunology PRACTALL consensus report. *J Allergy Clin Immunol*. 2012;130(6):1260-1274.

1271. Muraro A, Worm M, Alviani C, et al. EAACI guidelines: Anaphylaxis (2021 update). *Allergy*. 2022;77(2):357-377.

1272. van Hoffen E, Peeters KA, van Neerven RJ, et al. Effect of birch pollen-specific immunotherapy on birch pollen-related hazelnut allergy. *J Allergy Clin Immunol*. 2011;127:100-101.

1273. Worm M, Moneret-Vautrin A, Scherer K, et al. First European data from the network of severe allergic reactions (NORA). *Allergy*. 2014;69(10):1397-1404.

1274. Bucher C, Korner P, Wüthrich B. Allergy to bumblebee venom. *Curr Opin Allergy Clin Immunol*. 2001;1(4):361-365.

1275. Biló BMRF, Mosbech H. et al.; EAACI Interest Group on Insect Venom Hypersensitivity. Diagnosis of Hymenoptera venom allergy. *Allergy*. 2005;60(11):1339-1349. doi:10.1111/j.1398-9995.2005.00963.x

1276. Arzt L, Bokanovic D, Schrautzer C, et al. Immunological differences between insect venom-allergic patients with and without immunotherapy and asymptomatically sensitized subjects. *Allergy*. 2018;73(6):1223-1231.

1277. Golden DB. Insect sting allergy and venom immunotherapy: a model and a mystery. *J Allergy Clin Immunol*. 2005;115(3):439-447. quiz 448.

1278. Antonicelli L, Bilò MB, Bonifazi F. Epidemiology of Hymenoptera allergy. *Curr Opin Allergy Clin Immunol*. 2002;2(4):341-346.

1279. Blank S, Bilò MB, Ollert M. Component-resolved diagnostics to direct in venom immunotherapy: Important steps towards precision medicine. *Clin Exp Allergy*. 2018;48(4):354-364.

1280. Blank SBM, Grosch J, et al. Marker allergens in Hymenoptera venom allergy — Characteristics and potential use in precision medicine. *Allergo J Int*. 2021;30(1):26-38. doi:10.1007/s40629-020-00151-5

1281. Ruiz B, Serrano P, Verdú M, Moreno C. Sensitization to Api m 1, Api m 2, and Api m 4: association with safety of bee venom immunotherapy. *Ann Allergy Asthma Immunol*. 2015;114(4):350-352.

1282. Hamilton RG, Williams PB. Human IgE antibody serology: a primer for the practicing North American allergist/immunologist. *J Allergy Clin Immunol*. 2010;126(1):33-38.

1283. Cifuentes L, Vosseler S, Blank S, et al. Identification of Hymenoptera venom-allergic patients with negative specific IgE to venom extract by using recombinant allergens. *J Allergy Clin Immunol*. 2014;133(3):909-910.

1284. Rafei-Shamsabadi D, Müller S, Pfützner W, Spillner E, Ruëff F, Jakob T. Recombinant allergens rarely allow identification of Hymenoptera venom-allergic patients with negative
specific IgE to whole venom preparations. *J Allergy Clin Immunol.*
2014;134(2):493-494.

1285. Sturm GJ, Varga EM, Roberts G, et al. EAACI guidelines on al-lergen immunotherapy: Hymenoptera venom allergy. *Allergy*. 2018;73(4):744-764.

1286. Bilò MB, Pravettoni V, Bignardi D, et al. Hymenoptera Venom Allergy: Management of Children and Adults in Clinical Practice. *J Investig Allergol Clin Immunol.* 2019;29(3):180-205.

1287. Chugo S, Lizaso MT, Alvarez MJ, Arroabaren E, Lizarza S, Tabar Al. Vespa velutina nigritorax: A New Causative Agent in Anaphylaxis. *J Investig Allergol Clin Immunol.* 2015;25(3):231-232.

1288. Hoffman DR. Allergens in Hymenoptera venom. XVI: Studies of the structures and cross-reactivities of vespid venom phospholipases. *J Allergy Clin Immunol.* 1986;78(2):337-343.

1289. Monsalve RI, Vega A, Marqués L, et al. Component-resolved diagnosis of vespid venom-allergic individuals: phospholipases and antigen 5s are necessary to identify Vespula or Polistes sensitization. *Allergy*. 2012;67(4):528-536.

1290. Severino MG, Caruso B, Bonadonna P, et al. Cross reactivity between European hornet and yellow jacket venoms. *Eur Ann Allergy Clin Immunol.* 2010;42(4):141-145.

1291. Kolarich D, Léonard R, Hemmer W, Altmann F. The N-glycans of yellow jacket venom hyaluronidases and the protein sequence of its major isoform in Vespula vulgaris. *FEBS J.* 2005;272(20):5182-5190.

1292. Lee VS, Tu WC, Jinn TR, Peng CC, Lin LJ, Tzen JT. Molecular cloning of the precursor polypeptide of mastoparan B and its putative processing enzyme, dipeptidyl peptidase IV, from the black-bellied hornet, *Vespa basalis*. *Insect Mol Biol.* 2007;16(2):231-237.

1293. Blank S, Seismann H, McIntyre M, et al. Vitellogenins are new high molecular weight components and allergens (Api m 12 and Ves v 6) of Apis mellifera and Vespula vulgaris venom. *PLoS One*. 2013;8(4):e62009.

1294. Winningham KM, Fitch CD, Schmidt M, Hoffman DR. Hymenoptera venom protease allergens. *J Allergy Clin Immunol.* 2004;114(4):928-933.

1295. Grosch J, Hilger C, Bilò MB, et al. Shedding Light on the Venom Proteomes of the Allergy-Relevant Hymenoptera Polistes dominula (European Paper Wasp) and Vespula spp. (Yellow Jacket). *Toxins (Basel)*. 2020;12(5).

1296. Ebo DG, Faber M, Sabato V, Leysen J, Bridts CH, De Clerck LS. Component-resolved diagnosis of wasp (yellow jacket) venom allergy. *Clin Exp Allergy*. 2013;43(2):255-261.

1297. Michel J, Brockow K, Darsow U, et al. Added sensitivity of component-resolved diagnosis in hymenoptera venom-allergic patients with elevated serum tryptase and/or mastocytosis. *Allergy*. 2016;71(5):651-660.

1298. Vos B, Köhler J, Müller S, Stretz E, Ruëff F, Jakob T. Spiking venom with rVes v 5 improves sensitivity of IgE detection in patients with allergy to Vespula venom. *J Allergy Clin Immunol.* 2013;131(4):1225-1227. 1227.e1221.

1299. Sturm GJ, Bilò MB, Bonadonna P, et al. Ves v 5 can establish the diagnosis in patients without detectable specific IgE to wasp venom and a possible north-south difference in Api m 1 sensitization in Europe. *J Allergy Clin Immunol.* 2012;130:817.

1300. Korošec P, Valenta R, Mittermann I, et al. High sensitivity of CAP-FEIA rVes v 5 and rVes v 1 for diagnosis of Vespula venom allergy. *J Allergy Clin Immunol.* 2012;129:1406-1408.

1301. Hofmann SC, Pfender N, Weckesser S, Huss-Marp J, Jakob T. Added value of IgE detection to rApi m 1 and rVes v 5 in patients with Hymenoptera venom allergy. *J Allergy Clin Immunol.* 2011;127:265-267.

1302. Šelb J, Kogovšek R, Šilar M, Košnik M, Korošec P. Improved recombinant Api m 1- and Ves v 5-based IgE testing to dissect bee and yellow jacket allergy and their correlation with the severity of the sting reaction. *Clin Exp Allergy*. 2016;46(4):621-630.

1303. Seismann H, Blank S, Braren I, et al. Dissecting cross-reactivity in hymenoptera venom allergy by circumvention of alpha-1,3-core fucosylation. *Mol Immunol.* 2010;47(4):799-808.

1304. Schrautzer C, Bokanovic D, Hemmer W, et al. Sensitivity and specificity of Hymenoptera allergen components depend on the diagnostic assay employed. *J Allergy Clin Immunol.* 2016;137(5):1603-1605.

1305. Bilò MB, Martini M, Bonadonna P, et al. Prevalence of Pol d 1 Sensitization in Polistes dominula Allergy and Its Diagnostic Role in Vespid Double-Positivity. *J Allergy Clin Immunol Pract.* 2021;9(10):3781-3787.

1306. Blank S, Bazon ML, Grosch J, et al. Antigen 5 Allergens of Hymenoptera Venoms and Their Role in Diagnosis and Therapy of Venom Allergy. *Curr Allergy Asthma Rep.* 2020;20(10):58.

1307. Blanca M, Garcia F, Miranda A, et al. Determination of IgE antibodies to Polistes dominulus, Vespula germanica and Vespa crabro in sera of patients allergic to vespids. *Allergy*. 1991;46(2):109-114.

1308. Severino MG, Campi P, Macchia D, et al. European Polistes venom allergy. *Allergy*. 2006;61(7):860-863.

1309. Blank S, Neu C, Hasche D, Bantleon FI, Jakob T, Spillner E. Polistes species venom is devoid of carbohydrate-based cross-reactivity and allows interference-free diagnostics. *J Allergy Clin Immunol.* 2013;131(4):1239-1242.

1310. Golden DB, Demain J, Freeman T, et al. Stinging insect hypersensitivity: A practice parameter update 2016. *Ann Allergy Asthma Immunol.* 2017;118(1):28-54.

1311. Golden DB, Kelly D, Hamilton RG, Wang NY, Kagey-Sobotka A. Dialyzed venom skin tests for identifying yellow jacket-allergic patients not detected using standard venom. *Ann Allergy Asthma Immunol.* 2009;102(1):47-50.

1312. Pantera B, Hoffman DR, Carresi L, et al. Characterization of the major allergens purified from the venom of the paper wasp Polistes gallicus. *Biochim Biophys Acta.* 2003;1623(2-3):72-81.

1313. Macchia D, Cortellini G, Mauro M, et al. Vespa crabro immunotherapy versus Vespula-venom immunotherapy in Vespa crabro allergy: a comparison study in field re-stings. *World Allergy Organ J.* 2018;11(1):3.

1314. Gattinger P, Lupinek C, Kalogiros L, et al. The culprit insect but not severity of allergic reactions to bee and wasp venom can be determined by molecular diagnosis. *PLoS One*. 2018;13(6):e0199250.

1315. Alvarez-Twose I, González de Olano D, Sánchez-Muñoz L, et al. Clinical, biological, and molecular characteristics of clonal mast cell disorders presenting with systemic mast cell activation symptoms. *J Allergy Clin Immunol.* 2010;125(6):1269-1278.e1262.

1316. Vos B, van Anrooij B, van Doormaal JJ, Dubois AEJ, Oude Elberink JNG. Fatal Anaphylaxis to Yellow Jacket Stings in Mastocytosis: Options for Identification and Treatment of At-Risk Patients. *J Allergy Clin Immunol Pract.* 2017;5(5):1264-1271.

1317. Galindo-Bonilla PA, Galán-Nieto A, Alfaya-Arias T, García-Rodríguez C, de la Roca-Pinzón F, Feo-Brito F. Component-resolved diagnosis in vespid venom-allergic individuals. *Allergol Immunopathol (Madr).* 2015;43(4):398-402.

1318. Jakob T, Müller U, Helbling A, Spillner E. Component resolved diagnostics for hymenoptera venom allergy. *Curr Opin Allergy Clin Immunol.* 2017;17(5):363-372.

1319. Caruso B, Bonadonna P, Severino MG, et al. Evaluation of the IgE cross-reactions among vespid venoms. A possible approach for the choice of immunotherapy. *Allergy*. 2007;62(5):561-564.

1320. Savi E, Peveri S, Makri E, Pravettoni V, Incorvaia C. Comparing the ability of molecular diagnosis and CAP-inhibition in identifying the really causative venom in patients with positive tests to Vespula and Polistes species. *Clin Mol Allergy*. 2016;14:3.

1321. Quercia O, Cova V, Martini M, et al. CAP-Inhibition, Molecular Diagnostics, and Total IgE in the Evaluation of Polistes and
specific IgE to whole venom preparations. *J Allergy Clin Immunol.*
2014;134(2):493-494.

1285. Sturm GJ, Varga EM, Roberts G, et al. EAACI guidelines on al-lergen immunotherapy: Hymenoptera venom allergy. *Allergy*. 2018;73(4):744-764.

1286. Bilò MB, Pravettoni V, Bignardi D, et al. Hymenoptera Venom Allergy: Management of Children and Adults in Clinical Practice. *J Investig Allergol Clin Immunol.* 2019;29(3):180-205.

1287. Chugo S, Lizaso MT, Alvarez MJ, Arroabaren E, Lizarza S, Tabar Al. Vespa velutina nigritorax: A New Causative Agent in Anaphylaxis. *J Investig Allergol Clin Immunol.* 2015;25(3):231-232.

1288. Hoffman DR. Allergens in Hymenoptera venom. XVI: Studies of the structures and cross-reactivities of vespid venom phospholipases. *J Allergy Clin Immunol.* 1986;78(2):337-343.

1289. Monsalve RI, Vega A, Marqués L, et al. Component-resolved diagnosis of vespid venom-allergic individuals: phospholipases and antigen 5s are necessary to identify Vespula or Polistes sensitization. *Allergy*. 2012;67(4):528-536.

1290. Severino MG, Caruso B, Bonadonna P, et al. Cross reactivity between European hornet and yellow jacket venoms. *Eur Ann Allergy Clin Immunol.* 2010;42(4):141-145.

1291. Kolarich D, Léonard R, Hemmer W, Altmann F. The N-glycans of yellow jacket venom hyaluronidases and the protein sequence of its major isoform in Vespula vulgaris. *FEBS J.* 2005;272(20):5182-5190.

1292. Lee VS, Tu WC, Jinn TR, Peng CC, Lin LJ, Tzen JT. Molecular cloning of the precursor polypeptide of mastoparan B and its putative processing enzyme, dipeptidyl peptidase IV, from the black-bellied hornet, *Vespa basalis*. *Insect Mol Biol.* 2007;16(2):231-237.

1293. Blank S, Seismann H, McIntyre M, et al. Vitellogenins are new high molecular weight components and allergens (Api m 12 and Ves v 6) of Apis mellifera and Vespula vulgaris venom. *PLoS One*. 2013;8(4):e62009.

1294. Winningham KM, Fitch CD, Schmidt M, Hoffman DR. Hymenoptera venom protease allergens. *J Allergy Clin Immunol.* 2004;114(4):928-933.

1295. Grosch J, Hilger C, Bilò MB, et al. Shedding Light on the Venom Proteomes of the Allergy-Relevant Hymenoptera Polistes dominula (European Paper Wasp) and Vespula spp. (Yellow Jacket). *Toxins (Basel)*. 2020;12(5).

1296. Ebo DG, Faber M, Sabato V, Leysen J, Bridts CH, De Clerck LS. Component-resolved diagnosis of wasp (yellow jacket) venom allergy. *Clin Exp Allergy*. 2013;43(2):255-261.

1297. Michel J, Brockow K, Darsow U, et al. Added sensitivity of component-resolved diagnosis in hymenoptera venom-allergic patients with elevated serum tryptase and/or mastocytosis. *Allergy*. 2016;71(5):651-660.

1298. Vos B, Köhler J, Müller S, Stretz E, Ruëff F, Jakob T. Spiking venom with rVes v 5 improves sensitivity of IgE detection in patients with allergy to Vespula venom. *J Allergy Clin Immunol.* 2013;131(4):1225-1227. 1227.e1221.

1299. Sturm GJ, Bilò MB, Bonadonna P, et al. Ves v 5 can establish the diagnosis in patients without detectable specific IgE to wasp venom and a possible north-south difference in Api m 1 sensitization in Europe. *J Allergy Clin Immunol.* 2012;130:817.

1300. Korošec P, Valenta R, Mittermann I, et al. High sensitivity of CAP-FEIA rVes v 5 and rVes v 1 for diagnosis of Vespula venom allergy. *J Allergy Clin Immunol.* 2012;129:1406-1408.

1301. Hofmann SC, Pfender N, Weckesser S, Huss-Marp J, Jakob T. Added value of IgE detection to rApi m 1 and rVes v 5 in patients with Hymenoptera venom allergy. *J Allergy Clin Immunol.* 2011;127:265-267.

1302. Šelb J, Kogovšek R, Šilar M, Košnik M, Korošec P. Improved recombinant Api m 1- and Ves v 5-based IgE testing to dissect bee and yellow jacket allergy and their correlation with the severity of the sting reaction. *Clin Exp Allergy*. 2016;46(4):621-630.

1303. Seismann H, Blank S, Braren I, et al. Dissecting cross-reactivity in hymenoptera venom allergy by circumvention of alpha-1,3-core fucosylation. *Mol Immunol.* 2010;47(4):799-808.

1304. Schrautzer C, Bokanovic D, Hemmer W, et al. Sensitivity and specificity of Hymenoptera allergen components depend on the diagnostic assay employed. *J Allergy Clin Immunol.* 2016;137(5):1603-1605.

1305. Bilò MB, Martini M, Bonadonna P, et al. Prevalence of Pol d 1 Sensitization in Polistes dominula Allergy and Its Diagnostic Role in Vespid Double-Positivity. *J Allergy Clin Immunol Pract.* 2021;9(10):3781-3787.

1306. Blank S, Bazon ML, Grosch J, et al. Antigen 5 Allergens of Hymenoptera Venoms and Their Role in Diagnosis and Therapy of Venom Allergy. *Curr Allergy Asthma Rep.* 2020;20(10):58.

1307. Blanca M, Garcia F, Miranda A, et al. Determination of IgE antibodies to Polistes dominulus, Vespula germanica and Vespa crabro in sera of patients allergic to vespids. *Allergy*. 1991;46(2):109-114.

1308. Severino MG, Campi P, Macchia D, et al. European Polistes venom allergy. *Allergy*. 2006;61(7):860-863.

1309. Blank S, Neu C, Hasche D, Bantleon FI, Jakob T, Spillner E. Polistes species venom is devoid of carbohydrate-based cross-reactivity and allows interference-free diagnostics. *J Allergy Clin Immunol.* 2013;131(4):1239-1242.

1310. Golden DB, Demain J, Freeman T, et al. Stinging insect hypersensitivity: A practice parameter update 2016. *Ann Allergy Asthma Immunol.* 2017;118(1):28-54.

1311. Golden DB, Kelly D, Hamilton RG, Wang NY, Kagey-Sobotka A. Dialyzed venom skin tests for identifying yellow jacket-allergic patients not detected using standard venom. *Ann Allergy Asthma Immunol.* 2009;102(1):47-50.

1312. Pantera B, Hoffman DR, Carresi L, et al. Characterization of the major allergens purified from the venom of the paper wasp Polistes gallicus. *Biochim Biophys Acta.* 2003;1623(2-3):72-81.

1313. Macchia D, Cortellini G, Mauro M, et al. Vespa crabro immunotherapy versus Vespula-venom immunotherapy in Vespa crabro allergy: a comparison study in field re-stings. *World Allergy Organ J.* 2018;11(1):3.

1314. Gattinger P, Lupinek C, Kalogiros L, et al. The culprit insect but not severity of allergic reactions to bee and wasp venom can be determined by molecular diagnosis. *PLoS One*. 2018;13(6):e0199250.

1315. Alvarez-Twose I, González de Olano D, Sánchez-Muñoz L, et al. Clinical, biological, and molecular characteristics of clonal mast cell disorders presenting with systemic mast cell activation symptoms. *J Allergy Clin Immunol.* 2010;125(6):1269-1278.e1262.

1316. Vos B, van Anrooij B, van Doormaal JJ, Dubois AEJ, Oude Elberink JNG. Fatal Anaphylaxis to Yellow Jacket Stings in Mastocytosis: Options for Identification and Treatment of At-Risk Patients. *J Allergy Clin Immunol Pract.* 2017;5(5):1264-1271.

1317. Galindo-Bonilla PA, Galán-Nieto A, Alfaya-Arias T, García-Rodríguez C, de la Roca-Pinzón F, Feo-Brito F. Component-resolved diagnosis in vespid venom-allergic individuals. *Allergol Immunopathol (Madr).* 2015;43(4):398-402.

1318. Jakob T, Müller U, Helbling A, Spillner E. Component resolved diagnostics for hymenoptera venom allergy. *Curr Opin Allergy Clin Immunol.* 2017;17(5):363-372.

1319. Caruso B, Bonadonna P, Severino MG, et al. Evaluation of the IgE cross-reactions among vespid venoms. A possible approach for the choice of immunotherapy. *Allergy*. 2007;62(5):561-564.

1320. Savi E, Peveri S, Makri E, Pravettoni V, Incorvaia C. Comparing the ability of molecular diagnosis and CAP-inhibition in identifying the really causative venom in patients with positive tests to Vespula and Polistes species. *Clin Mol Allergy*. 2016;14:3.

1321. Quercia O, Cova V, Martini M, et al. CAP-Inhibition, Molecular Diagnostics, and Total IgE in the Evaluation of Polistes and
Vespula Double Sensitization. *Int Arch Allergy Immunol.* 2018;177(4):365-369.

1322. Dalmau Duch G, Gázquez García V, Gaig Jané P, Galán Nieto A, Monsalve Clemente Rl. Importance of controlled sting challenge and component-resolved diagnosis in the success of venom immunotherapy. *J Investig Allergol Clin Immunol.* 2012;22(2):135-136.

1323. Korošč P, Šilar M, Eržen R, et al. Clinical routine utility of basophil activation testing for diagnosis of hymenoptera-allergic patients with emphasis on individuals with negative venom-specific IgE antibodies. *Int Arch Allergy Immunol.* 2013;161(4):363-368.

1324. Eberlein B, Krischan L, Darsow U, Ollert M, Ring J. Double positivity to bee and wasp venom: improved diagnostic procedure by recombinant allergen-based IgE testing and basophil activation test including data about cross-reactive carbohydrate determinants. *J Allergy Clin Immunol.* 2012;130(1):155-161.

1325. Peternelj A, Silar M, Erzen R, Kosnik M, Korosec P. Basophil sensitivity in patients not responding to venom immunotherapy. *Int Arch Allergy Immunol.* 2008;146(3):248-254.

1326. Ruëff F, Przybilla B, Müller U, Mosbech H. The sting challenge test in Hymenoptera venom allergy. Position paper of the Subcommittee on Insect Venom Allergy of the European Academy of Allergology and Clinical Immunology. *Allergy*. 1996;51(4):216-225.

1327. Sturm GJ, Herzog SA, Aberer W, et al. β-blockers and ACE inhibitors are not a risk factor for severe systemic sting reactions and adverse events during venom immunotherapy. *Allergy*. 2021;76(7):2166-2176.

1328. Bilò MB, Cichocka-Jarosz E, Pumphrey R, et al. Self-medication of anaphylactic reactions due to Hymenoptera stings-an EAACI Task Force Consensus Statement. *Allergy*. 2016;71(7):931-943.

1329. Kranert P, Forchhammer S, Volc S, Stenger F, Schaller M, Fischer J. Safety and Effectiveness of a 3-Day Rush Insect Venom Immunotherapy Protocol. *Int Arch Allergy Immunol.* 2020;181(2):111-118.

1330. Bonadonna P, Gonzalez-de-Olano D, Zanotti R, et al. Venom immunotherapy in patients with clonal mast cell disorders: efficacy, safety, and practical considerations. *J Allergy Clin Immunol Pract.* 2013;1(5):474-478.

1331. Quirce S, Bernstein JA. Old and new causes of occupational asthma. *Immunol Allergy Clin North Am.* 2011;31(4):677-698. v.

1332. Cartier A. New causes of immunologic occupational asthma, 2012-2014. *Curr Opin Allergy Clin Immunol.* 2015;15(2):117-123.

1333. Tarlo SM, Malo JL, de Blay F, et al. An Official American Thoracic Society Workshop Report: Presentations and Discussion of the Sixth Jack Pepys Workshop on Asthma in the Workplace. *Ann Am Thorac Soc.* 2017;14(9):1361-1372.

1334. Raulf M. Allergen component analysis as a tool in the diagnosis of occupational allergy. *Curr Opin Allergy Clin Immunol.* 2016;16(2):93-100.

1335. Raulf M, Quirce S, Vandenplas O. Addressing Molecular Diagnosis of Occupational Allergies. *Curr Allergy Asthma Rep.* 2018;18(1):6.

1336. Raulf M. Allergen component analysis as a tool in the diagnosis and management of occupational allergy. *Mol Immunol.* 2018;100:21-27.

1337. Raulf M. The latex story. *Chem Immunol Allergy*. 2014;100:248-255.

1338. Vandenplas O, Raulf M. Occupational Latex Allergy: the Current State of Affairs. *Curr Allergy Asthma Rep.* 2017;17(3):14.

1339. Raulf M. Current state of occupational latex allergy. *Curr Opin Allergy Clin Immunol.* 2020;20(2):112-116.

1340. Parisi CAS, Kelly KJ, Ansotegui RJ, et al. Update on latex allergy: New insights into an old problem. *World Allergy Organ J.* 2021;14(8):100569.

1341. Slater JE, Vedvick T, Arthur-Smith A, Trybul DE, Kekwick RG. Identification, cloning, and sequence of a major allergen (Hev b 5) from natural rubber latex (Hevea brasiliensis). *J Biol Chem.* 1996;271(41):25394-25399.

1342. Posch A, Chen Z, Raulf-Heimsoth M, Baur X. Latex allergens. *Clin Exp Allergy*. 1998;28(2):134-140.

1343. Raulf-Heimsoth M, Rihs HP, Rozynek P, et al. Quantitative analysis of immunoglobulin E reactivity profiles in patients allergic or sensitized to natural rubber latex (Hevea brasiliensis). *Clin Exp Allergy*. 2007;37(11):1657-1667.

1344. Vandenplas O, Froidure A, Meurer U, et al. The role of allergen components for the diagnosis of latex-induced occupational asthma. *Allergy*. 2016;71(6):840-849.

1345. Ebo DG, Hagendorrens MM, De Knop KJ, et al. Component-resolved diagnosis from latex allergy by microarray. *Clin Exp Allergy*. 2010;40(2):348-358.

1346. Peixinho C, Tavares-Ratado P, Tomás MR, Taborda-Barata L, Tomaz CT. Latex allergy: new insights to explain different sensitization profiles in different risk groups. *Br J Dermatol.* 2008;159(1):132-136.

1347. Wagner S, Breiteneder H. The latex-fruit syndrome. *Biochem Soc Trans.* 2002;30(Pt 6):935-940.

1348. Barre A, Culerrier R, Granier C, et al. Mapping of IgE-binding epitopes on the major latex allergen Hev b 2 and the cross-reacting 1,3beta-glucanase fruit allergens as a molecular basis for the latex-fruit syndrome. *Mol Immunol.* 2009;46(8-9):1595-1604.

1349. Chen Z, Posch A, Cremer R, Raulf-Heimsoth M, Baur X. Identification of hevein (Hev b 6.02) in Hevea latex as a major cross-reacting allergen with avocado fruit in patients with latex allergy. *J Allergy Clin Immunol.* 1998;102(3):476-481.

1350. Posch A, Wheeler CH, Chen Z, et al. Class I endochitinase containing a hevein domain is the causative allergen in latex-associated avocado allergy. *Clin Exp Allergy*. 1999;29(5):667-672.

1351. Raulf-Heimsoth M, Stark R, Sander I, et al. Anaphylactic reaction to apple juice containing acerola: cross-reactivity to latex due to prohevein. *J Allergy Clin Immunol.* 2002;109:715-716.

1352. Schmidt MHH, Raulf-Heimsoth M, Posch A. Evaluation of patatin as a major cross-reactive allergen in latex-induced potato allergy. *Ann Allergy Asthma Immunol.* 2002;89(6):613-618.

1353. Brandi SL, Poulsen LK, Garvey LH. The Clinical Relevance of Natural Rubber Latex-Specific IgE in Patients Sensitized to Timothy Grass Pollen. *Int Arch Allergy Immunol.* 2019;178(4): 345-354.

1354. Raulf-Heimsoth M, Kespohl S, Crespo JF, et al. Natural rubber latex and chestnut allergy: cross-reactivity or co-sensitization? *Allergy*. 2007;62(11):1277-1281.

1355. Rihs HP, Ruëff F, Lundberg M, et al. Relevance of the recombinant lipid transfer protein of Hevea brasiliensis: IgE-binding reactivity in fruit-allergic adults. *Ann Allergy Asthma Immunol.* 2006;97(5):643-649.

1356. Kespohl S, Schlünssen V, Jacobsen G, et al. Impact of cross-reactive carbohydrate determinants on wood dust sensitization. *Clin Exp Allergy*. 2010;40(7):1099-1106.

1357. Hemmer W, Altmann F, Holzweber F, Gruber C, Wantke F, Wöhrl S. ImmunoCAP cellulose displays cross-reactive carbohydrate determinant (CCD) epitopes and can cause false-positive test results in patients with high anti-CCD IgE antibody levels. *J Allergy Clin Immunol.* 2018;141(1):372-381.e373.

1358. Huss-Marp J, Raulf M, Jakob T. Spiking with recombinant allergens to improve allergen extracts: benefits and limitations for the use in routine diagnostics: Part 19 of the Series Molecular Allergology. *Allergo J Int.* 2015;24:236-243.

1359. Quirce S, Diaz-Perales A. Diagnosis and management of grain-induced asthma. *Allergy Asthma Immunol Res.* 2013;5(6):348-356.

1360. Brisman J. Baker's asthma. *Occup Environ Med.* 2002;59(7):498-502. quiz 502, 426.

1361. Sander I, Flagge A, Merget R, Halder TM, Meyer HE, Baur X. Identification of wheat flour allergens by means of 2-dimensional immunoblotting. *J Allergy Clin Immunol.* 2001;107(5):907-913.
Vespula Double Sensitization. *Int Arch Allergy Immunol.* 2018;177(4):365-369.

1322. Dalmau Duch G, Gázquez García V, Gaig Jané P, Galán Nieto A, Monsalve Clemente Rl. Importance of controlled sting challenge and component-resolved diagnosis in the success of venom immunotherapy. *J Investig Allergol Clin Immunol.* 2012;22(2):135-136.

1323. Korošč P, Šilar M, Eržen R, et al. Clinical routine utility of basophil activation testing for diagnosis of hymenoptera-allergic patients with emphasis on individuals with negative venom-specific IgE antibodies. *Int Arch Allergy Immunol.* 2013;161(4):363-368.

1324. Eberlein B, Krischan L, Darsow U, Ollert M, Ring J. Double positivity to bee and wasp venom: improved diagnostic procedure by recombinant allergen-based IgE testing and basophil activation test including data about cross-reactive carbohydrate determinants. *J Allergy Clin Immunol.* 2012;130(1):155-161.

1325. Peternelj A, Silar M, Erzen R, Kosnik M, Korosec P. Basophil sensitivity in patients not responding to venom immunotherapy. *Int Arch Allergy Immunol.* 2008;146(3):248-254.

1326. Ruëff F, Przybilla B, Müller U, Mosbech H. The sting challenge test in Hymenoptera venom allergy. Position paper of the Subcommittee on Insect Venom Allergy of the European Academy of Allergology and Clinical Immunology. *Allergy*. 1996;51(4):216-225.

1327. Sturm GJ, Herzog SA, Aberer W, et al. β-blockers and ACE inhibitors are not a risk factor for severe systemic sting reactions and adverse events during venom immunotherapy. *Allergy*. 2021;76(7):2166-2176.

1328. Bilò MB, Cichocka-Jarosz E, Pumphrey R, et al. Self-medication of anaphylactic reactions due to Hymenoptera stings-an EAACI Task Force Consensus Statement. *Allergy*. 2016;71(7):931-943.

1329. Kranert P, Forchhammer S, Volc S, Stenger F, Schaller M, Fischer J. Safety and Effectiveness of a 3-Day Rush Insect Venom Immunotherapy Protocol. *Int Arch Allergy Immunol.* 2020;181(2):111-118.

1330. Bonadonna P, Gonzalez-de-Olano D, Zanotti R, et al. Venom immunotherapy in patients with clonal mast cell disorders: efficacy, safety, and practical considerations. *J Allergy Clin Immunol Pract.* 2013;1(5):474-478.

1331. Quirce S, Bernstein JA. Old and new causes of occupational asthma. *Immunol Allergy Clin North Am.* 2011;31(4):677-698. v.

1332. Cartier A. New causes of immunologic occupational asthma, 2012-2014. *Curr Opin Allergy Clin Immunol.* 2015;15(2):117-123.

1333. Tarlo SM, Malo JL, de Blay F, et al. An Official American Thoracic Society Workshop Report: Presentations and Discussion of the Sixth Jack Pepys Workshop on Asthma in the Workplace. *Ann Am Thorac Soc.* 2017;14(9):1361-1372.

1334. Raulf M. Allergen component analysis as a tool in the diagnosis of occupational allergy. *Curr Opin Allergy Clin Immunol.* 2016;16(2):93-100.

1335. Raulf M, Quirce S, Vandenplas O. Addressing Molecular Diagnosis of Occupational Allergies. *Curr Allergy Asthma Rep.* 2018;18(1):6.

1336. Raulf M. Allergen component analysis as a tool in the diagnosis and management of occupational allergy. *Mol Immunol.* 2018;100:21-27.

1337. Raulf M. The latex story. *Chem Immunol Allergy*. 2014;100:248-255.

1338. Vandenplas O, Raulf M. Occupational Latex Allergy: the Current State of Affairs. *Curr Allergy Asthma Rep.* 2017;17(3):14.

1339. Raulf M. Current state of occupational latex allergy. *Curr Opin Allergy Clin Immunol.* 2020;20(2):112-116.

1340. Parisi CAS, Kelly KJ, Ansotegui RJ, et al. Update on latex allergy: New insights into an old problem. *World Allergy Organ J.* 2021;14(8):100569.

1341. Slater JE, Vedvick T, Arthur-Smith A, Trybul DE, Kekwick RG. Identification, cloning, and sequence of a major allergen (Hev b 5) from natural rubber latex (Hevea brasiliensis). *J Biol Chem.* 1996;271(41):25394-25399.

1342. Posch A, Chen Z, Raulf-Heimsoth M, Baur X. Latex allergens. *Clin Exp Allergy*. 1998;28(2):134-140.

1343. Raulf-Heimsoth M, Rihs HP, Rozynek P, et al. Quantitative analysis of immunoglobulin E reactivity profiles in patients allergic or sensitized to natural rubber latex (Hevea brasiliensis). *Clin Exp Allergy*. 2007;37(11):1657-1667.

1344. Vandenplas O, Froidure A, Meurer U, et al. The role of allergen components for the diagnosis of latex-induced occupational asthma. *Allergy*. 2016;71(6):840-849.

1345. Ebo DG, Hagendorrens MM, De Knop KJ, et al. Component-resolved diagnosis from latex allergy by microarray. *Clin Exp Allergy*. 2010;40(2):348-358.

1346. Peixinho C, Tavares-Ratado P, Tomás MR, Taborda-Barata L, Tomaz CT. Latex allergy: new insights to explain different sensitization profiles in different risk groups. *Br J Dermatol.* 2008;159(1):132-136.

1347. Wagner S, Breiteneder H. The latex-fruit syndrome. *Biochem Soc Trans.* 2002;30(Pt 6):935-940.

1348. Barre A, Culerrier R, Granier C, et al. Mapping of IgE-binding epitopes on the major latex allergen Hev b 2 and the cross-reacting 1,3beta-glucanase fruit allergens as a molecular basis for the latex-fruit syndrome. *Mol Immunol.* 2009;46(8-9):1595-1604.

1349. Chen Z, Posch A, Cremer R, Raulf-Heimsoth M, Baur X. Identification of hevein (Hev b 6.02) in Hevea latex as a major cross-reacting allergen with avocado fruit in patients with latex allergy. *J Allergy Clin Immunol.* 1998;102(3):476-481.

1350. Posch A, Wheeler CH, Chen Z, et al. Class I endochitinase containing a hevein domain is the causative allergen in latex-associated avocado allergy. *Clin Exp Allergy*. 1999;29(5):667-672.

1351. Raulf-Heimsoth M, Stark R, Sander I, et al. Anaphylactic reaction to apple juice containing acerola: cross-reactivity to latex due to prohevein. *J Allergy Clin Immunol.* 2002;109:715-716.

1352. Schmidt MHH, Raulf-Heimsoth M, Posch A. Evaluation of patatin as a major cross-reactive allergen in latex-induced potato allergy. *Ann Allergy Asthma Immunol.* 2002;89(6):613-618.

1353. Brandi SL, Poulsen LK, Garvey LH. The Clinical Relevance of Natural Rubber Latex-Specific IgE in Patients Sensitized to Timothy Grass Pollen. *Int Arch Allergy Immunol.* 2019;178(4): 345-354.

1354. Raulf-Heimsoth M, Kespohl S, Crespo JF, et al. Natural rubber latex and chestnut allergy: cross-reactivity or co-sensitization? *Allergy*. 2007;62(11):1277-1281.

1355. Rihs HP, Ruëff F, Lundberg M, et al. Relevance of the recombinant lipid transfer protein of Hevea brasiliensis: IgE-binding reactivity in fruit-allergic adults. *Ann Allergy Asthma Immunol.* 2006;97(5):643-649.

1356. Kespohl S, Schlünssen V, Jacobsen G, et al. Impact of cross-reactive carbohydrate determinants on wood dust sensitization. *Clin Exp Allergy*. 2010;40(7):1099-1106.

1357. Hemmer W, Altmann F, Holzweber F, Gruber C, Wantke F, Wöhrl S. ImmunoCAP cellulose displays cross-reactive carbohydrate determinant (CCD) epitopes and can cause false-positive test results in patients with high anti-CCD IgE antibody levels. *J Allergy Clin Immunol.* 2018;141(1):372-381.e373.

1358. Huss-Marp J, Raulf M, Jakob T. Spiking with recombinant allergens to improve allergen extracts: benefits and limitations for the use in routine diagnostics: Part 19 of the Series Molecular Allergology. *Allergo J Int.* 2015;24:236-243.

1359. Quirce S, Diaz-Perales A. Diagnosis and management of grain-induced asthma. *Allergy Asthma Immunol Res.* 2013;5(6):348-356.

1360. Brisman J. Baker's asthma. *Occup Environ Med.* 2002;59(7):498-502. quiz 502, 426.

1361. Sander I, Flagge A, Merget R, Halder TM, Meyer HE, Baur X. Identification of wheat flour allergens by means of 2-dimensional immunoblotting. *J Allergy Clin Immunol.* 2001;107(5):907-913.
1362. van Kampen V, de Blay F, Folletti I, et al. Evaluation of commer-
cial skin prick test solutions for selected occupational allergens.
*Allergy*. 2013;68(5):651-658.

1363. van Kampen V, de Blay F, Folletti I, et al. EAACI position paper: skin prick testing in the diagnosis of occupational type I allergies. *Allergy*. 2013;68(5):580-584.

1364. Olivieri M, Biscardo CA, Palazzo P, et al. Wheat IgE profiling and wheat IgE levels in bakers with allergic occupational phenotypes. *Occup Environ Med*. 2013;70(9):617-622.

1365. Gómez-Casado C, Garrido-Arandia M, Pereira C, et al. Component-resolved diagnosis of wheat flour allergy in baker's asthma. *J Allergy Clin Immunol*. 2014;134(2):480-483.

1366. Sander I, Rihs HP, Brüning T, Raulf M. A further wheat al-
lergen for baker's asthma: Tri a 40. *J Allergy Clin Immunol.*
2016;137(4):1286.

1367. Sussman GL, Beezhold DH, Cohn JR, Silvers WS, Zeiger JS, Nayak AP. Cannabis: An Emerging Occupational Allergen? *Ann Work Expo Health*. 2020;64(7):679-682.

1368. Decuyper II, Van Gasse A, Faber MA, et al. Occupational cannabis exposure and allergy risks. *Occup Environ Med*. 2019;76(2):78-82.

1369. Decuyper II, Faber MA, Lapeere H, et al. Cannabis allergy: A diag-
nostic challenge. *Allergy*. 2018;73(9):1911-1914.

1370. Quirce S, Polo F, Figueredo E, González R, Sastre J. Occupational asthma caused by soybean flour in bakers–differences with soybean-induced epidemic asthma. *Clin Exp Allergy*. 2000;30(6):839-846.

1371. Peters U, Frenzel K, Brettschneider R, Oldenburg M, Bittner C. Identification of two metallothioneins as novel inhalative coffee allergens cof a 2 and cof a 3. *PLoS One*. 2015;10(5):e0126455.

1372. Kespohl S, Kotschy-Lang N, Tomm JM, et al. Occupational IgE-mediated softwood allergy: characterization of the causative allergen. *Int Arch Allergy Immunol*. 2012;157(2):202-208.

1373. Kespohl S, Sander I, Merget R, et al. Identification of an obeche (Triplochiton scleroxylon) wood allergen as a class I chitinase. *Allergy*. 2005;60(6):808-814.

1374. Hannu T, Lindström I, Palmroos P, Kuuliala O, Sauni R. Prediction of obeche wood-induced asthma by specific skin prick testing. *Occup Med (Lond)*. 2013;63(6):429-431.

1375. Aranda A, Campo P, Palacin A, et al. Antigenic proteins involved in occupational rhinitis and asthma caused by obeche wood (Triplochiton scleroxylon). *PLoS One*. 2013;8(1):e53926.

1376. Zahradnik E, Raulf M. Animal allergens and their presence in the environment. *Front Immunol*. 2014;5:76.

1377. Caballero ML, Ordaz E, Bermejo M, et al. Characterization of oc-
cupational sensitization by multiallergen immunoblotting in work-
ers exposed to laboratory animals. *Ann Allergy Asthma Immunol*.
2012;108(3):178-181.

1378. Choi GS, Kim JH, Lee HN, Sung JM, Lee JW, Park HS. Occupational asthma caused by inhalation of bovine serum albumin powder. *Allergy Asthma Immunol Res*. 2009;1(1):45-47.

1379. Toskala E, Piipari R, Aalto-Korte K, Tuppurainen M, Kuuliala O, Keskinen H. Occupational asthma and rhinitis caused by milk proteins. *J Occup Environ Med*. 2004;46:1100-1101.

1380. Bernaola G, Echechipía S, Urrutia I, Fernández E, Audícana M. Fernández de Corres L. Occupational asthma and rhinoconjunctivitis from inhalation of dried cow's milk caused by sensitization to alpha-lactalbumin. *Allergy*. 1994;49(3):189-191.

1381. Olaguibel JM, Hernandez D, Morales P, Peris A, Basomba A. Occupational asthma caused by inhalation of casein. *Allergy*. 1990;45(4):306-308.

1382. Lopata AL, Kleine-Tebbe J, Kamath SD. Allergens and molecular diagnostics of shellfish allergy: Part 22 of the Series Molecular Allergology. *Allergo J Int*. 2016;25(7):210-218.

1383. Wilfinger D, Kuehn A, Takacs S, Galli-Novak E, Machan B, Aberer W. Occupational allergic contact urticaria to tropomyosin from squid. *Allergol Select*. 2020;4:129-134.

1384. Siracusa A, Folletti I. Gerth van Wijk R, et al. Occupational ana-
phylaxis-an EAACI task force consensus statement. *Allergy*.
2015;70(2):141-152.

1385. Larsen AI, Cederkvist L, Lykke AM, Wagner P, Johnsen CR, Poulsen LK. Allergy Development in Adulthood: An Occupational Cohort Study of the Manufacturing of Industrial Enzymes. *J Allergy Clin Immunol Pract*. 2020;8(1):210-218.e215.

1386. Kespohl S, Raulf M. Mould allergens: Where do we stand with molecular allergy diagnostics?: Part 13 of the series Molecular Allergology. *Allergo J Int*. 2014;23(4):120-125.

1387. Kespohl S, Maryska S, Bünger J, et al. How to diagnose mould al-
lergy? Comparison of skin prick tests with specific IgE results. *Clin
Exp Allergy*. 2016;46(7):981-991.

1388. Allmers H, Huber H, Baur X. Two year follow-up of a garbage collector with allergic bronchopulmonary aspergillosis (ABPA). Am J Ind Med. 2000;37(4):438-442.

1389. Poole CJ, Wong M. Allergic bronchopulmonary aspergillosis in garden waste (compost) collectors-occupational implications. *Occup Med (Lond)*. 2013;63(7):517-519.

1390. Preisser AM, Koschel D, Merget R, Nowak D, Raulf M, Heidrich J. Workplace-related inhalation test - Specific inhalation challenge: S2k Guideline of the German Society for Occupational and Environmental Medicine e.V. (DGAUM), the German Society for Pneumology and Respiratory Medicine e.V. (DGP) and the German Society for Allergology and Clinical Immunology e.V. (DGAKI). *Allergol Select*. 2021;5:315-334.

1391. Raulf M. Occupational Respiratory Allergy: Risk Factors, Diagnosis, and Management. *Handb Exp Pharmacol*. 2022;268:213-225.

1392. van Kampen V, Rabstein S, Sander I, et al. Prediction of challenge test results by flour-specific IgE and skin prick test in symptomatic bakers. *Allergy*. 2008;63(7):897-902.

1393. Witke W. The role of profilin complexes in cell motility and other cellular processes. *Trends Cell Biol*. 2004;14(8):461-469.

1394. Valenta R, Duchene M, Ebner C, et al. Profilins constitute a novel family of functional plant pan-allergens. *J Exp Med*. 1992;175(2):377-385.

1395. Mari A. Multiple pollen sensitization: a molecular approach to the diagnosis. *Int Arch Allergy Immunol*. 2001;125(1):57-65.

1396. Núñez R, Carballada F, Lombardero M, Jimeno L, Boquete M. Profilin as an aeroallergen by means of conjunctival allergen challenge with purified date palm profilin. *Int Arch Allergy Immunol*. 2012;158(2):115-119.

1397. Ruiz-García M, García Del Potro M, Fernández-Nieto M, Barber D, Jimeno-Nogales L, Sastre J. Profilin: a relevant aeroallergen? *J Allergy Clin Immunol*. 2011;128:416-418.

1398. Asero R, Villalta D. Profilin may be a primary airborne sensitizer: a case report. *J Investig Allergol Clin Immunol*. 2013;23(2):134-135.

1399. Ruiz-Hornillos J, López-Matas MA, Berges Jimeno P, et al. Profilin is a marker of severity in allergic respiratory diseases. *Allergy*. 2020;75(4):853-861.

1400. Wensing M, Akkerdaas JH, van Leeuwen WA, et al. IgE to Bet v 1 and profilin: cross-reactivity patterns and clinical relevance. *J Allergy Clin Immunol*. 2002;110(3):435-442.

1401. Reindl J, Rihs HP, Scheurer S, Wangorsch A, Haustein D, Vieths S. IgE reactivity to profilin in pollen-sensitized subjects with adverse reactions to banana and pineapple. *Int Arch Allergy Immunol*. 2002;128(2):105-114.

1402. Rodriguez-Perez R, Crespo JF, Rodríguez J, Salcedo G. Profilin is a relevant melon allergen susceptible to pepsin digestion in patients with oral allergy syndrome. *J Allergy Clin Immunol*. 2003;111(3):634-639.

1403. Westphal S, Kempf W, Foetisch K, Retzek M, Vieths S, Scheurer S. Tomato profilin Lyc e 1: IgE cross-reactivity and allergenic potency. *Allergy*. 2004;59(5):526-532.

1404. Anliker MD, Reindl J, Vieths S, Wüthrich B. Allergy caused by in-
gestion of persimmon (Diospyros kaki): detection of specific IgE
1362. van Kampen V, de Blay F, Folletti I, et al. Evaluation of commer-
cial skin prick test solutions for selected occupational allergens.
*Allergy*. 2013;68(5):651-658.

1363. van Kampen V, de Blay F, Folletti I, et al. EAACI position paper: skin prick testing in the diagnosis of occupational type I allergies. *Allergy*. 2013;68(5):580-584.

1364. Olivieri M, Biscardo CA, Palazzo P, et al. Wheat IgE profiling and wheat IgE levels in bakers with allergic occupational phenotypes. *Occup Environ Med*. 2013;70(9):617-622.

1365. Gómez-Casado C, Garrido-Arandia M, Pereira C, et al. Component-resolved diagnosis of wheat flour allergy in baker's asthma. *J Allergy Clin Immunol*. 2014;134(2):480-483.

1366. Sander I, Rihs HP, Brüning T, Raulf M. A further wheat al-
lergen for baker's asthma: Tri a 40. *J Allergy Clin Immunol.*
2016;137(4):1286.

1367. Sussman GL, Beezhold DH, Cohn JR, Silvers WS, Zeiger JS, Nayak AP. Cannabis: An Emerging Occupational Allergen? *Ann Work Expo Health*. 2020;64(7):679-682.

1368. Decuyper II, Van Gasse A, Faber MA, et al. Occupational cannabis exposure and allergy risks. *Occup Environ Med*. 2019;76(2):78-82.

1369. Decuyper II, Faber MA, Lapeere H, et al. Cannabis allergy: A diag-
nostic challenge. *Allergy*. 2018;73(9):1911-1914.

1370. Quirce S, Polo F, Figueredo E, González R, Sastre J. Occupational asthma caused by soybean flour in bakers-differences with soybean-induced epidemic asthma. *Clin Exp Allergy*. 2000;30(6):839-846.

1371. Peters U, Frenzel K, Brettschneider R, Oldenburg M, Bittner C. Identification of two metallothioneins as novel inhalative coffee allergens cof a 2 and cof a 3. *PLoS One*. 2015;10(5):e0126455.

1372. Kespohl S, Kotschy-Lang N, Tomm JM, et al. Occupational IgE-mediated softwood allergy: characterization of the causative allergen. *Int Arch Allergy Immunol*. 2012;157(2):202-208.

1373. Kespohl S, Sander I, Merget R, et al. Identification of an obeche (Triplochiton scleroxylon) wood allergen as a class I chitinase. *Allergy*. 2005;60(6):808-814.

1374. Hannu T, Lindström I, Palmroos P, Kuuliala O, Sauni R. Prediction of obeche wood-induced asthma by specific skin prick testing. *Occup Med (Lond)*. 2013;63(6):429-431.

1375. Aranda A, Campo P, Palacin A, et al. Antigenic proteins involved in occupational rhinitis and asthma caused by obeche wood (Triplochiton scleroxylon). *PLoS One*. 2013;8(1):e53926.

1376. Zahradnik E, Raulf M. Animal allergens and their presence in the environment. *Front Immunol*. 2014;5:76.

1377. Caballero ML, Ordaz E, Bermejo M, et al. Characterization of oc-
cupational sensitization by multiallergen immunoblotting in work-
ers exposed to laboratory animals. *Ann Allergy Asthma Immunol*.
2012;108(3):178-181.

1378. Choi GS, Kim JH, Lee HN, Sung JM, Lee JW, Park HS. Occupational asthma caused by inhalation of bovine serum albumin powder. *Allergy Asthma Immunol Res*. 2009;1(1):45-47.

1379. Toskala E, Piipari R, Aalto-Korte K, Tuppurainen M, Kuuliala O, Keskinen H. Occupational asthma and rhinitis caused by milk proteins. *J Occup Environ Med*. 2004;46:1100-1101.

1380. Bernaola G, Echechipía S, Urrutia I, Fernández E, Audícana M. Fernández de Corres L. Occupational asthma and rhinoconjunctivitis from inhalation of dried cow's milk caused by sensitization to alpha-lactalbumin. *Allergy*. 1994;49(3):189-191.

1381. Olaguibel JM, Hernandez D, Morales P, Peris A, Basomba A. Occupational asthma caused by inhalation of casein. *Allergy*. 1990;45(4):306-308.

1382. Lopata AL, Kleine-Tebbe J, Kamath SD. Allergens and molecular diagnostics of shellfish allergy: Part 22 of the Series Molecular Allergology. *Allergo J Int*. 2016;25(7):210-218.

1383. Wilfinger D, Kuehn A, Takacs S, Galli-Novak E, Machan B, Aberer W. Occupational allergic contact urticaria to tropomyosin from squid. *Allergol Select*. 2020;4:129-134.

1384. Siracusa A, Folletti I. Gerth van Wijk R, et al. Occupational ana-
phylaxis-an EAACI task force consensus statement. *Allergy*.
2015;70(2):141-152.

1385. Larsen AI, Cederkvist L, Lykke AM, Wagner P, Johnsen CR, Poulsen LK. Allergy Development in Adulthood: An Occupational Cohort Study of the Manufacturing of Industrial Enzymes. *J Allergy Clin Immunol Pract*. 2020;8(1):210-218.e215.

1386. Kespohl S, Raulf M. Mould allergens: Where do we stand with molecular allergy diagnostics?: Part 13 of the series Molecular Allergology. *Allergo J Int*. 2014;23(4):120-125.

1387. Kespohl S, Maryska S, Bünger J, et al. How to diagnose mould al-
lergy? Comparison of skin prick tests with specific IgE results. *Clin
Exp Allergy*. 2016;46(7):981-991.

1388. Allmers H, Huber H, Baur X. Two year follow-up of a garbage collector with allergic bronchopulmonary aspergillosis (ABPA). Am J Ind Med. 2000;37(4):438-442.

1389. Poole CJ, Wong M. Allergic bronchopulmonary aspergillosis in garden waste (compost) collectors-occupational implications. *Occup Med (Lond)*. 2013;63(7):517-519.

1390. Preisser AM, Koschel D, Merget R, Nowak D, Raulf M, Heidrich J. Workplace-related inhalation test - Specific inhalation challenge: S2k Guideline of the German Society for Occupational and Environmental Medicine e.V. (DGAUM), the German Society for Pneumology and Respiratory Medicine e.V. (DGP) and the German Society for Allergology and Clinical Immunology e.V. (DGAKI). *Allergol Select*. 2021;5:315-334.

1391. Raulf M. Occupational Respiratory Allergy: Risk Factors, Diagnosis, and Management. *Handb Exp Pharmacol*. 2022;268:213-225.

1392. van Kampen V, Rabstein S, Sander I, et al. Prediction of challenge test results by flour-specific IgE and skin prick test in symptomatic bakers. *Allergy*. 2008;63(7):897-902.

1393. Witke W. The role of profilin complexes in cell motility and other cellular processes. *Trends Cell Biol*. 2004;14(8):461-469.

1394. Valenta R, Duchene M, Ebner C, et al. Profilins constitute a novel family of functional plant pan-allergens. *J Exp Med*. 1992;175(2):377-385.

1395. Mari A. Multiple pollen sensitization: a molecular approach to the diagnosis. *Int Arch Allergy Immunol*. 2001;125(1):57-65.

1396. Núñez R, Carballada F, Lombardero M, Jimeno L, Boquete M. Profilin as an aeroallergen by means of conjunctival allergen challenge with purified date palm profilin. *Int Arch Allergy Immunol*. 2012;158(2):115-119.

1397. Ruiz-García M, García Del Potro M, Fernández-Nieto M, Barber D, Jimeno-Nogales L, Sastre J. Profilin: a relevant aeroallergen? *J Allergy Clin Immunol*. 2011;128:416-418.

1398. Asero R, Villalta D. Profilin may be a primary airborne sensitizer: a case report. *J Investig Allergol Clin Immunol*. 2013;23(2):134-135.

1399. Ruiz-Hornillos J, López-Matas MA, Berges Jimeno P, et al. Profilin is a marker of severity in allergic respiratory diseases. *Allergy*. 2020;75(4):853-861.

1400. Wensing M, Akkerdaas JH, van Leeuwen WA, et al. IgE to Bet v 1 and profilin: cross-reactivity patterns and clinical relevance. *J Allergy Clin Immunol*. 2002;110(3):435-442.

1401. Reindl J, Rihs HP, Scheurer S, Wangorsch A, Haustein D, Vieths S. IgE reactivity to profilin in pollen-sensitized subjects with adverse reactions to banana and pineapple. *Int Arch Allergy Immunol*. 2002;128(2):105-114.

1402. Rodriguez-Perez R, Crespo JF, Rodríguez J, Salcedo G. Profilin is a relevant melon allergen susceptible to pepsin digestion in patients with oral allergy syndrome. *J Allergy Clin Immunol*. 2003;111(3):634-639.

1403. Westphal S, Kempf W, Foetisch K, Retzek M, Vieths S, Scheurer S. Tomato profilin Lyc e 1: IgE cross-reactivity and allergenic potency. *Allergy*. 2004;59(5):526-532.

1404. Anliker MD, Reindl J, Vieths S, Wüthrich B. Allergy caused by in-
gestion of persimmon (Diospyros kaki): detection of specific IgE
and cross-reactivity to profilin and carbohydrate determinants. *J Allergy Clin Immunol.* 2001;107(4):718-723.

1405. Reindl J, Anliker MD, Karamloo F, Vieths S, Wüthrich B. Allergy caused by ingestion of zucchini (Cucurbita pepo): characterization of allergens and cross-reactivity to pollen and other foods. *J Allergy Clin Immunol.* 2000;106(2):379-385.

1406. Asero R, Mistrello G, Amato S. The nature of melon allergy in ragweed-allergic subjects: A study of 1000 patients. *Allergy Asthma Proc.* 2011;32(1):64-67.

1407. Palacin A, Quirce S, Sanchez-Monge R, et al. Sensitization profiles to purified plant food allergens among pediatric patients with allergy to banana. *Pediatr Allergy Immunol.* 2011;22(2):186-195.

1408. Alvarado MI, Jimeno L, De La Torre F, et al. Profilin as a severe food allergen in allergic patients overexposed to grass pollen. *Allergy.* 2014;69(12):1610-1616.

1409. Kapingidza AB, Pye SE, Hyduke N, et al. Comparative structural and thermal stability studies of Cuc m 2.0101, Art v 4.0101 and other allergenic profilins. *Mol Immunol.* 2019;114:19-29.

1410. Quercia O, Stefaniini GF, Scardovi A, Asero R. Patients monosen- sitised to Hev b 8 (Hevea brasiliensis latex profilin) may safely un- dergo major surgery in a normal (non-latex safe) environment. *Eur Ann Allergy Clin Immunol.* 2009;41(4):112-116.

1411. Schuler S, Ferrari G, Schmid-Grendelmeier P, Harr T. Microarray- based component-resolved diagnosis of latex allergy: isolated IgE-mediated sensitization to latexprofilin Hev b8 may act as con- founder. *Clin Transl Allergy.* 2013;3(1):11.

1412. Asero R. Hypersensitivity to pollen panallergens (profilin and polcalcin) detected *in vitro* and *in vivo*: a comparative analysis. *J Investig Allergol Clin Immunol.* 2011;21(4):323-324.

1413. Villalta D, Asero R. Sensitization to the pollen pan-allergen profilin. Is the detection of immunoglobulin E to multiple homologous pro- teins from different sources clinically useful? *J Investig Allergol Clin Immunol.* 2010;20(7):591-595.

1414. Asero R, Villalta D. Are anti-Phl p 12 IgE levels predictive of oral al- lergy syndrome in profilin hypersensitive patients? *Eur Ann Allergy Clin Immunol.* 2011;43(6):184-187.

1415. Ganglberger E, Radauer C, Wagner S, et al. Hev b 8, the Hevea brasiliensis latex profilin, is a cross-reactive allergen of latex, plant foods and pollen. *Int Arch Allergy Immunol.* 2001;125(3): 216-227.

1416. Sirvent S, Tordesillas L, Villalba M, et al. Pollen and plant food pro- filin allergens show equivalent IgE reactivity. *Ann Allergy Asthma Immunol.* 2011;106(5):429-435.

1417. Asero R, Mistrello G, Roncarolo D, Amato S. Parietaria profilin shows only limited cross-reactivity with birch and grass profilins. *Int Arch Allergy Immunol.* 2004;133(2):121-124.

1418. Bonura A, Trapani A, Gulino L, et al. Cloning, expression in *E. coli* and immunological characterization of Par j 3.0201, a Parietaria pollen profilin variant. *Mol Immunol.* 2014;57(2):220-225.

1419. Scala E, Abeni D, Guerra EC, et al. Cosensitization to profilin is as- sociated with less severe reactions to foods in nsLTPs and storage proteins reactors and with less severe respiratory allergy. *Allergy.* 2018;73(9):1921-1923.

1420. Kelso JM, Jones RT, Tellez R, Yunginger JW. Oral allergy syndrome successfully treated with pollen immunotherapy. *Ann Allergy Asthma Immunol.* 1995;74(5):391-396.

1421. Asero R, Mistrello G, Amato S. Detection of pan-allergens in com- mercial pollen extracts for allergen immunotherapy. *Ann Allergy Asthma Immunol.* 2016;117(2):180-185.

1422. Obeso D, Mera-Berriatua L, Rodríguez-Coira J, et al. Multi-omics analysis points to altered platelet functions in severe food- associated respiratory allergy. *Allergy.* 2018;73(11):2137-2149.

1423. Lund G, Brand S, Ramos T, et al. Strong and frequent T-cell re- sponses to the minor allergen Phl p 12 in Spanish patients IgE- sensitized to Profilins. *Allergy.* 2018;73(5):1013-1021.

1424. Barber D, Villaseñor A, Escribese MM. Metabolomics strategies to discover new biomarkers associated to severe allergic phenotypes. *Asia Pac Allergy.* 2019;9(4):e37.

1425. Breiteneder H, Pettenburger K, Bito A, et al. The gene coding for the major birch pollen allergen Betv1, is highly homologous to a pea disease resistance response gene. *EMBO J.* 1989;8(7):1935-1938.

1426. Gajhede M, Osmark P, Poulsen FM, et al. X-ray and NMR struc- ture of Bet v 1, the origin of birch pollen allergy. *Nat Struct Biol.* 1996;3(12):1040-1045.

1427. Jahn-Schmid B, Radakovics A, Lüttkopf D, et al. Bet v 1142-156 is the dominant T-cell epitope of the major birch pollen allergen and important for cross-reactivity with Bet v 1-related food allergens. *J Allergy Clin Immunol.* 2005;116(1):213-219.

1428. Kitzmüller C, Zulehner N, Roulias A, et al. Correlation of sensitizing capacity and T-cell recognition within the Bet v 1 family. *J Allergy Clin Immunol.* 2015;136(1):151-158.

1429. Gepp B, Lengger N, Dublin M, Hemmer W, Breiteneder H, Radauer C. Chimeras of Bet v 1 and Api g 1 reveal heterogeneous IgE re- sponses in patients with birch pollen allergy. *J Allergy Clin Immunol.* 2014;134(1):188-194.

1430. Antoniw JFRC, Pierpoints WS, et al. Comparison of three pathogenesis-related proteins from plants of two cultivars of tobacco infected with TMV. *J Gen Virol.* 1980;47:79-87. doi:10.1099/0022-1317-47-1-79

1431. Ali S, Ganai BA, Kamili AN, et al. Pathogenesis-related proteins and peptides as promising tools for engineering plants with multiple stress tolerance. *Microbiol Res.* 2018;212-213:29-37.

1432. Geroldinger-Simic M, Zelniker T, Aberer W, et al. Birch pollen- related food allergy: clinical aspects and the role of allergen- specific IgE and IgG4 antibodies. *J Allergy Clin Immunol.* 2011;127(3):616-622.

1433. Hauser M, Asam C, Himly M, et al. Bet v 1-like pollen allergens of multiple Fagales species can sensitize atopic individuals. *Clin Exp Allergy.* 2011;41(12):1804-1814.

1434. Breiteneder H, Ebner C. Molecular and biochemical classification of plant-derived food allergens. *J Allergy Clin Immunol.* 2000;106(1 Pt 1):27-36.

1435. Moneo I, Gómez M, Sánchez-Monge R, et al. Lack of crossreaction with Bet v 1 in patients sensitized to Dau c 1, a carrot allergen. *Ann Allergy Asthma Immunol.* 1999;83(1):71-75.

1436. Ballmer-Weber BK, Wüthrich B, Wangorsch A, Fötisch K, Altmann F, Vieths S. Carrot allergy: double-blinded, placebo-controlled food challenge and identification of allergens. *J Allergy Clin Immunol.* 2001;108(2):301-307.

1437. Moreno-Ancillo A, Gil-Adrados AC, Domínguez-Noche C, Cosmes PM, Pineda F. Occupational asthma due to carrot in a cook. *Allergol Immunopathol (Madr).* 2005;33(5):288-290.

1438. Flinterman AE, Akkerdaas JH, den Hartog Jager CF, et al. Lipid transfer protein-linked hazelnut allergy in children from a non- Mediterranean birch-endemic area. *J Allergy Clin Immunol.* 2008;121(2):423-428.

1439. Aglas L, Soh WT, Kraiem A, Wenger M, Brandstetter H, Ferreira F. Ligand binding of PR-10 proteins with a particular focus on the Bet v 1 allergen family. *Curr Allergy Asthma Rep.* 2020;20(7):25.

1440. Jacob T, von Loetzen CS, Reuter A, et al. Identification of a natural ligand of the hazel allergen Cor a 1. *Sci Rep.* 2019;9(1):8714.

1441. Seutter von Loetzen C, Jacob T, Hartl-Spiegelhauer O, et al. Ligand recognition of the major birch pollen allergen bet v 1 is isoform dependent. *PLoS One.* 2015;10(6):e0128677.

1442. Casañal A, Zander U, Muñoz C, et al. The strawberry pathogenesis-related 10 (PR-10) Fra a proteins control flavonoid biosynthesis by binding to metabolic intermediates. *J Biol Chem.* 2013;288(49):35322-35332.

1443. Mogensen JE, Wimmer R, Larsen JN, Spangfort MD, Otzen DE. The major birch allergen, Bet v 1, shows
and cross-reactivity to profilin and carbohydrate determinants. *J Allergy Clin Immunol.* 2001;107(4):718-723.

1405. Reindl J, Anliker MD, Karamloo F, Vieths S, Wüthrich B. Allergy caused by ingestion of zucchini (Cucurbita pepo): characterization of allergens and cross-reactivity to pollen and other foods. *J Allergy Clin Immunol.* 2000;106(2):379-385.

1406. Asero R, Mistrello G, Amato S. The nature of melon allergy in ragweed-allergic subjects: A study of 1000 patients. *Allergy Asthma Proc.* 2011;32(1):64-67.

1407. Palacin A, Quirce S, Sanchez-Monge R, et al. Sensitization profiles to purified plant food allergens among pediatric patients with allergy to banana. *Pediatr Allergy Immunol.* 2011;22(2):186-195.

1408. Alvarado MI, Jimeno L, De La Torre F, et al. Profilin as a severe food allergen in allergic patients overexposed to grass pollen. *Allergy.* 2014;69(12):1610-1616.

1409. Kapingidza AB, Pye SE, Hyduke N, et al. Comparative structural and thermal stability studies of Cuc m 2.0101, Art v 4.0101 and other allergenic profilins. *Mol Immunol.* 2019;114:19-29.

1410. Quercia O, Stefaniini GF, Scardovi A, Asero R. Patients monosen- sitised to Hev b 8 (Hevea brasiliensis latex profilin) may safely un- dergo major surgery in a normal (non-latex safe) environment. *Eur Ann Allergy Clin Immunol.* 2009;41(4):112-116.

1411. Schuler S, Ferrari G, Schmid-Grendelmeier P, Harr T. Microarray- based component-resolved diagnosis of latex allergy: isolated IgE-mediated sensitization to latexprofilin Hev b8 may act as con- founder. *Clin Transl Allergy.* 2013;3(1):11.

1412. Asero R. Hypersensitivity to pollen panallergens (profilin and polcalcin) detected *in vitro* and *in vivo*: a comparative analysis. *J Investig Allergol Clin Immunol.* 2011;21(4):323-324.

1413. Villalta D, Asero R. Sensitization to the pollen pan-allergen profilin. Is the detection of immunoglobulin E to multiple homologous proteins from different sources clinically useful? *J Investig Allergol Clin Immunol.* 2010;20(7):591-595.

1414. Asero R, Villalta D. Are anti-Phl p 12 IgE levels predictive of oral al- lergy syndrome in profilin hypersensitive patients? *Eur Ann Allergy Clin Immunol.* 2011;43(6):184-187.

1415. Ganglberger E, Radauer C, Wagner S, et al. Hev b 8, the Hevea brasiliensis latex profilin, is a cross-reactive allergen of latex, plant foods and pollen. *Int Arch Allergy Immunol.* 2001;125(3): 216-227.

1416. Sirvent S, Tordesillas L, Villalba M, et al. Pollen and plant food pro- filin allergens show equivalent IgE reactivity. *Ann Allergy Asthma Immunol.* 2011;106(5):429-435.

1417. Asero R, Mistrello G, Roncarolo D, Amato S. Parietaria profilin shows only limited cross-reactivity with birch and grass profilins. *Int Arch Allergy Immunol.* 2004;133(2):121-124.

1418. Bonura A, Trapani A, Gulino L, et al. Cloning, expression in *E. coli* and immunological characterization of Par j 3.0201, a Parietaria pollen profilin variant. *Mol Immunol.* 2014;57(2):220-225.

1419. Scala E, Abeni D, Guerra EC, et al. Cosensitization to profilin is as- sociated with less severe reactions to foods in nsLTPs and storage proteins reactors and with less severe respiratory allergy. *Allergy.* 2018;73(9):1921-1923.

1420. Kelso JM, Jones RT, Tellez R, Yunginger JW. Oral allergy syndrome successfully treated with pollen immunotherapy. *Ann Allergy Asthma Immunol.* 1995;74(5):391-396.

1421. Asero R, Mistrello G, Amato S. Detection of pan-allergens in com- mercial pollen extracts for allergen immunotherapy. *Ann Allergy Asthma Immunol.* 2016;117(2):180-185.

1422. Obeso D, Mera-Berriatua L, Rodríguez-Coira J, et al. Multi-omics analysis points to altered platelet functions in severe food- associated respiratory allergy. *Allergy.* 2018;73(11):2137-2149.

1423. Lund G, Brand S, Ramos T, et al. Strong and frequent T-cell re- sponses to the minor allergen Phl p 12 in Spanish patients IgE- sensitized to Profilins. *Allergy.* 2018;73(5):1013-1021.

1424. Barber D, Villaseñor A, Escribese MM. Metabolomics strategies to discover new biomarkers associated to severe allergic phenotypes. *Asia Pac Allergy.* 2019;9(4):e37.

1425. Breiteneder H, Pettenburger K, Bito A, et al. The gene coding for the major birch pollen allergen Betv1, is highly homologous to a pea disease resistance response gene. *EMBO J.* 1989;8(7):1935-1938.

1426. Gajhede M, Osmark P, Poulsen FM, et al. X-ray and NMR struc- ture of Bet v 1, the origin of birch pollen allergy. *Nat Struct Biol.* 1996;3(12):1040-1045.

1427. Jahn-Schmid B, Radakovics A, Lüttkopf D, et al. Bet v 1142-156 is the dominant T-cell epitope of the major birch pollen allergen and important for cross-reactivity with Bet v 1-related food allergens. *J Allergy Clin Immunol.* 2005;116(1):213-219.

1428. Kitzmüller C, Zulehner N, Roulias A, et al. Correlation of sensitizing capacity and T-cell recognition within the Bet v 1 family. *J Allergy Clin Immunol.* 2015;136(1):151-158.

1429. Gepp B, Lengger N, Dublin M, Hemmer W, Breiteneder H, Radauer C. Chimeras of Bet v 1 and Api g 1 reveal heterogeneous IgE re- sponses in patients with birch pollen allergy. *J Allergy Clin Immunol.* 2014;134(1):188-194.

1430. Antoniw JFRC, Pierpoints WS, et al. Comparison of three pathogenesis-related proteins from plants of two cultivars of tobacco infected with TMV. *J Gen Virol.* 1980;47:79-87. doi:10.1099/0022-1317-47-1-79

1431. Ali S, Ganai BA, Kamili AN, et al. Pathogenesis-related proteins and peptides as promising tools for engineering plants with multiple stress tolerance. *Microbiol Res.* 2018;212-213:29-37.

1432. Geroldinger-Simic M, Zelniker T, Aberer W, et al. Birch pollen- related food allergy: clinical aspects and the role of allergen- specific IgE and IgG4 antibodies. *J Allergy Clin Immunol.* 2011;127(3):616-622.

1433. Hauser M, Asam C, Himly M, et al. Bet v 1-like pollen allergens of multiple Fagales species can sensitize atopic individuals. *Clin Exp Allergy.* 2011;41(12):1804-1814.

1434. Breiteneder H, Ebner C. Molecular and biochemical classification of plant-derived food allergens. *J Allergy Clin Immunol.* 2000;106(1 Pt 1):27-36.

1435. Moneo I, Gómez M, Sánchez-Monge R, et al. Lack of crossreaction with Bet v 1 in patients sensitized to Dau c 1, a carrot allergen. *Ann Allergy Asthma Immunol.* 1999;83(1):71-75.

1436. Ballmer-Weber BK, Wüthrich B, Wangorsch A, Fötisch K, Altmann F, Vieths S. Carrot allergy: double-blinded, placebo-controlled food challenge and identification of allergens. *J Allergy Clin Immunol.* 2001;108(2):301-307.

1437. Moreno-Ancillo A, Gil-Adrados AC, Domínguez-Noche C, Cosmes PM, Pineda F. Occupational asthma due to carrot in a cook. *Allergol Immunopathol (Madr).* 2005;33(5):288-290.

1438. Flinterman AE, Akkerdaas JH, den Hartog Jager CF, et al. Lipid transfer protein-linked hazelnut allergy in children from a non- Mediterranean birch-endemic area. *J Allergy Clin Immunol.* 2008;121(2):423-428.

1439. Aglas L, Soh WT, Kraiem A, Wenger M, Brandstetter H, Ferreira F. Ligand binding of PR-10 proteins with a particular focus on the Bet v 1 allergen family. *Curr Allergy Asthma Rep.* 2020;20(7):25.

1440. Jacob T, von Loetzen CS, Reuter A, et al. Identification of a natural ligand of the hazel allergen Cor a 1. *Sci Rep.* 2019;9(1):8714.

1441. Seutter von Loetzen C, Jacob T, Hartl-Spiegelhauer O, et al. Ligand recognition of the major birch pollen allergen bet v 1 is isoform dependent. *PLoS One.* 2015;10(6):e0128677.

1442. Casañal A, Zander U, Muñoz C, et al. The strawberry pathogenesis-related 10 (PR-10) Fra a proteins control flavonoid biosynthesis by binding to metabolic intermediates. *J Biol Chem.* 2013;288(49):35322-35332.

1443. Mogensen JE, Wimmer R, Larsen JN, Spangfort MD, Otzen DE. The major birch allergen, Bet v 1, shows
affinity for a broad spectrum of physiological ligands. *J Biol Chem.* 2002;277(26):23684-23692.

1444. Muñoz C, Hoffmann T, Escobar NM, et al. The strawberry fruit Fra a allergen functions in flavonoid biosynthesis. *Mol Plant*. 2010;3(1):113-124.

1445. Seutter von Loetzen C, Hoffmann T, Hartl MJ, et al. Secret of the major birch pollen allergen Bet v 1: identification of the physiological ligand. *Biochem J.* 2014;457(3):379-390.

1446. Lee KS, Kim K, Choi YJ, et al. Increased sensitization rates to tree pollens in allergic children and adolescents and a change in the pollen season in the metropolitan area of Seoul, Korea. *Pediatr Allergy Immunol.* 2021;32(5):872-879.

1447. Villalta D, Asero R. Is the detection of IgE to multiple Bet v 1-homologous food allergens by means of allergen microarray clinically useful? *J Allergy Clin Immunol.* 2010;125:1158-1161.

1448. Cochrane SA, Salt LJ, Wantling E, et al. Development of a standardized low-dose double-blind placebo-controlled challenge vehicle for the EuroPrevall project. *Allergy*. 2012;67(1):107-113.

1449. Nothegger B, Reider N, Covaciu CE, et al. Oral birch pollen immunotherapy with apples: Results of a phase II clinical pilot study. *Immun Inflamm Dis.* 2021;9(2):503-511.

1450. Salcedo G, Sánchez-Monge R, Barber D, Díaz-Perales A. Plant non-specific lipid transfer proteins: an interface between plant defence and human allergy. *Biochim Biophys Acta*. 2007;1771(6):781-791.

1451. Pastorello EA, Monza M, Pravettoni V, et al. Characterization of the T-cell epitopes of the major peach allergen Pru p 3. *Int Arch Allergy Immunol.* 2010;153(1):1-12.

1452. Cavatorta V, Sforza S, Aquino G, et al. *In vitro* gastrointestinal digestion of the major peach allergen Pru p 3, a lipid transfer protein: molecular characterization of the products and assessment of their IgE binding abilities. *Mol Nutr Food Res.* 2010;54(10):1452-1457.

1453. Barber D, Díaz-Perales A, Escribese MM, et al. Molecular allergology and its impact in specific allergy diagnosis and therapy. *Allergy*. 2021;76(12):3642-3658.

1454. Skypala IJ, Bartra J, Ebo DG, et al. The diagnosis and management of allergic reactions in patients sensitized to non-specific lipid transfer proteins. *Allergy*. 2021;76(8):2433-2446.

1455. Dubiela P, Dölle-Bierke S, Aurich S, Worm M, Hoffmann-Sommergruber K. Component-resolved diagnosis in adult patients with food-dependent anaphylaxis. *World Allergy Organ J.* 2021;14(3):100530.

1456. Oeo-Santos C, Navas A, Benedé S, et al. New insights into the sensitization to nonspecific lipid transfer proteins from pollen and food: New role of allergen Ole e 7. *Allergy*. 2020;75(4):798-807.

1457. Palacín A, Gómez-Casado C, Rivas LA, et al. Graph based study of allergen cross-reactivity of plant lipid transfer proteins (LTPs) using microarray in a multicenter study. *PLoS One*. 2012;7(12):e50799.

1458. Díaz-Perales A, Tabar AI, Sánchez-Monge R, et al. Characterization of asparagus allergens: a relevant role of lipid transfer proteins. *J Allergy Clin Immunol.* 2002;110(5):790-796.

1459. Tordesillas L, Pacios LF, Palacín A, et al. Molecular basis of allergen cross-reactivity: non-specific lipid transfer proteins from wheat flour and peach fruit as models. *Mol Immunol.* 2009;47(2-3):534-540.

1460. Pastorello EA, Farioli L, Pravettoni V, et al. Pru p 3-sensitised Italian peach-allergic patients are less likely to develop severe symptoms when also presenting IgE antibodies to Pru p 1 and Pru p 4. *Int Arch Allergy Immunol.* 2011;156(4):362-372.

1461. Ruano-Zaragoza M, Somoza ML, Jiménez-Rodriguez TW, et al. Lipid transfer protein sensitization: risk of anaphylaxis and molecular sensitization profile in Pru p 3-sensitized patients. *Int Arch Allergy Immunol.* 2021;182(5):425-432.

1462. Mota I, Gaspar À, Benito-Garcia F, et al. Anaphylaxis caused by lipid transfer proteins: an unpredictable clinical syndrome. *Allergol Immunopathol (Madr).* 2018;46(6):565-570.

1463. Pastorello EA, Farioli L, Stafylaraki C, et al. Wheat-dependent exercise-induced anaphylaxis caused by a lipid transfer protein and not by ω-5 gliadin. *Ann Allergy Asthma Immunol.* 2014;112(4):386-387.e381.

1464. Palomares F, Gomez F, Bogas G, et al. Immunological changes induced in peach allergy patients with systemic reactions by Pru p 3 sublingual immunotherapy. *Mol Nutr Food Res.* 2018;62(3).

1465. Majorek KA, Porebski PJ, Dayal A, et al. Structural and immunologic characterization of bovine, horse, and rabbit serum albumins. *Mol Immunol.* 2012;52(3-4):174-182.

1466. Fiocchi A, Restani P, Riva E, et al. Heat treatment modifies the allergenicity of beef and bovine serum albumin. *Allergy*. 1998;53(8):798-802.

1467. Chruszcz M, Mikolajczak K, Mank N, Majorek KA, Porebski PJ, Minor W. Serum albumins-unusual allergens. *Biochim Biophys Acta*. 2013;1830(12):5375-5381.

1468. Jenkins JA, Breiteneder H, Mills EN. Evolutionary distance from human homologs reflects allergenicity of animal food proteins. *J Allergy Clin Immunol.* 2007;120(6):1399-1405.

1469. Fanta C, Ebner C. Allergy to mare's milk. *Allergy*. 1998;53(5):539-540.

1470. Drouet M, Sabbah A, Le Sellin J, Bonneau JC, Gay G, Dubois-Gosnet C. Fatal anaphylaxis after eating wild boar meat in a patient with pork-cat syndrome. *Allerg Immunol (Paris)*. 2001;33(4):163-165.

1471. Morisset M, Arumugam K, Ollert M, Hilger C. Horse-meat allergy mediated by dog-allergy: a case report and review of the literature. *Allergo J.* 2016;25(3):30-35.

1472. Alvarez-Perea A, Caralli ME, Zubeldia JM, Baeza ML. Pork-cat syndrome as a cause of occupational asthma. *J Investig Allergol Clin Immunol.* 2014;24(3):209-211.

1473. Quirce S, Maranon F, Umpierrez A. de las Heras M, Fernandez-Caldas E, Sastre J. Chicken serum albumin (Gal d 5*) is a partially heat-labile inhalant and food allergen implicated in the bird-egg syndrome. *Allergy*. 2001;56(8):754-762.

1474. WHO. WHO expert committee on biological standardization. World Health Organ Tech Rep Ser; 2007;(941):1-340

1475. de Silva R, Dasanayake W, Wickramasinhe GD, et al. Sensitization to bovine serum albumin as a possible cause of allergic reactions to vaccines. *Vaccine*. 2017;35(11):1494-1500.

1476. Dewachter P, Jacquenet S, Beloucif S, Goarin JP, Koskas F, Mouton-Faivre C. Pork-cat syndrome revealed after surgery: Anaphylaxis to bovine serum albumin tissue adhesive. *J Allergy Clin Immunol Pract.* 2019;7(7):2450-2452.

1477. Hilger C, Clark E, Swiontek K, et al. Anaphylaxis to bovine serum albumin tissue adhesive in a non-meat-allergic patient. *J Investig Allergol Clin Immunol.* 2020;30(5):369-371.

1478. Kasahara A, Kita K, Tomita E, Toyota J, Imai Y, Kumada H. Repeated administration of recombinant human serum albumin caused no serious allergic reactions in patients with liver cirrhosis: a multicenter clinical study. *J Gastroenterol.* 2008;43(6):464-472.

1479. Moreno Lozano L, Galindo Bonilla P, Borja Segade J, Extremera Ortega A, Gomez Torrijos E, Garcia Rodriguez R. Human serum albumin induced anaphylaxis in a patient with good tolerance to human plasma. *J Investig Allergol Clin Immunol.* 2019;29(1):51-53.

1480. Wang M, Zhu D, Zhu J, Nussinov R, Ma B. Local and global anatomy of antibody-protein antigen recognition. *J Mol Recognit.* 2018;31(5):e2693.

1481. Wisnewski AV, Liu J, Redlich CA. Antigenic changes in human albumin caused by reactivity with the occupational allergen diphenylmethane diisocyanate. *Anal Biochem.* 2010;400(2):251-258.

1482. Wisnewski AV, Stowe MH, Cartier A, et al. Isocyanate vapor-induced antigenicity of human albumin. *J Allergy Clin Immunol.* 2004;113(6):1178-1184.

1483. Reese G, Schicktanz S, Lauer I, et al. Structural, immunological and functional properties of natural recombinant Pen a 1, the major allergen of Brown Shrimp, *Penaeus aztecus*. *Clin Exp Allergy.* 2006;36(4):517-524.
affinity for a broad spectrum of physiological ligands. *J Biol Chem.* 2002;277(26):23684-23692.

1444. Muñoz C, Hoffmann T, Escobar NM, et al. The strawberry fruit Fra a allergen functions in flavonoid biosynthesis. *Mol Plant*. 2010;3(1):113-124.

1445. Seutter von Loetzen C, Hoffmann T, Hartl MJ, et al. Secret of the major birch pollen allergen Bet v 1: identification of the physiological ligand. *Biochem J.* 2014;457(3):379-390.

1446. Lee KS, Kim K, Choi YJ, et al. Increased sensitization rates to tree pollens in allergic children and adolescents and a change in the pollen season in the metropolitan area of Seoul, Korea. *Pediatr Allergy Immunol.* 2021;32(5):872-879.

1447. Villalta D, Asero R. Is the detection of IgE to multiple Bet v 1-homologous food allergens by means of allergen microarray clinically useful? *J Allergy Clin Immunol.* 2010;125:1158-1161.

1448. Cochrane SA, Salt LJ, Wantling E, et al. Development of a standardized low-dose double-blind placebo-controlled challenge vehicle for the EuroPrevall project. *Allergy*. 2012;67(1):107-113.

1449. Nothegger B, Reider N, Covaciu CE, et al. Oral birch pollen immunotherapy with apples: Results of a phase II clinical pilot study. *Immun Inflamm Dis.* 2021;9(2):503-511.

1450. Salcedo G, Sánchez-Monge R, Barber D, Díaz-Perales A. Plant non-specific lipid transfer proteins: an interface between plant defence and human allergy. *Biochim Biophys Acta*. 2007;1771(6):781-791.

1451. Pastorello EA, Monza M, Pravettoni V, et al. Characterization of the T-cell epitopes of the major peach allergen Pru p 3. *Int Arch Allergy Immunol.* 2010;153(1):1-12.

1452. Cavatorta V, Sforza S, Aquino G, et al. *In vitro* gastrointestinal digestion of the major peach allergen Pru p 3, a lipid transfer protein: molecular characterization of the products and assessment of their IgE binding abilities. *Mol Nutr Food Res.* 2010;54(10):1452-1457.

1453. Barber D, Díaz-Perales A, Escribese MM, et al. Molecular allergology and its impact in specific allergy diagnosis and therapy. *Allergy*. 2021;76(12):3642-3658.

1454. Skypala IJ, Bartra J, Ebo DG, et al. The diagnosis and management of allergic reactions in patients sensitized to non-specific lipid transfer proteins. *Allergy*. 2021;76(8):2433-2446.

1455. Dubiela P, Dölle-Bierke S, Aurich S, Worm M, Hoffmann-Sommergruber K. Component-resolved diagnosis in adult patients with food-dependent anaphylaxis. *World Allergy Organ J.* 2021;14(3):100530.

1456. Oeo-Santos C, Navas A, Benedé S, et al. New insights into the sensitization to nonspecific lipid transfer proteins from pollen and food: New role of allergen Ole e 7. *Allergy*. 2020;75(4):798-807.

1457. Palacín A, Gómez-Casado C, Rivas LA, et al. Graph based study of allergen cross-reactivity of plant lipid transfer proteins (LTPs) using microarray in a multicenter study. *PLoS One*. 2012;7(12):e50799.

1458. Díaz-Perales A, Tabar AI, Sánchez-Monge R, et al. Characterization of asparagus allergens: a relevant role of lipid transfer proteins. *J Allergy Clin Immunol.* 2002;110(5):790-796.

1459. Tordesillas L, Pacios LF, Palacín A, et al. Molecular basis of allergen cross-reactivity: non-specific lipid transfer proteins from wheat flour and peach fruit as models. *Mol Immunol.* 2009;47(2-3):534-540.

1460. Pastorello EA, Farioli L, Pravettoni V, et al. Pru p 3-sensitised Italian peach-allergic patients are less likely to develop severe symptoms when also presenting IgE antibodies to Pru p 1 and Pru p 4. *Int Arch Allergy Immunol.* 2011;156(4):362-372.

1461. Ruano-Zaragoza M, Somoza ML, Jiménez-Rodriguez TW, et al. Lipid transfer protein sensitization: risk of anaphylaxis and molecular sensitization profile in Pru p 3-sensitized patients. *Int Arch Allergy Immunol.* 2021;182(5):425-432.

1462. Mota I, Gaspar À, Benito-Garcia F, et al. Anaphylaxis caused by lipid transfer proteins: an unpredictable clinical syndrome. *Allergol Immunopathol (Madr).* 2018;46(6):565-570.

1463. Pastorello EA, Farioli L, Stafylaraki C, et al. Wheat-dependent exercise-induced anaphylaxis caused by a lipid transfer protein and not by ω-5 gliadin. *Ann Allergy Asthma Immunol.* 2014;112(4):386-387.e381.

1464. Palomares F, Gomez F, Bogas G, et al. Immunological changes induced in peach allergy patients with systemic reactions by Pru p 3 sublingual immunotherapy. *Mol Nutr Food Res.* 2018;62(3).

1465. Majorek KA, Porebski PJ, Dayal A, et al. Structural and immunologic characterization of bovine, horse, and rabbit serum albumins. *Mol Immunol.* 2012;52(3-4):174-182.

1466. Fiocchi A, Restani P, Riva E, et al. Heat treatment modifies the allergenicity of beef and bovine serum albumin. *Allergy*. 1998;53(8):798-802.

1467. Chruszcz M, Mikolajczak K, Mank N, Majorek KA, Porebski PJ, Minor W. Serum albumins-unusual allergens. *Biochim Biophys Acta*. 2013;1830(12):5375-5381.

1468. Jenkins JA, Breiteneder H, Mills EN. Evolutionary distance from human homologs reflects allergenicity of animal food proteins. *J Allergy Clin Immunol.* 2007;120(6):1399-1405.

1469. Fanta C, Ebner C. Allergy to mare's milk. *Allergy*. 1998;53(5):539-540.

1470. Drouet M, Sabbah A, Le Sellin J, Bonneau JC, Gay G, Dubois-Gosnet C. Fatal anaphylaxis after eating wild boar meat in a patient with pork-cat syndrome. *Allerg Immunol (Paris)*. 2001;33(4):163-165.

1471. Morisset M, Arumugam K, Ollert M, Hilger C. Horse-meat allergy mediated by dog-allergy: a case report and review of the literature. *Allergo J.* 2016;25(3):30-35.

1472. Alvarez-Perea A, Caralli ME, Zubeldia JM, Baeza ML. Pork-cat syndrome as a cause of occupational asthma. *J Investig Allergol Clin Immunol.* 2014;24(3):209-211.

1473. Quirce S, Maranon F, Umpierrez A. de las Heras M, Fernandez-Caldas E, Sastre J. Chicken serum albumin (Gal d 5*) is a partially heat-labile inhalant and food allergen implicated in the bird-egg syndrome. *Allergy*. 2001;56(8):754-762.

1474. WHO. WHO expert committee on biological standardization. World Health Organ Tech Rep Ser; 2007;(941):1-340

1475. de Silva R, Dasanayake W, Wickramasinhe GD, et al. Sensitization to bovine serum albumin as a possible cause of allergic reactions to vaccines. *Vaccine*. 2017;35(11):1494-1500.

1476. Dewachter P, Jacquenet S, Beloucif S, Goarin JP, Koskas F, Mouton-Faivre C. Pork-cat syndrome revealed after surgery: Anaphylaxis to bovine serum albumin tissue adhesive. *J Allergy Clin Immunol Pract.* 2019;7(7):2450-2452.

1477. Hilger C, Clark E, Swiontek K, et al. Anaphylaxis to bovine serum albumin tissue adhesive in a non-meat-allergic patient. *J Investig Allergol Clin Immunol.* 2020;30(5):369-371.

1478. Kasahara A, Kita K, Tomita E, Toyota J, Imai Y, Kumada H. Repeated administration of recombinant human serum albumin caused no serious allergic reactions in patients with liver cirrhosis: a multicenter clinical study. *J Gastroenterol.* 2008;43(6):464-472.

1479. Moreno Lozano L, Galindo Bonilla P, Borja Segade J, Extremera Ortega A, Gomez Torrijos E, Garcia Rodriguez R. Human serum albumin induced anaphylaxis in a patient with good tolerance to human plasma. *J Investig Allergol Clin Immunol.* 2019;29(1):51-53.

1480. Wang M, Zhu D, Zhu J, Nussinov R, Ma B. Local and global anatomy of antibody-protein antigen recognition. *J Mol Recognit.* 2018;31(5):e2693.

1481. Wisnewski AV, Liu J, Redlich CA. Antigenic changes in human albumin caused by reactivity with the occupational allergen diphenylmethane diisocyanate. *Anal Biochem.* 2010;400(2):251-258.

1482. Wisnewski AV, Stowe MH, Cartier A, et al. Isocyanate vapor-induced antigenicity of human albumin. *J Allergy Clin Immunol.* 2004;113(6):1178-1184.

1483. Reese G, Schicktanz S, Lauer I, et al. Structural, immunological and functional properties of natural recombinant Pen a 1, the major allergen of Brown Shrimp, *Penaeus aztecus*. *Clin Exp Allergy.* 2006;36(4):517-524.
1484. Daul CB, Slattery M, Reese G, Lehrer SB. Identification of the major brown shrimp (Penaeus aztecus) allergen as the muscle protein tropomyosin. *Int Arch Allergy Immunol.* 1994;105(1):49-55.

1485. Reese G, Jeoung BJ, Daul CB, Lehrer SB. Characterization of recombinant shrimp allergen Pen a 1 (tropomyosin). *Int Arch Allergy Immunol.* 1997;113(1-3):240-242.

1486. James JK, Pike DH, Khan IJ, Nanda V. Structural and dynamic properties of allergen and non-allergen forms of tropomyosin. *Structure*. 2018;26(7):997-1006.

1487. Hoffman DR, Day ED Jr, Miller JS. The major heat stable allergen of shrimp. *Ann Allergy*. 1981;47(1):17-22.

1488. Naqpal S, Rajappa L, Metcalfe DD, Rao PV. Isolation and characterization of heat-stable allergens from shrimp (*Penaeus indicus*). *J Allergy Clin Immunol.* 1989;83(1):26-36.

1489. Leung PS, Chu KH, Chow WK, et al. Cloning, expression, and primary structure of Metapenaeus ensis tropomyosin, the major heat-stable shrimp allergen. *J Allergy Clin Immunol.* 1994;94(5):882-890.

1490. Ayuso R, Reese G, Leong-Kee S, Plante M, Lehrer SB. Molecular basis of arthropod cross-reactivity: IgE-binding cross-reactive epitopes of shrimp, house dust mite and cockroach tropomyosins. *Int Arch Allergy Immunol.* 2002;129(1):38-48.

1491. Leung NY, Wai CY, Shu S, et al. Current immunological and molecular biological perspectives on seafood allergy: a comprehensive review. *Clin Rev Allergy Immunol.* 2014;46(3):180-197.

1492. Yi FC, Cheong N, Shek LP, Wang DY, Chua KY, Lee BW. Identification of shared and unique immunoglobulin E epitopes of the highly conserved tropomyosins in *Blomia tropicalis* and *Dermatophagoides pteronyssinus*. *Clin Exp Allergy.* 2002;32(8):1203-1210.

1493. Leung PS, Chow WK, Duffey S, Kwan HS, Gershwin ME, Chu KH. IgE reactivity against a cross-reactive allergen in crustacea and mollusca: evidence for tropomyosin as the common allergen. *J Allergy Clin Immunol.* 1996;98(5 Pt 1):954-961.

1494. Cantillo JF, Puerta L, Fernandez-Caldas E, et al. Tropomyosins in mosquito and house dust mite cross-react at the humoral and cellular level. *Clin Exp Allergy.* 2018;48(10):1354-1363.

1495. Sokol WN. Grasshopper sensitization in patients allergic to crustaceans, mites, and cockroaches: should grasshopper-containing products carry a warning? *Ann Allergy Asthma Immunol.* 2020;124(5):518-520.

1496. Palmer LK, Marsh JT, Lu M, Goodman RE, Zeece MG, Johnson PE. Shellfish tropomyosin IgE cross-reactivity differs among edible insect species. *Mol Nutr Food Res.* 2020;64(8):e1900923.

1497. Santos AB, Rocha GM, Oliver C, et al. Cross-reactive IgE antibody responses to tropomyosins from Ascaris lumbricoides and cockroach. *J Allergy Clin Immunol.* 2008;121(4):1040-1046.

1498. Acevedo N, Sánchez J, Erler A, et al. IgE cross-reactivity between Ascaris and domestic mite allergens: the role of tropomyosin and the nematode polyprotein ABA-1. *Allergy.* 2009;64(11):1635-1643.

1499. Kamath SD, Johnston EB, Iyer S, et al. IgE reactivity to shrimp allergens in infants and their cross-reactivity to house dust mite. *Pediatr Allergy Immunol.* 2017;28(7):703-707.

1500. Zakzuk J, Mercado D, Bornacelly A, et al. Hygienic conditions influence sensitization to Blomia tropicalis allergenic components: Results from the FRAAT birth cohort. *Pediatr Allergy Immunol.* 2019;30(2):172-178.

1501. Buendía E, Zakzuk J, Mercado D, Alvarez A, Caraballo L. The IgE response to Ascaris molecular components is associated with clinical indicators of asthma severity. *World Allergy Organ J.* 2015;8(1):8.

1502. Sousa-Santos A, Moreno AS, Santos ABR, et al. Parasite infections, allergy and asthma: a role for tropomyosin in promoting type 2 immune responses. *Int Arch Allergy Immunol.* 2020;181(3):221-227.

1503. Asero R, Pravettoni V, Scala E, Villalta D. House dust mite-shrimp allergen interrelationships. *Curr Allergy Asthma Rep.* 2020;20(4):9.

1504. Fernandes J, Reshef A, Patton L, Ayuso R, Reese G, Lehrer SB. Immunoglobulin E antibody reactivity to the major shrimp allergen, tropomyosin, in unexposed Orthodox Jews. *Clin Exp Allergy.* 2003;33(7):956-961.

1505. Liu R, Holck AL, Yang E, Liu C, Xue W. Tropomyosin from tilapia (Oreochromis mossambicus) as an allergen. *Clin Exp Allergy.* 2013;43(3):365-377.

1506. Weghofer M, Thomas WR, Kronqvist M, et al. Variability of IgE reactivity profiles among European mite allergic patients. *Eur J Clin Invest.* 2008;38(12):959-965.

1507. Cantillo JF, Fernández-Caldas E, Puerta L. Immunological aspects of the immune response induced by mosquito allergens. *Int Arch Allergy Immunol.* 2014;165(4):271-282.

1508. Celi G, Brusca I, Scala E, et al. House dust mite allergy and shrimp allergy: a complex interaction. *Eur Ann Allergy Clin Immunol.* 2020;52(5):205-209.

1509. Iparraguirre A, Rodríguez-Pérez R, Juste S, Ledesma A, Moneo I, Caballero ML. Selective allergy to lobster in a case of primary sensitization to house dust mites. *J Investig Allergol Clin Immunol.* 2009;19(5):409-413.

1510. Niederberger V, Hayek B, Vrtala S, et al. Calcium-dependent immunoglobulin E recognition of the apo- and calcium-bound form of a cross-reactive two EF-hand timothy grass pollen allergen, Phl p 7. *FASEB J.* 1999;13(8):843-856.

1511. Henzl MT, Davis ME, Tan A. Polcalcin divalent ion-binding behavior and thermal stability: comparison of Bet v 4, Bra n 1, and Bra n 2 to Phl p 7. *Biochemistry.* 2010;49(10):2256-2268.

1512. Barderas R, Villalba M, Pascual CY, Batanero E, Rodríguez R. Profilin (Che a 2) and polcalcin (Che a 3) are relevant allergens of *Chenopodium album* pollen: isolation, amino acid sequences, and immunologic properties. *J Allergy Clin Immunol.* 2004;113(6):1192-1198.

1513. Movérare R, Larsson H, Carlsson R, Holmquist I. Mugwort-sensitized individuals from North Europe, South Europe and North America show different IgE reactivity patterns. *Int Arch Allergy Immunol.* 2011;154(2):164-172.

1514. Orovitg A, Guardia P, Barber D, et al. Enhanced diagnosis of pollen allergy using specific immunoglobulin E determination to detect major allergens and panallergens. *J Investig Allergol Clin Immunol.* 2011;21(4):253-259.

1515. San Nicoló M, Braun T, Eder K, Berghaus A, Gröger M. Clinical relevance of IgE to profilin and/or polcalcin in pollen-sensitized patients. *Int Arch Allergy Immunol.* 2016;169(2):101-107.

1516. Compés E, Hernández E, Quirce S, et al. Hypersensitivity to black locust (*Robinia pseudoacacia*) pollen: "allergy mirages". *Ann Allergy Asthma Immunol.* 2006;96(4):586-592.

1517. Moya R, González-Ruiz A, Beitia JM, Carnés J, López-Matas M. Ole e 3, a candidate for *in vivo* diagnosis of polcalcin sensitization. *Int Arch Allergy Immunol.* 2021;182(6):465-473.

1518. Engel E, Richter K, Obermeyer G, et al. Immunological and biological properties of Bet v 4, a novel birch pollen allergen with two EF-hand calcium-binding domains. *J Biol Chem.* 1997;272(45):28630-28637.

1519. Gregoire C, Rosinski-Chupin I, Rabillon J, Alzari PM, David B, Dandeu JP. cDNA cloning and sequencing reveal the major horse allergen Equ c1 to be a glycoprotein member of the lipocalin superfamily. *J Biol Chem.* 1996;271(51):32951-32959.

1520. Lascombe MB, Grégoire C, Poncet P, et al. Crystal structure of the allergen Equ c 1. A dimeric lipocalin with restricted IgE-reactive epitopes. *J Biol Chem.* 2000;275(28):21572-21577.

1521. Goubran Botros H, Poncet P, Rabillon J, Fontaine T, Laval JM, David B. Biochemical characterization and surfactant properties of horse allergens. *Eur J Biochem.* 2001;268(10):3126-3136.

1522. Liccardi G, Emenius G, Merritt AS, Salzillo A, D'Amato M, D'Amato G. Direct and indirect exposure to horse: risk for sensitization and asthma. *Curr Allergy Asthma Rep.* 2012;12(5):429-437.

1523. Merritt AS, Emenius G, Elfman L, Smedje G. Measurement of horse allergen (Equ cx) in schools. *ISRN Allergy.* 2011;2011:574258.
1484. Daul CB, Slattery M, Reese G, Lehrer SB. Identification of the major brown shrimp (Penaeus aztecus) allergen as the muscle protein tropomyosin. *Int Arch Allergy Immunol.* 1994;105(1):49-55.

1485. Reese G, Jeoung BJ, Daul CB, Lehrer SB. Characterization of recombinant shrimp allergen Pen a 1 (tropomyosin). *Int Arch Allergy Immunol.* 1997;113(1-3):240-242.

1486. James JK, Pike DH, Khan IJ, Nanda V. Structural and dynamic properties of allergen and non-allergen forms of tropomyosin. *Structure*. 2018;26(7):997-1006.

1487. Hoffman DR, Day ED Jr, Miller JS. The major heat stable allergen of shrimp. *Ann Allergy*. 1981;47(1):17-22.

1488. Naqpal S, Rajappa L, Metcalfe DD, Rao PV. Isolation and characterization of heat-stable allergens from shrimp (*Penaeus indicus*). *J Allergy Clin Immunol.* 1989;83(1):26-36.

1489. Leung PS, Chu KH, Chow WK, et al. Cloning, expression, and primary structure of Metapenaeus ensis tropomyosin, the major heat-stable shrimp allergen. *J Allergy Clin Immunol.* 1994;94(5):882-890.

1490. Ayuso R, Reese G, Leong-Kee S, Plante M, Lehrer SB. Molecular basis of arthropod cross-reactivity: IgE-binding cross-reactive epitopes of shrimp, house dust mite and cockroach tropomyosins. *Int Arch Allergy Immunol.* 2002;129(1):38-48.

1491. Leung NY, Wai CY, Shu S, et al. Current immunological and molecular biological perspectives on seafood allergy: a comprehensive review. *Clin Rev Allergy Immunol.* 2014;46(3):180-197.

1492. Yi FC, Cheong N, Shek LP, Wang DY, Chua KY, Lee BW. Identification of shared and unique immunoglobulin E epitopes of the highly conserved tropomyosins in *Blomia tropicalis* and *Dermatophagoides pteronyssinus*. *Clin Exp Allergy.* 2002;32(8):1203-1210.

1493. Leung PS, Chow WK, Duffey S, Kwan HS, Gershwin ME, Chu KH. IgE reactivity against a cross-reactive allergen in crustacea and mollusca: evidence for tropomyosin as the common allergen. *J Allergy Clin Immunol.* 1996;98(5 Pt 1):954-961.

1494. Cantillo JF, Puerta L, Fernandez-Caldas E, et al. Tropomyosins in mosquito and house dust mite cross-react at the humoral and cellular level. *Clin Exp Allergy.* 2018;48(10):1354-1363.

1495. Sokol WN. Grasshopper sensitization in patients allergic to crustaceans, mites, and cockroaches: should grasshopper-containing products carry a warning? *Ann Allergy Asthma Immunol.* 2020;124(5):518-520.

1496. Palmer LK, Marsh JT, Lu M, Goodman RE, Zeece MG, Johnson PE. Shellfish tropomyosin IgE cross-reactivity differs among edible insect species. *Mol Nutr Food Res.* 2020;64(8):e1900923.

1497. Santos AB, Rocha GM, Oliver C, et al. Cross-reactive IgE antibody responses to tropomyosins from Ascaris lumbricoides and cockroach. *J Allergy Clin Immunol.* 2008;121(4):1040-1046.

1498. Acevedo N, Sánchez J, Erler A, et al. IgE cross-reactivity between Ascaris and domestic mite allergens: the role of tropomyosin and the nematode polyprotein ABA-1. *Allergy.* 2009;64(11):1635-1643.

1499. Kamath SD, Johnston EB, Iyer S, et al. IgE reactivity to shrimp allergens in infants and their cross-reactivity to house dust mite. *Pediatr Allergy Immunol.* 2017;28(7):703-707.

1500. Zakzuk J, Mercado D, Bornacelly A, et al. Hygienic conditions influence sensitization to Blomia tropicalis allergenic components: Results from the FRAAT birth cohort. *Pediatr Allergy Immunol.* 2019;30(2):172-178.

1501. Buendía E, Zakzuk J, Mercado D, Alvarez A, Caraballo L. The IgE response to Ascaris molecular components is associated with clinical indicators of asthma severity. *World Allergy Organ J.* 2015;8(1):8.

1502. Sousa-Santos A, Moreno AS, Santos ABR, et al. Parasite infections, allergy and asthma: a role for tropomyosin in promoting type 2 immune responses. *Int Arch Allergy Immunol.* 2020;181(3):221-227.

1503. Asero R, Pravettoni V, Scala E, Villalta D. House dust mite-shrimp allergen interrelationships. *Curr Allergy Asthma Rep.* 2020;20(4):9.

1504. Fernandes J, Reshef A, Patton L, Ayuso R, Reese G, Lehrer SB. Immunoglobulin E antibody reactivity to the major shrimp allergen, tropomyosin, in unexposed Orthodox Jews. *Clin Exp Allergy.* 2003;33(7):956-961.

1505. Liu R, Holck AL, Yang E, Liu C, Xue W. Tropomyosin from tilapia (Oreochromis mossambicus) as an allergen. *Clin Exp Allergy.* 2013;43(3):365-377.

1506. Weghofer M, Thomas WR, Kronqvist M, et al. Variability of IgE reactivity profiles among European mite allergic patients. *Eur J Clin Invest.* 2008;38(12):959-965.

1507. Cantillo JF, Fernández-Caldas E, Puerta L. Immunological aspects of the immune response induced by mosquito allergens. *Int Arch Allergy Immunol.* 2014;165(4):271-282.

1508. Celi G, Brusca I, Scala E, et al. House dust mite allergy and shrimp allergy: a complex interaction. *Eur Ann Allergy Clin Immunol.* 2020;52(5):205-209.

1509. Iparraguirre A, Rodríguez-Pérez R, Juste S, Ledesma A, Moneo I, Caballero ML. Selective allergy to lobster in a case of primary sensitization to house dust mites. *J Investig Allergol Clin Immunol.* 2009;19(5):409-413.

1510. Niederberger V, Hayek B, Vrtala S, et al. Calcium-dependent immunoglobulin E recognition of the apo- and calcium-bound form of a cross-reactive two EF-hand timothy grass pollen allergen, Phl p 7. *FASEB J.* 1999;13(8):843-856.

1511. Henzl MT, Davis ME, Tan A. Polcalcin divalent ion-binding behavior and thermal stability: comparison of Bet v 4, Bra n 1, and Bra n 2 to Phl p 7. *Biochemistry.* 2010;49(10):2256-2268.

1512. Barderas R, Villalba M, Pascual CY, Batanero E, Rodríguez R. Profilin (Che a 2) and polcalcin (Che a 3) are relevant allergens of *Chenopodium album* pollen: isolation, amino acid sequences, and immunologic properties. *J Allergy Clin Immunol.* 2004;113(6):1192-1198.

1513. Movérare R, Larsson H, Carlsson R, Holmquist I. Mugwort-sensitized individuals from North Europe, South Europe and North America show different IgE reactivity patterns. *Int Arch Allergy Immunol.* 2011;154(2):164-172.

1514. Orovitg A, Guardia P, Barber D, et al. Enhanced diagnosis of pollen allergy using specific immunoglobulin E determination to detect major allergens and panallergens. *J Investig Allergol Clin Immunol.* 2011;21(4):253-259.

1515. San Nicoló M, Braun T, Eder K, Berghaus A, Gröger M. Clinical relevance of IgE to profilin and/or polcalcin in pollen-sensitized patients. *Int Arch Allergy Immunol.* 2016;169(2):101-107.

1516. Compés E, Hernández E, Quirce S, et al. Hypersensitivity to black locust (*Robinia pseudoacacia*) pollen: "allergy mirages". *Ann Allergy Asthma Immunol.* 2006;96(4):586-592.

1517. Moya R, González-Ruiz A, Beitia JM, Carnés J, López-Matas M. Ole e 3, a candidate for *in vivo* diagnosis of polcalcin sensitization. *Int Arch Allergy Immunol.* 2021;182(6):465-473.

1518. Engel E, Richter K, Obermeyer G, et al. Immunological and biological properties of Bet v 4, a novel birch pollen allergen with two EF-hand calcium-binding domains. *J Biol Chem.* 1997;272(45):28630-28637.

1519. Gregoire C, Rosinski-Chupin I, Rabillon J, Alzari PM, David B, Dandeu JP. cDNA cloning and sequencing reveal the major horse allergen Equ c1 to be a glycoprotein member of the lipocalin superfamily. *J Biol Chem.* 1996;271(51):32951-32959.

1520. Lascombe MB, Grégoire C, Poncet P, et al. Crystal structure of the allergen Equ c 1. A dimeric lipocalin with restricted IgE-reactive epitopes. *J Biol Chem.* 2000;275(28):21572-21577.

1521. Goubran Botros H, Poncet P, Rabillon J, Fontaine T, Laval JM, David B. Biochemical characterization and surfactant properties of horse allergens. *Eur J Biochem.* 2001;268(10):3126-3136.

1522. Liccardi G, Emenius G, Merritt AS, Salzillo A, D'Amato M, D'Amato G. Direct and indirect exposure to horse: risk for sensitization and asthma. *Curr Allergy Asthma Rep.* 2012;12(5):429-437.

1523. Merritt AS, Emenius G, Elfman L, Smedje G. Measurement of horse allergen (Equ cx) in schools. *ISRN Allergy.* 2011;2011:574258.
1524. Immonen A, Kinnunen T, Sirven P, et al. The major horse allergen Equ c 1 contains one immunodominant region of T cell epitopes. *Clin Exp Allergy*. 2007;37(6):939-947.

1525. Haka J, Niemi MH, Mattila P, Jänis J, Takkinen K, Rouvinen J. Development of hypoallergenic variants of the major horse allergen Equ c 1 for immunotherapy by rational structure based engineering. *Sci Rep*. 2019;9(1):20148.

1526. Wintersand A, Alsved M, Jakobsson J, et al. Individual airborne characteristics of dog allergens. *Clin Exp Allergy*. 2021.

1527. Custovic A, Green R, Fletcher A, et al. Aerodynamic properties of the major dog allergen Can f 1: distribution in homes, concentration, and particle size of allergen in the air. *Am J Respir Crit Care Med*. 1997;155(1):94-98.

1528. Chruszcz M, Kapingidza AB, Dolamore C, Kowal K. A robust method for the estimation and visualization of IgE cross-reactivity likelihood between allergens belonging to the same protein family. *PLoS One*. 2018;13(11):e0208276.

1529. Hilger C, Swiontek K, Arumugam K, Lehners C, Hentges F. Identification of a new major dog allergen highly cross-reactive with Fel d 4 in a population of cat- and dog-sensitized patients. *J Allergy Clin Immunol*. 2012;129(4):1149-1151.

1530. Apostolovic D, Sánchez-Vidaurre S, Waden K, et al. The cat lipocalin Fel d 7 and its cross-reactivity with the dog lipocalin Can f 1. *Allergy*. 2016;71(10):1490-1495.

1531. Hemmer W, Sestak-Greinecker G, Braunsteiner T, Wantke F, Wöhrl S. Molecular sensitization patterns in animal allergy: Relationship with clinical relevance and pet ownership. *Allergy*. 2021;76:3687-3696.

1532. Madhurantakam C, Nilsson OB, Uchtenhagen H, et al. Crystal structure of the dog lipocalin allergen Can f 2: implications for cross-reactivity to the cat allergen Fel d 4. *J Mol Biol*. 2010;401(1):68-83.

1533. Mattsson L, Lundgren T, Olsson P, Sundberg M, Lidholm J. Molecular and immunological characterization of Can f 4: a dog dander allergen cross-reactive with a 23 kDa odorant-binding protein in cow dander. *Clin Exp Allergy*. 2010;40(8):1276-1287.

1534. Jakob T, Hilger C, Hentges F. Clinical relevance of sensitization to cross-reactive lipocalin Can f 6. *Allergy*. 2013;68(5):690-691.

1535. Shewry PR, Napier JA, Tatham AS. Seed storage proteins: structures and biosynthesis. *Plant Cell*. 1995;7(7):945-956.

1536. Slavokhotova AA, Rogozhin EA. Defense peptides from the α-hairpinin family are components of plant innate immunity. *Front Plant Sci*. 2020;11:465.

1537. Aalberse RC, Mueller GA, Derksen NIL, et al. Identification of the amino-terminal fragment of Ara h 1 as a major target of the IgE-binding activity in the basic peanut protein fraction. *Clin Exp Allergy*. 2020;50(3):401-405.

1538. Peeters KA, Koppelman SJ, Penninks AH, et al. Clinical relevance of sensitization to lupine in peanut-sensitized adults. *Allergy*. 2009;64(4):549-555.

1539. Verhoeckx KCM, Vissers YM, Baumert JL, et al. Food processing and allergenicity. *Food Chem Toxicol*. 2015;80:223-240.

1540. Klemans RJ, van Os-Medendorp H, Blankestijn M, Bruijnzeel-Koomen CA, Knol EF, Knulst AC. Diagnostic accuracy of specific IgE to components in diagnosing peanut allergy: a systematic review. *Clin Exp Allergy*. 2015;45(4):720-730.

1541. Lange L, Lasota L, Finger A, et al. Ana o 3-specific IgE is a good predictor for clinically relevant cashew allergy in children. *Allergy*. 2017;72(4):598-603.

1542. Sato S, Yamamoto M, Yanagida N, et al. Jug r 1 sensitization is important in walnut-allergic children and youth. *J Allergy Clin Immunol Pract*. 2017;5(6):1784-1786.

1543. Cabanillas B, Jappe U, Novak N. Allergy to peanut, soybean, and other legumes: recent advances in allergen characterization, stability to processing and IgE cross-reactivity. *Mol Nutr Food Res*. 2018;62(1).

1544. Geiselhart S, Hoffmann-Sommergruber K, Bublin M. Tree nut allergens. *Mol Immunol*. 2018;100:71-81.

1545. López-Torrejón G, Salcedo G, Martín-Esteban M, Díaz-Perales A, Pascual CY, Sánchez-Monge R. Len c 1, a major allergen and vicilin from lentil seeds: protein isolation and cDNA cloning. *J Allergy Clin Immunol*. 2003;112(6):1208-1215.

1546. Blankestijn MA, den Hartog Jager CF, Blom WM, et al. A subset of walnut allergic adults is sensitized to walnut 11S globulin Jug r 4. *Clin Exp Allergy*. 2018;48(9):1206-1213.

1547. Kabasser S, Hafner C, Chinthrajah S, et al. Identification of Pru du 6 as a potential marker allergen for almond allergy. *Allergy*. 2021;76(5):1463-1472.

1548. Magni C, Ballabio C, Restani P, et al. Molecular insight into IgE-mediated reactions to sesame (*Sesamum indicum* L.) seed proteins. *Ann Allergy Asthma Immunol*. 2010;105(6):458-464.

1549. Klemans RJ, Otte D, Knol M, et al. The diagnostic value of specific IgE to Ara h 2 to predict peanut allergy in children is comparable to a validated and updated diagnostic prediction model. *J Allergy Clin Immunol*. 2013;131(1):157-163.

1550. Ballmer-Weber BK, Lidholm J, Lange L, et al. Allergen recognition patterns in walnut allergy are age dependent and correlate with the severity of allergic reactions. *J Allergy Clin Immunol Pract*. 2019;7(5):1560-1567.

1551. Garcia-Blanca A, Aranda A, Blanca-Lopez N, et al. Influence of age on IgE response in peanut-allergic children and adolescents from the Mediterranean area. *Pediatr Allergy Immunol*. 2015;26(6):497-502.

1552. Villalta D, Scala E, Mistrello G, Amato S, Asero R. Evidence of cross-reactivity between different seed storage proteins from hazelnut (*Corylus avellana*) and Walnut (*Juglans regia*) using recombinant allergen proteins. *Int Arch Allergy Immunol*. 2019;178(1):89-92.

1553. Bublin M, Breiteneder H. Cross-reactivities of non-homologous allergens. *Allergy*. 2020;75(5):1019-1022.

1554. Bublin M, Kostadinova M, Radauer C, et al. IgE cross-reactivity between the major peanut allergen Ara h 2 and the nonhomologous allergens Ara h 1 and Ara h 3. *J Allergy Clin Immunol*. 2013;132(1):118-124.

1555. Croote D, Darmanis S, Nadeau KC, Quake SR. High-affinity allergen-specific human antibodies cloned from single IgE B cell transcriptomes. *Science*. 2018;362(6420):1306-1309.

1556. Stiefel G, Anagnostou K, Boyle RJ, et al. BSACI guideline for the diagnosis and management of peanut and tree nut allergy. *Clin Exp Allergy*. 2017;47(6):719-739.

1557. Chan ES, Greenhawt MJ, Fleischer DM, Caubet JC. Managing cross-reactivity in those with peanut allergy. *J Allergy Clin Immunol Pract*. 2019;7(2):381-386.

1558. Martínez San Ireneo M, Ibáñez MD, Fernández-Caldas E, Carnés J. *In vitro* and *in vivo* cross-reactivity studies of legume allergy in a Mediterranean population. *Int Arch Allergy Immunol*. 2008;147(3):222-230.

1559. Masthoff LJ, van Hoffen E, Mattsson L, et al. Peanut allergy is common among hazelnut-sensitized subjects but is not primarily the result of IgE cross-reactivity. *Allergy*. 2015;70(3):265-274.

1560. Valcour A, Lidholm J, Borres MP, Hamilton RG. Sensitization profiles to hazelnut allergens across the United States. *Ann Allergy Asthma Immunol*. 2019;122(1):111-116.e111.

1561. Inomata N, Okazaki F, Moriyama T, et al. Identification of peamalein as a marker allergen related to systemic reactions in peach allergy. *Ann Allergy Asthma Immunol*. 2014;112(2):175-177.

1562. Su T, Han M, Cao D, Xu M. Molecular and biological properties of snakins: the foremost cysteine-rich plant host defense peptides. *J Fungi (Basel)*. 2020;6(4).

1563. Tanaka N, Konishi H, Khan MM, Komatsu S. Proteome analysis of rice tissues by two-dimensional electrophoresis: an approach to the investigation of gibberellin regulated proteins. *Mol Genet Genomics*. 2004;270(6):485-496.
1524. Immonen A, Kinnunen T, Sirven P, et al. The major horse allergen Equ c 1 contains one immunodominant region of T cell epitopes. *Clin Exp Allergy*. 2007;37(6):939-947.

1525. Haka J, Niemi MH, Mattila P, Jänis J, Takkinen K, Rouvinen J. Development of hypoallergenic variants of the major horse allergen Equ c 1 for immunotherapy by rational structure based engineering. *Sci Rep*. 2019;9(1):20148.

1526. Wintersand A, Alsved M, Jakobsson J, et al. Individual airborne characteristics of dog allergens. *Clin Exp Allergy*. 2021.

1527. Custovic A, Green R, Fletcher A, et al. Aerodynamic properties of the major dog allergen Can f 1: distribution in homes, concentration, and particle size of allergen in the air. *Am J Respir Crit Care Med*. 1997;155(1):94-98.

1528. Chruszcz M, Kapingidza AB, Dolamore C, Kowal K. A robust method for the estimation and visualization of IgE cross-reactivity likelihood between allergens belonging to the same protein family. *PLoS One*. 2018;13(11):e0208276.

1529. Hilger C, Swiontek K, Arumugam K, Lehners C, Hentges F. Identification of a new major dog allergen highly cross-reactive with Fel d 4 in a population of cat- and dog-sensitized patients. *J Allergy Clin Immunol*. 2012;129(4):1149-1151.

1530. Apostolovic D, Sánchez-Vidaurre S, Waden K, et al. The cat lipocalin Fel d 7 and its cross-reactivity with the dog lipocalin Can f 1. *Allergy*. 2016;71(10):1490-1495.

1531. Hemmer W, Sestak-Greinecker G, Braunsteiner T, Wantke F, Wöhrl S. Molecular sensitization patterns in animal allergy: Relationship with clinical relevance and pet ownership. *Allergy*. 2021;76:3687-3696.

1532. Madhurantakam C, Nilsson OB, Uchtenhagen H, et al. Crystal structure of the dog lipocalin allergen Can f 2: implications for cross-reactivity to the cat allergen Fel d 4. *J Mol Biol*. 2010;401(1):68-83.

1533. Mattsson L, Lundgren T, Olsson P, Sundberg M, Lidholm J. Molecular and immunological characterization of Can f 4: a dog dander allergen cross-reactive with a 23 kDa odorant-binding protein in cow dander. *Clin Exp Allergy*. 2010;40(8):1276-1287.

1534. Jakob T, Hilger C, Hentges F. Clinical relevance of sensitization to cross-reactive lipocalin Can f 6. *Allergy*. 2013;68(5):690-691.

1535. Shewry PR, Napier JA, Tatham AS. Seed storage proteins: structures and biosynthesis. *Plant Cell*. 1995;7(7):945-956.

1536. Slavokhotova AA, Rogozhin EA. Defense peptides from the α-hairpinin family are components of plant innate immunity. *Front Plant Sci*. 2020;11:465.

1537. Aalberse RC, Mueller GA, Derksen NIL, et al. Identification of the amino-terminal fragment of Ara h 1 as a major target of the IgE-binding activity in the basic peanut protein fraction. *Clin Exp Allergy*. 2020;50(3):401-405.

1538. Peeters KA, Koppelman SJ, Penninks AH, et al. Clinical relevance of sensitization to lupine in peanut-sensitized adults. *Allergy*. 2009;64(4):549-555.

1539. Verhoeckx KCM, Vissers YM, Baumert JL, et al. Food processing and allergenicity. *Food Chem Toxicol*. 2015;80:223-240.

1540. Klemans RJ, van Os-Medendorp H, Blankestijn M, Bruijnzeel-Koomen CA, Knol EF, Knulst AC. Diagnostic accuracy of specific IgE to components in diagnosing peanut allergy: a systematic review. *Clin Exp Allergy*. 2015;45(4):720-730.

1541. Lange L, Lasota L, Finger A, et al. Ana o 3-specific IgE is a good predictor for clinically relevant cashew allergy in children. *Allergy*. 2017;72(4):598-603.

1542. Sato S, Yamamoto M, Yanagida N, et al. Jug r 1 sensitization is important in walnut-allergic children and youth. *J Allergy Clin Immunol Pract*. 2017;5(6):1784-1786.

1543. Cabanillas B, Jappe U, Novak N. Allergy to peanut, soybean, and other legumes: recent advances in allergen characterization, stability to processing and IgE cross-reactivity. *Mol Nutr Food Res*. 2018;62(1).

1544. Geiselhart S, Hoffmann-Sommergruber K, Bublin M. Tree nut allergens. *Mol Immunol*. 2018;100:71-81.

1545. López-Torrejón G, Salcedo G, Martín-Esteban M, Díaz-Perales A, Pascual CY, Sánchez-Monge R. Len c 1, a major allergen and vicilin from lentil seeds: protein isolation and cDNA cloning. *J Allergy Clin Immunol*. 2003;112(6):1208-1215.

1546. Blankestijn MA, den Hartog Jager CF, Blom WM, et al. A subset of walnut allergic adults is sensitized to walnut 11S globulin Jug r 4. *Clin Exp Allergy*. 2018;48(9):1206-1213.

1547. Kabasser S, Hafner C, Chinthrajah S, et al. Identification of Pru du 6 as a potential marker allergen for almond allergy. *Allergy*. 2021;76(5):1463-1472.

1548. Magni C, Ballabio C, Restani P, et al. Molecular insight into IgE-mediated reactions to sesame (*Sesamum indicum* L.) seed proteins. *Ann Allergy Asthma Immunol*. 2010;105(6):458-464.

1549. Klemans RJ, Otte D, Knol M, et al. The diagnostic value of specific IgE to Ara h 2 to predict peanut allergy in children is comparable to a validated and updated diagnostic prediction model. *J Allergy Clin Immunol*. 2013;131(1):157-163.

1550. Ballmer-Weber BK, Lidholm J, Lange L, et al. Allergen recognition patterns in walnut allergy are age dependent and correlate with the severity of allergic reactions. *J Allergy Clin Immunol Pract*. 2019;7(5):1560-1567.

1551. Garcia-Blanca A, Aranda A, Blanca-Lopez N, et al. Influence of age on IgE response in peanut-allergic children and adolescents from the Mediterranean area. *Pediatr Allergy Immunol*. 2015;26(6):497-502.

1552. Villalta D, Scala E, Mistrello G, Amato S, Asero R. Evidence of cross-reactivity between different seed storage proteins from hazelnut (*Corylus avellana*) and Walnut (*Juglans regia*) using recombinant allergen proteins. *Int Arch Allergy Immunol*. 2019;178(1):89-92.

1553. Bublin M, Breiteneder H. Cross-reactivities of non-homologous allergens. *Allergy*. 2020;75(5):1019-1022.

1554. Bublin M, Kostadinova M, Radauer C, et al. IgE cross-reactivity between the major peanut allergen Ara h 2 and the nonhomologous allergens Ara h 1 and Ara h 3. *J Allergy Clin Immunol*. 2013;132(1):118-124.

1555. Croote D, Darmanis S, Nadeau KC, Quake SR. High-affinity allergen-specific human antibodies cloned from single IgE B cell transcriptomes. *Science*. 2018;362(6420):1306-1309.

1556. Stiefel G, Anagnostou K, Boyle RJ, et al. BSACI guideline for the diagnosis and management of peanut and tree nut allergy. *Clin Exp Allergy*. 2017;47(6):719-739.

1557. Chan ES, Greenhawt MJ, Fleischer DM, Caubet JC. Managing cross-reactivity in those with peanut allergy. *J Allergy Clin Immunol Pract*. 2019;7(2):381-386.

1558. Martínez San Ireneo M, Ibáñez MD, Fernández-Caldas E, Carnés J. *In vitro* and *in vivo* cross-reactivity studies of legume allergy in a Mediterranean population. *Int Arch Allergy Immunol*. 2008;147(3):222-230.

1559. Masthoff LJ, van Hoffen E, Mattsson L, et al. Peanut allergy is common among hazelnut-sensitized subjects but is not primarily the result of IgE cross-reactivity. *Allergy*. 2015;70(3):265-274.

1560. Valcour A, Lidholm J, Borres MP, Hamilton RG. Sensitization profiles to hazelnut allergens across the United States. *Ann Allergy Asthma Immunol*. 2019;122(1):111-116.e111.

1561. Inomata N, Okazaki F, Moriyama T, et al. Identification of peamalein as a marker allergen related to systemic reactions in peach allergy. *Ann Allergy Asthma Immunol*. 2014;112(2):175-177.

1562. Su T, Han M, Cao D, Xu M. Molecular and biological properties of snakins: the foremost cysteine-rich plant host defense peptides. *J Fungi (Basel)*. 2020;6(4).

1563. Tanaka N, Konishi H, Khan MM, Komatsu S. Proteome analysis of rice tissues by two-dimensional electrophoresis: an approach to the investigation of gibberellin regulated proteins. *Mol Genet Genomics*. 2004;270(6):485-496.