REFERENCES

1. Gessain A, Cassar O. 2012. Epidemiological aspects and world distribution of HTLV-1 infection. Front Microbiol 3:388. https://doi.org/10.3389/fmicb.2012.00388

2. Martin F, Tagaya Y, Gallo R. 2018. Time to eradicate HTLV-1: an open letter to WHO. The Lancet 391:1893–1894. https://doi.org/10.1016/S0140-6736(18)30974-7

3. Yoshida M, Seiki M, Yamaguchi K, Takatsuki K. 1984. Monoclonal integration of human T-cell leukemia provirus in all primary tumors of adult T-cell leukemia suggests causative role of human T-cell leukemia virus in the disease. Proc Natl Acad Sci USA 81:2534–2537. https://doi.org/10.1073/pnas.81.8.2534

4. Uchiyama T, Yodoi J, Sagawa K, Takatsuki K, Uchino H. 1977. Adult T-cell leukemia: clinical and hematologic features of 16 cases. Blood 50:481–492. https://doi.org/10.1182/blood.V50.3.481.481

5. Gessain A, Barin F, Vernant JC, Gout O, Maurs L, Calender A, de Thé G. 1985. Antibodies to human T-lymphotropic virus type-I in patients with tropical spastic paraparesis. Lancet 2:407–410. https://doi.org/10.1016/S0140-6736(85)92734-5

6. Nakagawa M, Izumo S, Ijichi S, Kubota H, Arimura K, Kawabata M, Osame M. 1995. HTLV-I-associated myelopathy: analysis of 213 patients based on clinical features and laboratory findings. J Neurovirol 1:50–61. https://doi.org/10.3109/13550289509111010

7. Proietti FA, Carneiro-Proietti ABF, Catalan-Soares BC, Murphy EL. 2005. Global epidemiology of HTLV-I infection and associated diseases. Oncogene 24:6058–6068. https://doi.org/10.1038/sj.onc.1208968

8. Manns A, Hisada M, Grenade LL. 1999. Human T-lymphotropic virus type I infection. The Lancet 353:1951–1958. https://doi.org/10.1016/s0140-6736(98)09460-4

9. Wills JW, Craven RC. 1991. Form, function, and use of retroviral gag proteins. AIDS 5:639–654. https://doi.org/10.1097/00002030-199106000-00002

10. Le Blanc I, Grange MP, Delamarre L, Rosenberg AR, Blot V, Pique C, Dokhélar MC. 2001. HTLV-1 structural proteins. Virus Res 78:5–16. https://doi.org/10.1016/s0168-1702(01)00278-7

11. Maldonado JO, Cao S, Zhang W, Mansky LM. 2016. Distinct morphology of human T-cell leukemia virus type 1-like particles. Viruses 8:132. https://doi.org/10.3390/v8050132

12. Meissner ME, Mendonça LM, Zhang W, Mansky LM. 2017. Polymorphic nature of human T-cell leukemia virus type 1 particle cores as revealed through characterization of a chronically infected cell line. J Virol 91:e00369-17. https://doi.org/10.1128/JVI.00369-17

13. Miyamoto K, Tomita N, Ishii A, Nishizaki T, Kitajima K, Tanaka T, Nakamura T, Watanabe S, Oda T. 1984. Transformation of ATLA-negative leukocytes by blood components from anti-ATLA-positive donors in vitro. Int J Cancer 33:721–725. https://doi.org/10.1002/ijc.2910330603

14. Donegan E, Lee H, Operskalski EA, Shaw GM, Kleinman SH, Busch MP, Stevens CE, Schiff ER, Nowicki MJ, Hollingsworth CG, Mosley JW, Buckley JD, Gaiennie J, Harris M, Kasper CK, Pike MC, Succar M, Zhou Y, Dietrich SL. 1994. Transfusion transmission of Retroviruses: Human T-Lymphotropic virus types I and II compared with human immunodeficiency virus type 1. Transfusion 34:478–483. https://doi.org/10.1046/j.1537-2995.1994.34694295061.x

15. Yamamoto N, Okada M, Koyanagi Y, Kannagi M, Hinuma Y. 1982. Transformation of human leukocytes by cocultivation with an adult T cell leukemia virus producer cell line. Science 217:737–739. https://doi.org/10.1126/science.6980467

16. Alais S, Mahieux R, Dutartre H. 2015. Viral source-independent high susceptibility of dendritic cells to human T-cell leukemia virus type 1 infection compared to that of T lymphocytes. J Virol 89:10580–10590. https://doi.org/10.1128/JVI.01799-15

17. Pique C, Jones KS. 2012. Pathways of cell-cell transmission of HTLV-1. Front Microbiol 3:378. https://doi.org/10.3389/fmicb.2012.00378

18. Igakura T, Stinchcombe JC, Goon PKC, Taylor GP, Weber JN, Griffiths GM, Tanaka Y, Osame M, Bangham CRM. 2003. Spread of HTLV-I between lymphocytes by virus-induced polarization of the cytoskeleton. Science 299:1713–1716. https://doi.org/10.1126/science.1080115

19. Van Prooyen N, Gold H, Andresen V, Schwartz O, Jones K, Ruscetti F, Lockett S, Gudla P, Venzon D, Franchini G. 2010. Human T-cell leukemia virus type 1 P8 protein increases cellular conduits and virus

transmission. Proc Natl Acad Sci USA 107:20738–20743. https://doi.org/10.1073/pnas.1009635107

20. Hiraiwa N, Hiraiwa M, Kannagi R. 1997. Human T-cell leukemia virus-1 encoded tax protein transactivates alpha 1→3 fucosyltransferase Fuc-T VII, which synthesizes sialyl Lewis X, a selectin ligand expressed on adult T-cell leukemia cells. Biochem Biophys Res Commun 231:183–186. https://doi.org/10.1006/bbrc.1997.6068

21. Tarasevich A, Filatov A, Pichugin A, Mazurov D. 2015. Monoclonal antibody profiling of cell surface proteins associated with the viral biofilms on HTLV-1 transformed cells. Acta Virol 59:247–256. https://doi.org/10.4149/av_2015_03_247

22. Assil S, Futsch N, Décembre E, Alais S, Gessain A, Cosset F-L, Mahieux R, Dreux M, Dutartre H. 2019. Sensing of cell-associated HTLV by plasmacytoid dendritic cells is regulated by dense β-galactoside glycosylation. PLoS Pathog 15:e1007589. https://doi.org/10.1371/journal.ppat.1007589

23. Millen S, Gross C, Donhauser N, Mann MC, Péloponèse Jr. J-M, Thoma-Kress AK. 2019. Collagen IV (COL4A1, COL4A2), a component of the viral biofilm, is induced by the HTLV-1 oncoprotein tax and impacts virus transmission. Front Microbiol 10:2439. https://doi.org/10.3389/fmicb.2019.02439

24. Pais-Correia A-M, Sachse M, Guadagnini S, Robbiati V, Lasserre R, Gessain A, Gout O, Alcover A, Thoulouze M-I. 2010. Biofilm-like extracellular viral assemblies mediate HTLV-1 cell-to-cell transmission at virological synapses. Nat Med 16:83–89. https://doi.org/10.1038/nm.2065

25. Thoulouze M-I, Alcover A. 2011. Can viruses form biofilms? Trends Microbiol 19:257–262. https://doi.org/10.1016/j.tim.2011.03.002

26. Maali Y, Journo C, Mahieux R, Dutartre H. 2020. Microbial biofilms: human T-cell leukemia virus type 1 first in line for viral biofilm but far behind bacterial biofilms. Front Microbiol 10:2141. https://doi.org/10.3389/fmicb.2020.02041

27. Charrin S, Jouannet S, Boucheix C, Rubinstein E. 2014. Tetraspanins at a glance. J Cell Sci 127:3641–3648. https://doi.org/10.1242/jcs.154906

28. Pileri P, Uematsu Y, Campagnoli S, Galli G, Falugi F, Petracca R, Weiner AJ, Houghton M, Rosa D, Grandi G, Abriignani S. 1998. Binding of hepatitis C virus to CD81. Science 282:938–941. https://doi.org/10.1126/science.282.5390.938

29. Scheffer KD, Gawlitza A, Spoden GA, Zhang XA, Lambert C, Berditchevski F, Florin L. 2013. Tetraspanin CD151 mediates papillomavirus type 16 endocytosis. J Virol 87:3435–3446. https://doi.org/10.1128/JVI.02906-12

30. Grigorov B, Attuil-Audenis V, Perugi F, Nedelec M, Watson S, Pique C, Darlix J-L, Conjeaud H, Muriaux D. 2009. A role for CD81 on the late steps of HIV-1 replication in a chronically infected T cell line. Retrovirology 6:28. https://doi.org/10.1186/1742-4690-6-28

31. Krentemsovd DN, Weng J, Lambelé M, Roy NH, Thali M. 2009. Tetraspanins regulate cell-to-cell transmission of HIV-1. Retrovirology 6:64. https://doi.org/10.1186/1742-4690-6-64

32. Deneka M, Pelchen-Matthews A, Byland R, Ruiz-Mateos E, Marsh M. 2007. In macrophages, HIV-1 assembles into an intracellular plasma membrane domain containing the tetraspanins CD81, CD9, and CD53. J Cell Biol 177:329–341. https://doi.org/10.1083/jcb.200609050

33. Mazurov D, Heidecker G, Derse D. 2007. The inner loop of tetraspanins CD82 and CD81 mediates interactions with human T cell lymphotrophic virus type 1 Gag protein. J Biol Chem 282:3896–3903. https://doi.org/10.1074/jbc.M607322200

34. Pique C, Lagaudrière-Gesbert C, Delamarre L, Rosenberg AR, Conjeaud H, Dokhélar MC. 2000. Interaction of CD82 tetraspanin proteins with HTLV-1 envelope glycoproteins inhibits cell-to-cell fusion and virus transmission. Virology 276:455–465. https://doi.org/10.1006/viro.2000.0538

35. Grigsby IF, Zhang W, Johnson JL, Fogarty KH, Chen Y, Rawson JM, Crosby AJ, Mueller JD, Mansky LM. 2010. Biophysical analysis of HTLV-1 particles reveals novel insights into particle morphology and Gag stoichiometry. Retrovirology 7:75. https://doi.org/10.1186/1742-4690-7-75

36. McNamara RP, Dittmer DP. 2020. Modern techniques for the isolation of extracellular vesicles and viruses. J Neuroimmune Pharmacol 15:459–472. https://doi.org/10.1007/s11481-019-09874-x

37. Gourdelier M, Swain J, Arone C, Mouttou A, Bracquemond D, Merida P, Saffarian S, Lyonnais S, Favard C, Muriaux D. 2022. Optimized production
and fluorescent labeling of SARS-CoV-2 virus-like particles. Sci Rep 12:14651. https://doi.org/10.1038/s41598-022-18681-z

38. Dufrêne YF, Boland T, Schneider JW, Barger WR, Lee GU. 1998. Characterization of the physical properties of model biomembranes at the nanometer scale with the atomic force microscope. Faraday Discuss 111:79-94. https://doi.org/10.1039/a807637e

39. Arone C, Dibsy R, Inamdar K, Lyonnais S, Arhel NJ, Favard C, Muriaux D. 2021. Illuminating the nanoscopic world of viruses by fluorescence super-resolution microscopy. Virologie (Montrouge) 25:47-60. https://doi.org/10.1684/vir.2021.0908

40. Cao S, Maldonado JO, Grigsby IF, Mansky LM, Zhang W. 2015. Analysis of human T-cell leukemia virus type 1 particles by using cryo-electron tomography. J Virol 89:2430-2435. https://doi.org/10.1128/JVI.02358-14

41. Gross C, Wiesmann V, Millen S, Kalmer M, Wittenberg T, Gettemans J, Thoma-Kress AK, Evans DT. 2016. The tax-inducible actin-bundling protein fascin is crucial for release and cell-to-cell transmission of human T-cell leukemia virus type. PLoS Pathog 12:e1005916. https://doi.org/10.1371/journal.ppat.1005916

42. GEO Accession viewer. Available from: https://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE17718. Retrieved. December 5, 2022

43. Gauthier S, Pelletier I, Ouellet M, Vargas A, Tremblay MJ, Sato S, Barbeau B. 2008. Induction of galectin-1 expression by HTLV-I tax and its impact on HTLV-I infectivity. Retrovirology 5:105. https://doi.org/10.1186/1742-4690-5-105

44. Bhat NK, Adachi Y, Samuel KP, Derse D. 1993. HTLV-1 gene expression by defective proviruses in an infected T-cell line. Virology 196:15-24. https://doi.org/10.1006/viro.1993.1450

45. Mazurov D, Ilinskaya A, Heidecker G, Filatov A. 2012. Role of O-glycosylation and expression of CD43 and CD45 on the surfaces of effector T cells in human T cell leukemia virus type 1 cell-to-cell infection. J Virol 86:2447-2458. https://doi.org/10.1128/JVI.06993-11

46. Charrin S, le Naour F, Silvie O, Milhiet P-E, Boucheix C, Rubinstein E. 2009. Lateral organization of membrane proteins: tetraspanins spin their web. Biochem J 420:133-154. https://doi.org/10.1042/BJ20082422

47. Termini CM, Gillette JM. 2017. Tetraspanins function as regulators of cellular signaling. Front Cell Dev Biol 5:34. https://doi.org/10.3389/fcell.2017.00034

48. Seigneuret M, Delaguillaumie A, Lagaudrière-Gesbert C, Conjeaud H. 2001. Structure of the tetraspanin main extracellular domain: a partially conserved fold with a structurally variable domain insertion*. J Biol Chem 276:40055-40064. https://doi.org/10.1074/jbc.M105557200

49. Zuidscherwoude M, Göttfert F, Dunlock VME, Figdor CG, van den Bogaart G, van Spriel AB. 2015. The tetraspanin web revisited by super-resolution microscopy. Sci Rep 5:12201. https://doi.org/10.1038/srep12201

50. Wang L, Liu L, Che Y, Wang L, Jiang L, Dong C, Zhang Y, Li Q. 2010. Egress of HSV-1 capsid requires the interaction of VP26 and a cellular tetraspanin membrane protein. J Virol 71:156. https://doi.org/10.1186/1743-422X-7-156

51. He J, Sun E, Bujny MV, Kim D, Davidson MW, Zhuang X. 2013. Dual function of CD81 in influenza virus uncoating and budding. PLoS Pathog 9:e1003701. https://doi.org/10.1371/journal.ppat.1003701

52. Jolly C, Sattentau QJ. 2007. Human immunodeficiency virus type 1 assembly, budding, and cell-cell spread in T cells take place in tetraspanin-enriched plasma membrane domains. J Virol 81:7873-7884. https://doi.org/10.1128/JVI.01845-06

53. Martin F, Roth DM, Jans DA, Pouton CW, Partridge LJ, Monk PN, Moseley GW. 2005. Tetraspanins in viral infections: a fundamental role in viral biology? J Virol 79:10839-10851. https://doi.org/10.1128/JVI.79.17.10839-10851.2005

54. Chertova E, Chertov O, Coren LV, Roser JD, Trubey CM, Bess JW, Sowder RC, Barsov E, Hood BL, Fisher RJ, Nagashima K, Conradts P, Veenstra TD, Lifson JD, Ott DE. 2006. Proteomic and biochemical analysis of purified human immunodeficiency virus type 1 produced from infected monocyte-derived macrophages. J Virol 80:9039-9052. https://doi.org/10.1128/JVI.01013-06

55. Mariani C, Desdouits M, Favard C, Benaroch P, Muriaux DM. 2014. Role of Gag and lipids during HIV-1 assembly in CD4(+) T cells and macrophages. Front Microbiol 5:312. https://doi.org/10.3389/fmicb.2014.00312

56. Grigorov B, Arcanger F, Roingeard P, Darlix J-L, Muriaux D. 2006. Assembly of infectious HIV-1 in human epithelial and T-lymphoblastic cell lines. J Mol Biol 359:848-862. https://doi.org/10.1016/j.jmb.2006.04.017

57. Dahmane S, Doucet C, Le Gall A, Chamontin C, Dosset P, Murcy F, Fernandez L, Salas D, Rubinstein E, Mougel M, Nollmann M, Milhiet P-E. 2019. Nanoscale organization of tetraspanins during HIV-1 budding by correlative dSTORM/AFM. Nanoscale 11:6036-6044. https://doi.org/10.1039/c8nr07269h

58. Roy NH, Chan J, Lambelé M, Thali M. 2013. Clustering and mobility of HIV-1 Env at viral assembly sites predict its propensity to induce cell-cell fusion. J Virol 87:7516-7525. https://doi.org/10.1128/JVI.00790-13

59. Termini CM, Cotter ML, Marjon KD, Buranda T, Lidke KA, Gillette JM. 2014. The membrane scaffold CD82 regulates cell adhesion by altering a4 integrin stability and molecular density. Mol Biol Cell 25:1560-1573. https://doi.org/10.1091/mbc.E13-11-0660

60. Li J, Xu J, Li L, Ianni A, Kumari P, Liu S, Sun P, Braun T, Tan X, Xiang R, Yue S. 2020. MGAT3-mediated glycosylation of tetraspanin CD82 at asparagine 157 suppresses ovarian cancer metastasis by inhibiting the integrin signaling pathway. Theranostics 10:6467-6482. https://doi.org/10.7150/thno.43865

61. Odintsova E, van Niel G, Conjeaud H, Raposo G, Iwamoto R, Mekada E, Berditchevski F. 2013. Metastasis suppressor tetraspanin CD82/KAI1 regulates ubiquitylation of epidermal growth factor receptor. J Biol Chem 288:26323-26334. https://doi.org/10.1074/jbc.M112.439380

62. Delaguillaumie A, Lagaudrière-Gesbert C, Popoff MR, Conjeaud H. 2002. Rho GTPases link cytoskeletal rearrangements and activation processes induced via the tetraspanin CD82 in T lymphocytes. J Cell Sci 115:433-443. https://doi.org/10.1242/jcs.115.2.433

63. Marjon KD, Termini CM, Karlen KL, Saito-Reis C, Soria CE, Lidke KA, Gillette JM. 2016. Tetraspanin CD82 regulates bone marrow homing of acute myeloid leukemia by modulating the molecular organization of N-cadherin. Oncogene 35:4132-4140. https://doi.org/10.1038/onc.2015.449

64. Stuck MW, Conley SM, Naash MI. 2015. Retinal degeneration slow (RDS) glycosylation plays a role in cone function and in the regulation of RDS-ROM-1 protein complex formation. J Biol Chem 290:27901-27913. https://doi.org/10.1074/jbc.M115.683698

65. Gurdap CO, Wedemann L, Sych T, Sezgin E. 2022. Influence of the extracellular domain size on the dynamic behavior of membrane proteins. Biophys J 121:3826-3836. https://doi.org/10.1016/j.bpj.2022.09.010

66. Fernandez L, Malrieu M, Bénistant C, Dosset P, Rubinstein E, Odintsova E, Berditchevski F, Milhiet P-E. 2021. CD82 and gangliosides tune CD81 membrane behavior. Int J Mol Sci 22:8459. https://doi.org/10.3390/ijms22168459

67. Wallis C, Melnick JL. 1967. Virus aggregation as the cause of the non-neutralizable persistent fraction. J Virol 1:478-488. https://doi.org/10.1128/JVI.1.3.478-488.1967

68. Galasso GJ. 1967. Quantitative studies on the quality, effects of aggregation and thermal inactivation of vesicular stomatitis virus. Archiv f Virusforschung 21:437-446. https://doi.org/10.1007/BF01241742

69. Inizan C, Caillet M, Desrames A, David A, Bomme P, Mallet A, Bourdic K, Lambotte O, Boufassa F, Mesel-Lemoine M, Tangy F, Pancino G, Mouquet H, Lagache T, Dufour A, Olivo-Marin J-C, Rey FA, Saez-Cirion A, Thoulouze M-I. 2021. HIV-1 Hijacks the cell extracellular matrix to spread collectively and efficiently between T lymphocytes. https://doi.org/10.1101/2021.09.27.461933

70. Malbec M, Sourisseau M, Guivel-Benhassine F, Porrot F, Blanchet F, Schwartz O, Casartelli N. 2013. HIV-1 Nef promotes the localization of Gag to the cell membrane and facilitates viral cell-to-cell transfer. Retrovirology 10:80. https://doi.org/10.1186/1742-4690-10-80

71. Cuevas JM, Durán-Moreno M, Sanjuán R. 2017. Multi-virion infectious units arise from free viral particles in an enveloped virus. Nat Microbiol 2:17078. https://doi.org/10.1038/nmicrobiol.2017.78

72. Morozov VA, Weiss RA. 1999. Two types of HTLV-1 particles are released from MT-2 cells. Virology 255:279-284. https://doi.org/10.1006/viro.1998.9578

73. Heidecker G, Lloyd PA, Fox K, Nagashima K, Derse D. 2004. Late assembly motifs of human T-cell leukemia virus type 1 and their relative roles in
and fluorescent labeling of SARS-CoV-2 virus-like particles. Sci Rep 12:14651. https://doi.org/10.1038/s41598-022-18681-z

38. Dufrêne YF, Boland T, Schneider JW, Barger WR, Lee GU. 1998. Characterization of the physical properties of model biomembranes at the nanometer scale with the atomic force microscope. Faraday Discuss 111:79-94. https://doi.org/10.1039/a807637e

39. Arone C, Dibsy R, Inamdar K, Lyonnais S, Arhel NJ, Favard C, Muriaux D. 2021. Illuminating the nanoscopic world of viruses by fluorescence super-resolution microscopy. Virologie (Montrouge) 25:47-60. https://doi.org/10.1684/vir.2021.0908

40. Cao S, Maldonado JO, Grigsby IF, Mansky LM, Zhang W. 2015. Analysis of human T-cell leukemia virus type 1 particles by using cryo-electron tomography. J Virol 89:2430-2435. https://doi.org/10.1128/JVI.02358-14

41. Gross C, Wiesmann V, Millen S, Kalmer M, Wittenberg T, Gettemans J, Thoma-Kress AK, Evans DT. 2016. The tax-inducible actin-bundling protein fascin is crucial for release and cell-to-cell transmission of human T-cell leukemia virus type. PLoS Pathog 12:e1005916. https://doi.org/10.1371/journal.ppat.1005916

42. GEO Accession viewer. Available from: https://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE17718. Retrieved. December 5, 2022

43. Gauthier S, Pelletier I, Ouellet M, Vargas A, Tremblay MJ, Sato S, Barbeau B. 2008. Induction of galectin-1 expression by HTLV-I tax and its impact on HTLV-I infectivity. Retrovirology 5:105. https://doi.org/10.1186/1742-4690-5-105

44. Bhat NK, Adachi Y, Samuel KP, Derse D. 1993. HTLV-1 gene expression by defective proviruses in an infected T-cell line. Virology 196:15-24. https://doi.org/10.1006/viro.1993.1450

45. Mazurov D, Ilinskaya A, Heidecker G, Filatov A. 2012. Role of O-glycosylation and expression of CD43 and CD45 on the surfaces of effector T cells in human T cell leukemia virus type 1 cell-to-cell infection. J Virol 86:2447-2458. https://doi.org/10.1128/JVI.06993-11

46. Charrin S, le Naour F, Silvie O, Milhiet P-E, Boucheix C, Rubinstein E. 2009. Lateral organization of membrane proteins: tetraspanins spin their web. Biochem J 420:133-154. https://doi.org/10.1042/BJ20082422

47. Termini CM, Gillette JM. 2017. Tetraspanins function as regulators of cellular signaling. Front Cell Dev Biol 5:34. https://doi.org/10.3389/fcell.2017.00034

48. Seigneuret M, Delaguillaumie A, Lagaudrière-Gesbert C, Conjeaud H. 2001. Structure of the tetraspanin main extracellular domain: a partially conserved fold with a structurally variable domain insertion*. J Biol Chem 276:40055-40064. https://doi.org/10.1074/jbc.M105557200

49. Zuidscherwoude M, Göttfert F, Dunlock VME, Figdor CG, van den Bogaart G, van Spriel AB. 2015. The tetraspanin web revisited by super-resolution microscopy. Sci Rep 5:12201. https://doi.org/10.1038/srep12201

50. Wang L, Liu L, Che Y, Wang L, Jiang L, Dong C, Zhang Y, Li Q. 2010. Egress of HSV-1 capsid requires the interaction of VP26 and a cellular tetraspanin membrane protein. J Virol 71:156. https://doi.org/10.1186/1743-422X-7-156

51. He J, Sun E, Bujny MV, Kim D, Davidson MW, Zhuang X. 2013. Dual function of CD81 in influenza virus uncoating and budding. PLoS Pathog 9:e1003701. https://doi.org/10.1371/journal.ppat.1003701

52. Jolly C, Sattentau QJ. 2007. Human immunodeficiency virus type 1 assembly, budding, and cell-cell spread in T cells take place in tetraspanin-enriched plasma membrane domains. J Virol 81:7873-7884. https://doi.org/10.1128/JVI.01845-06

53. Martin F, Roth DM, Jans DA, Pouton CW, Partridge LJ, Monk PN, Moseley GW. 2005. Tetraspanins in viral infections: a fundamental role in viral biology? J Virol 79:10839-10851. https://doi.org/10.1128/JVI.79.17.10839-10851.2005

54. Chertova E, Chertov O, Coren LV, Roser JD, Trubey CM, Bess JW, Sowder RC, Barsov E, Hood BL, Fisher RJ, Nagashima K, Conradts P, Veenstra TD, Lifson JD, Ott DE. 2006. Proteomic and biochemical analysis of purified human immunodeficiency virus type 1 produced from infected monocyte-derived macrophages. J Virol 80:9039-9052. https://doi.org/10.1128/JVI.01013-06

55. Mariani C, Desdouits M, Favard C, Benaroch P, Muriaux DM. 2014. Role of Gag and lipids during HIV-1 assembly in CD4(+) T cells and macrophages. Front Microbiol 5:312. https://doi.org/10.3389/fmicb.2014.00312

56. Grigorov B, Arcanger F, Roingeard P, Darlix J-L, Muriaux D. 2006. Assembly of infectious HIV-1 in human epithelial and T-lymphoblastic cell lines. J Mol Biol 359:848-862. https://doi.org/10.1016/j.jmb.2006.04.017

57. Dahmane S, Doucet C, Le Gall A, Chamontin C, Dosset P, Murcy F, Fernandez L, Salas D, Rubinstein E, Mougel M, Nollmann M, Milhiet P-E. 2019. Nanoscale organization of tetraspanins during HIV-1 budding by correlative dSTORM/AFM. Nanoscale 11:6036-6044. https://doi.org/10.1039/c8nr07269h

58. Roy NH, Chan J, Lambelé M, Thali M. 2013. Clustering and mobility of HIV-1 Env at viral assembly sites predict its propensity to induce cell-cell fusion. J Virol 87:7516-7525. https://doi.org/10.1128/JVI.00790-13

59. Termini CM, Cotter ML, Marjon KD, Buranda T, Lidke KA, Gillette JM. 2014. The membrane scaffold CD82 regulates cell adhesion by altering a4 integrin stability and molecular density. Mol Biol Cell 25:1560-1573. https://doi.org/10.1091/mbc.E13-11-0660

60. Li J, Xu J, Li L, Ianni A, Kumari P, Liu S, Sun P, Braun T, Tan X, Xiang R, Yue S. 2020. MGAT3-mediated glycosylation of tetraspanin CD82 at asparagine 157 suppresses ovarian cancer metastasis by inhibiting the integrin signaling pathway. Theranostics 10:6467-6482. https://doi.org/10.7150/thno.43865

61. Odintsova E, van Niel G, Conjeaud H, Raposo G, Iwamoto R, Mekada E, Berditchevski F. 2013. Metastasis suppressor tetraspanin CD82/KAI1 regulates ubiquitylation of epidermal growth factor receptor. J Biol Chem 288:26323-26334. https://doi.org/10.1074/jbc.M112.439380

62. Delaguillaumie A, Lagaudrière-Gesbert C, Popoff MR, Conjeaud H. 2002. Rho GTPases link cytoskeletal rearrangements and activation processes induced via the tetraspanin CD82 in T lymphocytes. J Cell Sci 115:433-443. https://doi.org/10.1242/jcs.115.2.433

63. Marjon KD, Termini CM, Karlen KL, Saito-Reis C, Soria CE, Lidke KA, Gillette JM. 2016. Tetraspanin CD82 regulates bone marrow homing of acute myeloid leukemia by modulating the molecular organization of N-cadherin. Oncogene 35:4132-4140. https://doi.org/10.1038/onc.2015.449

64. Stuck MW, Conley SM, Naash MI. 2015. Retinal degeneration slow (RDS) glycosylation plays a role in cone function and in the regulation of RDS-ROM-1 protein complex formation. J Biol Chem 290:27901-27913. https://doi.org/10.1074/jbc.M115.683698

65. Gurdap CO, Wedemann L, Sych T, Sezgin E. 2022. Influence of the extracellular domain size on the dynamic behavior of membrane proteins. Biophys J 121:3826-3836. https://doi.org/10.1016/j.bpj.2022.09.010

66. Fernandez L, Malrieu M, Bénistant C, Dosset P, Rubinstein E, Odintsova E, Berditchevski F, Milhiet P-E. 2021. CD82 and gangliosides tune CD81 membrane behavior. Int J Mol Sci 22:8459. https://doi.org/10.3390/ijms22168459

67. Wallis C, Melnick JL. 1967. Virus aggregation as the cause of the non-neutralizable persistent fraction. J Virol 1:478-488. https://doi.org/10.1128/JVI.1.3.478-488.1967

68. Galasso GJ. 1967. Quantitative studies on the quality, effects of aggregation and thermal inactivation of vesicular stomatitis virus. Archiv f Virusforschung 21:437-446. https://doi.org/10.1007/BF01241742

69. Inizan C, Caillet M, Desrames A, David A, Bomme P, Mallet A, Bourdic K, Lambotte O, Boufassa F, Mesel-Lemoine M, Tangy F, Pancino G, Mouquet H, Lagache T, Dufour A, Olivo-Marin J-C, Rey FA, Saez-Cirion A, Thoulouze M-I. 2021. HIV-1 Hijacks the cell extracellular matrix to spread collectively and efficiently between T lymphocytes. https://doi.org/10.1101/2021.09.27.461933

70. Malbec M, Sourisseau M, Guivel-Benhassine F, Porrot F, Blanchet F, Schwartz O, Casartelli N. 2013. HIV-1 Nef promotes the localization of Gag to the cell membrane and facilitates viral cell-to-cell transfer. Retrovirology 10:80. https://doi.org/10.1186/1742-4690-10-80

71. Cuevas JM, Durán-Moreno M, Sanjuán R. 2017. Multi-virion infectious units arise from free viral particles in an enveloped virus. Nat Microbiol 2:17078. https://doi.org/10.1038/nmicrobiol.2017.78

72. Morozov VA, Weiss RA. 1999. Two types of HTLV-1 particles are released from MT-2 cells. Virology 255:279-284. https://doi.org/10.1006/viro.1998.9578

73. Heidecker G, Lloyd PA, Fox K, Nagashima K, Derse D. 2004. Late assembly motifs of human T-cell leukemia virus type 1 and their relative roles in
particle release. J Virol 78:6636-6648. https://doi.org/10.1128/JVI.78.12.6636-6648.2004

74. Zufferey R, Nagy D, Mandel RJ, Naldini L, Trono D. 1997. Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo. Nat Biotechnol 15:871-875. https://doi.org/10.1038/nbt0997-871

75. Burniston MT, Cimarelli A, Colgan J, Curtis SP, Luban J. 1999. Human immunodeficiency virus type 1 Gag polyprotein multimerization requires the nucleocapsid domain and RNA and is promoted by the capsid-dimer interface and the basic region of matrix protein. J Virol 73:8527-8540. https://doi.org/10.1128/JVI.73.10.8527-8540.1999
particle release. J Virol 78:6636-6648. https://doi.org/10.1128/JVI.78.12.6636-6648.2004

74. Zufferey R, Nagy D, Mandel RJ, Naldini L, Trono D. 1997. Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo. Nat Biotechnol 15:871-875. https://doi.org/10.1038/nbt0997-871

75. Burniston MT, Cimarelli A, Colgan J, Curtis SP, Luban J. 1999. Human immunodeficiency virus type 1 Gag polyprotein multimerization requires the nucleocapsid domain and RNA and is promoted by the capsid-dimer interface and the basic region of matrix protein. J Virol 73:8527-8540. https://doi.org/10.1128/JVI.73.10.8527-8540.1999