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Virol."},{"key":"10.1016\/j.jbc.2026.111350_bib69","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1009807","article-title":"Engineering well-expressed, V2-immunofocusing HIV-1 envelope glycoprotein membrane trimers for use in heterologous prime-boost vaccine regimens","volume":"17","author":"Crooks","year":"2021","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2026.111350_bib70","doi-asserted-by":"crossref","first-page":"4862","DOI":"10.1021\/acs.jproteome.1c00587","article-title":"Variability in the glycosylation patterns of gp120 proteins from different human immunodeficiency virus type 1 isolates expressed in different host cells","volume":"20","author":"Zhao","year":"2021","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.jbc.2026.111350_bib71","doi-asserted-by":"crossref","DOI":"10.1016\/j.isci.2023.107403","article-title":"Soluble prefusion-closed HIV-envelope trimers with glycan-covered bases","volume":"26","author":"Olia","year":"2023","journal-title":"iScience"},{"key":"10.1016\/j.jbc.2026.111350_bib72","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1011601","article-title":"Glycan heterogeneity as a cause of the persistent fraction in HIV-1 neutralization","volume":"19","author":"Ringe","year":"2023","journal-title":"PLOS Pathog."},{"key":"10.1016\/j.jbc.2026.111350_bib73","article-title":"Sequential analysis of the N\/O-Glycosylation of heavily glycosylated HIV-1 gp120 using EThcD-sceHCD-MS\/MS","volume":"12","author":"Zhang","year":"2021","journal-title":"Front. 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Dis."},{"key":"10.1016\/j.jbc.2026.111350_bib76","doi-asserted-by":"crossref","DOI":"10.1016\/j.ebiom.2020.102682","article-title":"Understanding the mechanisms driving the spread of subtype C HIV-1","volume":"53","author":"Gartner","year":"2020","journal-title":"EBioMedicine"},{"key":"10.1016\/j.jbc.2026.111350_bib77","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.01968-19","article-title":"Glycan profiles of gp120 protein vaccines from four major HIV-1 subtypes produced from different host cell lines under Non-GMP or GMP conditions","volume":"94","author":"Wang","year":"2020","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111350_bib78","doi-asserted-by":"crossref","first-page":"556","DOI":"10.1021\/pr034112b","article-title":"A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation","volume":"3","author":"H\u00e4gglund","year":"2004","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.jbc.2026.111350_bib79","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1006093","article-title":"Exploiting glycan topography for computational design of Env glycoprotein antigenicity","volume":"14","author":"Yu","year":"2018","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.jbc.2026.111350_bib80","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.00797-21","article-title":"Limited evidence for a relationship between HIV-1 glycan shield features in early infection and the development of neutralization breadth","volume":"95","author":"Li","year":"2021","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111350_bib81","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.01552-21","article-title":"The glycan hole area of HIV-1 envelope trimers contributes prominently to the induction of autologous neutralization","volume":"96","author":"Schorcht","year":"2022","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111350_bib82","article-title":"Transmitted\/Founder (T\/F) HIV-1 derived from sexual contact exhibits greater transmission fitness in human cervical tissue than T\/F HIV-1 from blood-to-blood contact: unique glycan profiles on T\/F envelopes associated with transmission phenotypes","volume":"21","author":"Zhang","year":"2025","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2026.111350_bib83","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1038\/s41577-022-00753-w","article-title":"Strategies for HIV-1 vaccines that induce broadly neutralizing antibodies","volume":"23","author":"Haynes","year":"2023","journal-title":"Nat. Rev. Immunol."},{"key":"10.1016\/j.jbc.2026.111350_bib84","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1126\/science.1225416","article-title":"Broadly neutralizing antibodies present new prospects to counter highly antigenically diverse viruses","volume":"337","author":"Burton","year":"2012","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.111350_bib85","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1126\/science.aaf1279","article-title":"Enhanced clearance of HIV-1-infected cells by broadly neutralizing antibodies against HIV-1 in vivo","volume":"352","author":"Lu","year":"2016","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.111350_bib86","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms10844","article-title":"Elimination of HIV-1-infected cells by broadly neutralizing antibodies","volume":"7","author":"Bruel","year":"2016","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.111350_bib87","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1038\/nature06106","article-title":"Fc receptor but not complement binding is important in antibody protection against HIV","volume":"449","author":"Hessell","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.111350_bib88","doi-asserted-by":"crossref","first-page":"13","DOI":"10.3390\/vaccines8010013","article-title":"Exploiting B cell receptor analyses to inform on HIV-1 vaccination strategies","volume":"8","author":"Kreer","year":"2020","journal-title":"Vaccines (Basel)"},{"key":"10.1016\/j.jbc.2026.111350_bib89","doi-asserted-by":"crossref","first-page":"5844","DOI":"10.1128\/JVI.07139-11","article-title":"Selection pressure on HIV-1 envelope by broadly neutralizing antibodies to the conserved CD4-Binding site","volume":"86","author":"Wu","year":"2012","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111350_bib90","doi-asserted-by":"crossref","first-page":"E3268","DOI":"10.1073\/pnas.1217207109","article-title":"Complex-type -glycan recognition by potent broadly neutralizing HIV antibodies","volume":"109","author":"Mouquet","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1016\/j.jbc.2026.111350_bib91","doi-asserted-by":"crossref","first-page":"804","DOI":"10.1038\/nsmb.2600","article-title":"Structural basis for diverse N-glycan recognition by HIV-1-neutralizing V1-V2-directed antibody PG16","volume":"20","author":"Pancera","year":"2013","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.111350_bib92","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1016\/j.immuni.2014.04.008","article-title":"Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers","volume":"40","author":"Blattner","year":"2014","journal-title":"Immunity"},{"key":"10.1016\/j.jbc.2026.111350_bib93","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1038\/nature11544","article-title":"Broad and potent neutralization of HIV-1 by a gp41-specific human antibody","volume":"491","author":"Huang","year":"2012","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.111350_bib94","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1186\/s12977-018-0453-y","article-title":"The expanding array of HIV broadly neutralizing antibodies","volume":"15","author":"McCoy","year":"2018","journal-title":"Retrovirology"},{"key":"10.1016\/j.jbc.2026.111350_bib95","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1009407","article-title":"A cross-neutralizing antibody between HIV-1 and influenza virus","volume":"17","author":"Lee","year":"2021","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2026.111350_bib96","doi-asserted-by":"crossref","DOI":"10.1126\/science.aax4380","article-title":"A generalized HIV vaccine design strategy for priming of broadly neutralizing antibody responses","volume":"366","author":"Steichen","year":"2019","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.111350_bib97","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1038\/nature01470","article-title":"Antibody neutralization and escape by HIV-1","volume":"422","author":"Wei","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.111350_bib98","doi-asserted-by":"crossref","first-page":"7479","DOI":"10.1038\/ncomms8479","article-title":"Glycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodies","volume":"6","author":"Pritchard","year":"2015","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.111350_bib99","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1038\/nature10373","article-title":"Broad neutralization coverage of HIV by multiple highly potent antibodies","volume":"477","author":"Walker","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.111350_bib100","doi-asserted-by":"crossref","first-page":"4351","DOI":"10.1073\/pnas.1217537110","article-title":"Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9","volume":"110","author":"Julien","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.jbc.2026.111350_bib101","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1084\/jem.20161765","article-title":"Progress toward active or passive HIV-1 vaccination","volume":"214","author":"Escolano","year":"2017","journal-title":"J. Exp. 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HIV-1 neutralizing antibodies induced by native-like envelope trimers","volume":"349","author":"Sanders","year":"2015","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.111350_bib108","doi-asserted-by":"crossref","first-page":"2919","DOI":"10.1016\/j.cell.2024.04.033","article-title":"Vaccine induction of heterologous HIV-1-neutralizing antibody B cell lineages in humans","volume":"187","author":"Williams","year":"2024","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2026.111350_bib109","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1093\/molbev\/msw015","article-title":"The diversity and molecular evolution of B-Cell receptors during infection","volume":"33","author":"Hoehn","year":"2016","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.jbc.2026.111350_bib110","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1016\/j.cell.2019.03.016","article-title":"B cell responses: cell interaction dynamics and decisions","volume":"177","author":"Cyster","year":"2019","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2026.111350_bib111","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1038\/s41420-024-01889-5","article-title":"B cell memory: from generation to reactivation: a multipronged defense wall against pathogens","volume":"10","author":"Syeda","year":"2024","journal-title":"Cell Death Discov."},{"key":"10.1016\/j.jbc.2026.111350_bib112","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1097\/COH.0000000000000153","article-title":"HIV broadly neutralizing antibody targets","volume":"10","author":"Wibmer","year":"2015","journal-title":"Curr. Opin. HIV AIDS"},{"key":"10.1016\/j.jbc.2026.111350_bib113","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1111\/imr.12502","article-title":"B-cell responses to HIV infection","volume":"275","author":"Moir","year":"2017","journal-title":"Immunol. Rev."},{"key":"10.1016\/j.jbc.2026.111350_bib114","doi-asserted-by":"crossref","DOI":"10.2174\/011570162X358302250206074255","article-title":"The germline targeting vaccine concept: overview and updates from HIV pre-clinical and clinical trials","author":"Stamatatos","year":"2025","journal-title":"Curr. HIV Res."},{"key":"10.1016\/j.jbc.2026.111350_bib115","doi-asserted-by":"crossref","first-page":"250","DOI":"10.3389\/fimmu.2014.00250","article-title":"Immunologic basis for long HCDR3s in broadly neutralizing antibodies against HIV-1","volume":"5","author":"Yu","year":"2014","journal-title":"Front. 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Commun."},{"key":"10.1016\/j.jbc.2026.111350_bib121","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1084\/jem.20122824","article-title":"Engineering HIV envelope protein to activate germline B cell receptors of broadly neutralizing anti-CD4 binding site antibodies","volume":"210","author":"McGuire","year":"2013","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.jbc.2026.111350_bib122","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2025.115848","article-title":"Transient glycan shield reduction induces CD4-binding site broadly neutralizing antibodies in SHIV-infected macaques","volume":"44","author":"Morris","year":"2025","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2026.111350_bib123","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1146\/annurev-immunol-120419-022408","article-title":"Germinal centers","volume":"40","author":"Victora","year":"2022","journal-title":"Annu. Rev. Immunol."},{"key":"10.1016\/j.jbc.2026.111350_bib124","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1007431","article-title":"HIV-1 envelope glycan modifications that permit neutralization by germline-reverted VRC01-class broadly neutralizing antibodies","volume":"14","author":"LaBranche","year":"2018","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.jbc.2026.111350_bib125","doi-asserted-by":"crossref","DOI":"10.1126\/science.adj8321","article-title":"Vaccine priming of rare HIV broadly neutralizing antibody precursors in nonhuman primates","volume":"384","author":"Steichen","year":"2024","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.111350_bib126","article-title":"Impact of glycan depletion, glycan debranching and increased glycan charge on HIV-1 neutralization sensitivity and immunogenicity","volume":"34","author":"D'Addabbo","year":"2024","journal-title":"Glycobiology"},{"key":"10.1016\/j.jbc.2026.111350_bib127","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1016\/j.immuni.2016.09.001","article-title":"Germinal center B cell dynamics","volume":"45","author":"Mesin","year":"2016","journal-title":"Immunity"},{"key":"10.1016\/j.jbc.2026.111350_bib128","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1111\/imr.12512","article-title":"Tfh cells and HIV bnAbs, an immunodominance model of the HIV neutralizing antibody generation problem","volume":"275","author":"Havenar-Daughton","year":"2017","journal-title":"Immunol. Rev."},{"key":"10.1016\/j.jbc.2026.111350_bib129","doi-asserted-by":"crossref","DOI":"10.1084\/jem.20201254","article-title":"Modulating the quantity of HIV Env-specific CD4 T cell help promotes rare B cell responses in germinal centers","volume":"218","author":"Lee","year":"2021","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.jbc.2026.111350_bib130","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/j.it.2018.04.008","article-title":"Understanding and manipulating viral immunity: antibody immunodominance enters center stage","volume":"39","author":"Angeletti","year":"2018","journal-title":"Trends Immunol."},{"key":"10.1016\/j.jbc.2026.111350_bib131","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1016\/j.cell.2019.04.012","article-title":"Slow delivery immunization enhances HIV neutralizing antibody and germinal center responses via modulation of immunodominance","volume":"177","author":"Cirelli","year":"2019","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2026.111350_bib132","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1016\/j.immuni.2017.05.007","article-title":"Elicitation of robust tier 2 neutralizing antibody responses in nonhuman Primates by HIV envelope trimer immunization using optimized approaches","volume":"46","author":"Pauthner","year":"2017","journal-title":"Immunity"},{"key":"10.1016\/j.jbc.2026.111350_bib133","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1016\/j.immuni.2013.08.031","article-title":"Human circulating PD-1+CXCR3-CXCR5+ memory Tfh cells are highly functional and correlate with broadly neutralizing HIV antibody responses","volume":"39","author":"Locci","year":"2013","journal-title":"Immunity"},{"key":"10.1016\/j.jbc.2026.111350_bib134","doi-asserted-by":"crossref","DOI":"10.1126\/sciimmunol.aag0851","article-title":"Immune perturbations in HIV-1-infected individuals who make broadly neutralizing antibodies","volume":"1","author":"Moody","year":"2016","journal-title":"Sci. Immunol."},{"key":"10.1016\/j.jbc.2026.111350_bib135","doi-asserted-by":"crossref","first-page":"4587","DOI":"10.1073\/pnas.071063898","article-title":"Localization of CD4+ T cell epitope hotspots to exposed strands of HIV envelope glycoprotein suggests structural influences on antigen processing","volume":"98","author":"Surman","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.jbc.2026.111350_bib136","doi-asserted-by":"crossref","first-page":"4001","DOI":"10.4049\/jimmunol.168.8.4001","article-title":"Detailed analysis of CD4+ Th responses to envelope and Gag proteins of simian immunodeficiency virus reveals an exclusion of broadly reactive Th epitopes from the glycosylated regions of envelope","volume":"168","author":"Sarkar","year":"2002","journal-title":"J. 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