Additional file 1 of RNAi-mediated knockdown of gut receptor-like genes prohibitin and α-amylase altered the susceptibility of Galleria mellonella to Cry1AcF toxin
Creators: name: Dutta, Tushar K.
name: Mandal, Abhishek
name: Kundu, Artha
name: Phani, Victor
name: Mathur, Chetna
name: Veeresh, Arudhimath
name: Sreevathsa, Rohini
Publisher: name: figshare
Year: 2022
Subjects: subject: Biochemistry
subject: Medicine
subject: Genetics
subject: FOS: Biological sciences
subject: Molecular Biology
subject: 39999 Chemical Sciences not elsewhere classified
subject: FOS: Chemical sciences
subject: Ecology
subject: Cancer
subject: 110309 Infectious Diseases
subject: FOS: Health sciences

description: Additionalfile 1: Supplementary Figure S1. Protein-protein interaction between Cry1AcF ligand and known gut receptors CAD, ABCC2, ALP and APN1. Cry1AcF bound with these receptors via a number of Pi interactions, hydrogen bonds and salt bridges. The ZDock scores (greater value indicates greater contact surface area between ligand and receptor) for Cry-CAD, Cry-ABCC2, Cry-ALP and Cry-APN1 complexes were 2321, 1907, 2189 and 2060 Å2, respectively. Domain I, II and III of Cry1AcF arehighlighted in magenta, ochre yellow and green color, respectively. Supplementary Figure S2. Evolutionary relationship of ADAM protein from G. mellonella with their corresponding homologues from other insect species. The phylogenetic treewas constructed in MEGA X software using Maximum Likelihood method; best model was selected via MODELTEST using Le and Gascuel method. Bootstrap consensus was inferred from 1000 replicates and branches corresponding to &lt; 70% replicates were collapsed. The analyses included 61 amino acid sequences. NCBI accessionnumbers of different entries are provided in parentheses. All gaps and missingdata positions were eliminated after sequence alignment. Homo sapiens sequencefor the corresponding protein was used as the out-group (marked with ●), and G. mellonella entry is indicated in bold font. Entries in blue, black, red and green correspond to the members of the order Hymenoptera, Isoptera, Coleoptera and Lepidoptera, respectively. Supplementary Figure S3. Evolutionary relationship of prohibitin protein from G. mellonella with their corresponding homologues from other insect species. The phylogenetic tree was constructed in MEGA X software using Maximum Likelihood method; best model was selected via MODELTEST using Le and Gascuel method. Bootstrap consensus was inferred from 1000 replicates and branches corresponding to &lt; 70% replicates were collapsed. The analyses included 88 amino acid sequences. NCBI accession numbers ofdifferent entries are provided in parentheses. All gaps and missing data positions were eliminated after sequence alignment. Homo sapiens sequence for the corresponding protein was used as the out-group (marked with ●), and G. mellonella entry is indicated in bold font. Entries in red, teal, green, black,blue, purple, fuchsia, olive, maroon, grey and aqua correspond to the membersof the order Lepidoptera, Phasmatodea, Dictyoptera, Psocoptera, Coleoptera, Hemiptera, Zygentoma, Collembola, Hymenoptera, Siphonaptera and Diptera,respectively. Supplementary Figure S4. Evolutionary relationship of GLTP protein from G. mellonella with their corresponding homologues from insect species of different orders. The phylogenetic tree was constructed in MEGA X software using Maximum Likelihood method; best model was selected via MODELTEST using Le and Gascuel method. Bootstrap consensus was inferred from 1000 replicates and branches corresponding to &lt; 50% replicates were collapsed. The analyses included 77 amino acid sequences. A discrete Gamma distribution was used to model evolutionary rate differences among sites [5 categories (+G, parameter = 2.2830)]. Initial tree(s) for the heuristic search were obtained by applying the Neighbour-Joining method to a matrix of pairwise distances estimated using a JTT model, and then selecting the topology with superior log likelihood value). NCBI accession numbers of different entries are provided in parentheses. All gaps and missing data positions were eliminated after sequence alignment. Homo sapiens sequence for the corresponding protein was used as theout-group (marked with ●), and G. mellonella entry is indicated in bold font. Entries in blue, black, green, purple, teal, fuchsia and red correspond to the representative members of orders Hymenoptera, Thysanoptera, Ephemeroptera, Isoptera, Hemiptera, Phasmatodea and Lepidoptera, respectively. Supplementary Figure S5. Evolutionary relationship of arylphorin protein from G. mellonella with their corresponding homologues from insect species of different orders. The phylogenetic tree was constructed in MEGA X software using Maximum Likelihood method; best model was selected via MODELTEST using Le and Gascuel method. Bootstrap consensus was inferred from 1000 replicates and branches corresponding to &lt; 50% replicates were collapsed. The analyses included 45 amino acid sequences. A discrete Gamma distribution was used to model evolutionary rate differences among sites [5 categories (+G, parameter =1.4705)]. Initial tree(s) for the heuristic search were obtained by applying the Neighbour-Joining method to a matrix of pairwise distances estimated using a JTT model, and then selecting the topology with superior log likelihood value). NCBI accession numbers of different entries are provided in parentheses. All gaps and missing data positions were eliminated after sequence alignment. G. mellonella entry is indicated in bold font. Entries in blue, black, red and green correspond to the representative members of orders Lepidoptera, Siphonaptera and Diptera, respectively. No outgroup has been used inthe analyses because arylphorin orthologue was not found in Homo sapiens. Supplementary Figure S6. Evolutionary relationship of UDP-GT protein from G. mellonella with their corresponding homologues from insect species of order Lepidoptera. The phylogenetic tree was constructed in MEGA X software using Maximum Likelihood method; best model was selected via MODELTEST using Le and Gascuel method. Bootstrap consensus was inferred from 1000 replicates and branches corresponding to &lt; 50% replicates were collapsed. The analyses included 24 amino acid sequences. A discrete Gamma distribution was used to model evolutionary rate differences among sites [5 categories (+G, parameter =1.3839)]. Initial tree(s) for the heuristic search were obtained by applying the Neighbour-Joining method to a matrix of pairwise distances estimated using a JTT model, and then selecting the topology with superior log likelihood value). NCBI accession numbers of different entries are provided in parentheses. All gaps and missing data positions were eliminated after sequence alignment. Homo sapiens sequence for the corresponding protein was used as the out-group (marked with ●), and G. mellonella entry is indicated in bold font. Supplementary Figure S7. Evolutionary relationship of α-amylase protein from G. mellonella with their corresponding homologues from insect species of order Lepidoptera. The phylogenetic tree was constructed in MEGA X software using Maximum Likelihood method; best model was selected via MODELTEST using Le and Gascuel method. Bootstrap consensus was inferred from 1000 replicates and branches corresponding to &lt; 70% replicates were collapsed. The analyses included 37 amino acid sequences. A discrete Gamma distribution was used to model evolutionary rate differences among sites [5 categories (+G, parameter =0.9598)]. Initial tree(s) for the heuristic search were obtained by applying the Neighbour-Joining method to a matrix of pairwise distances estimated using a JTT model, and then selecting the topology with superior log likelihood value). NCBI accession numbers of different entries are provided in parentheses. All gaps and missing data positions were eliminated after sequence alignment. Homo sapiens sequence for the corresponding protein was used as the out-group (marked with ●), and G. mellonella entry is indicated in bold font. Supplementary Figure S8. The conserved motif distribution of ADAM proteins across the different insect orders. Each categorized motif logo generated by MEME is displayed in differentially colored boxes. Legend (at the bottom) depicts the protein sequence of corresponding motifs. Motifs were serially numbered according to their frequency of occurrence in MEME bioinformatics tool. Supplementary Figure S9. The conserved motif distribution of prohibitin proteins across the different insect orders. Each categorized motif logo generated by MEME is displayed in differentially colored boxes. Legend (at the bottom right) depicts the protein sequence of corresponding motifs. Motifs were serially numbered according to their frequency of occurrence in MEME bioinformatics tool. Supplementary Figure S10. The conserved motif distribution of UDP-GT proteins across the different insect orders. Each categorized motif logo generated by MEME is displayed in differentially colored boxes. Legend (at the bottom) depicts the protein sequence of corresponding motifs. Motifs were serially numbered according to their frequency of occurrence in MEME bioinformatics tool. Supplementary Figure S11. The conserved motif distribution of α-amylase proteins across the different insect orders. Each categorized motif logo generated by MEME is displayed in differentially colored boxes. Legend (at the bottom right) depicts the protein sequence of corresponding motifs. Motifs were serially numbered according to their frequency of occurrence in MEME bioinformatics tool. Supplementary Figure S12. The conserved motif distribution of arylphorin proteins across the different insect orders. Each categorized motif logo generated by MEME is displayed in differentially colored boxes. Legend (at the right hand side) depicts the protein sequence of corresponding motifs. Motifs were serially numbered according to their frequency of occurrence in MEME bioinformatics tool. Supplementary Figure S13. The conserved motif distribution of GLTP proteins across the different insect orders. Each categorized motif logo generated by MEME is displayed in differentially colored boxes. Legend (at the bottom right) depicts the protein sequence of corresponding motifs. Motifs were serially numbered according to their frequency of occurrence in MEME bioinformatics tool.