{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T06:25:44Z","timestamp":1791354344072,"version":"4.3.1"},"reference-count":115,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2015,4,1]],"date-time":"2015-04-01T00:00:00Z","timestamp":1427846400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Current Opinion in Virology"],"published-print":{"date-parts":[[2015,4]]},"DOI":"10.1016\/j.coviro.2015.04.002","type":"journal-article","created":{"date-parts":[[2015,4,24]],"date-time":"2015-04-24T09:16:02Z","timestamp":1429866962000},"page":"137-147","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":119,"special_numbering":"C","title":["Strategies to guide the antibody affinity maturation process"],"prefix":"10.1016","volume":"11","author":[{"given":"Nicole A","family":"Doria-Rose","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M Gordon","family":"Joyce","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.coviro.2015.04.002_bib0580","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1146\/annurev.iy.12.040194.001001","article-title":"Germinal centers","volume":"12","author":"MacLennan","year":"1994","journal-title":"Annu Rev Immunol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0585","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1111\/j.1600-065X.2012.01118.x","article-title":"Affinity-based selection and the germinal center response","volume":"247","author":"Chan","year":"2012","journal-title":"Immunol Rev"},{"key":"10.1016\/j.coviro.2015.04.002_bib0590","doi-asserted-by":"crossref","first-page":"2645","DOI":"10.1128\/JVI.03228-13","article-title":"Diverse recombinant HIV-1 Envs fail to activate B cells expressing the germline B cell receptors of the broadly neutralizing anti-HIV-1 antibodies PG9 and 447-52D","volume":"88","author":"McGuire","year":"2014","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0595","doi-asserted-by":"crossref","first-page":"1380","DOI":"10.1126\/science.1259206","article-title":"HIV antibodies, antigen modification regulates competition of broad and narrow neutralizing HIV antibodies","volume":"346","author":"McGuire","year":"2014","journal-title":"Science"},{"key":"10.1016\/j.coviro.2015.04.002_bib0600","doi-asserted-by":"crossref","first-page":"9998","DOI":"10.1128\/JVI.05045-11","article-title":"Analysis of a clonal lineage of HIV-1 envelope V2\/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors","volume":"85","author":"Bonsignori","year":"2011","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_sbref0605","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1038\/nature13036","article-title":"Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies","volume":"509","author":"Doria-Rose","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.coviro.2015.04.002_sbref0610","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1038\/nature12053","article-title":"Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus","volume":"496","author":"Liao","year":"2013","journal-title":"Nature"},{"key":"10.1016\/j.coviro.2015.04.002_bib0615","doi-asserted-by":"crossref","first-page":"1633","DOI":"10.1126\/science.1207227","article-title":"Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding","volume":"333","author":"Scheid","year":"2011","journal-title":"Science"},{"key":"10.1016\/j.coviro.2015.04.002_bib0620","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.coviro.2015.04.002_bib0625","doi-asserted-by":"crossref","first-page":"E3268","DOI":"10.1073\/pnas.1217207109","article-title":"Complex-type N-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.coviro.2015.04.002_bib0630","doi-asserted-by":"crossref","first-page":"17624","DOI":"10.1073\/pnas.1415789111","article-title":"Recombinant HIV envelope trimer selects for quaternary-dependent antibodies targeting the trimer apex","volume":"111","author":"Sok","year":"2014","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.coviro.2015.04.002_bib0635","doi-asserted-by":"crossref","first-page":"2361","DOI":"10.1084\/jem.20141050","article-title":"Enhanced HIV-1 immunotherapy by commonly arising antibodies that target virus escape variants","volume":"211","author":"Klein","year":"2014","journal-title":"J Exp Med"},{"key":"10.1016\/j.coviro.2015.04.002_bib0640","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1126\/science.1187659","article-title":"Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1","volume":"329","author":"Wu","year":"2010","journal-title":"Science"},{"key":"10.1016\/j.coviro.2015.04.002_bib0645","doi-asserted-by":"crossref","first-page":"4688","DOI":"10.1128\/JVI.07163-11","article-title":"Two distinct broadly neutralizing antibody specificities of different clonal lineages in a single HIV-1-infected donor: implications for vaccine design","volume":"86","author":"Bonsignori","year":"2012","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0650","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1038\/nature07930","article-title":"Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals","volume":"458","author":"Scheid","year":"2009","journal-title":"Nature"},{"key":"10.1016\/j.coviro.2015.04.002_bib0655","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1126\/science.1178746","article-title":"Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target","volume":"326","author":"Walker","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.coviro.2015.04.002_bib0660","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1038\/nature06890","article-title":"Rapid cloning of high-affinity human monoclonal antibodies against influenza virus","volume":"453","author":"Wrammert","year":"2008","journal-title":"Nature"},{"key":"10.1016\/j.coviro.2015.04.002_sbref0665","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1038\/nature13764","article-title":"Rapid development of broadly influenza neutralizing antibodies through redundant mutations","volume":"516","author":"Pappas","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.coviro.2015.04.002_bib0670","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1126\/science.1192819","article-title":"Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01","volume":"329","author":"Zhou","year":"2010","journal-title":"Science"},{"key":"10.1016\/j.coviro.2015.04.002_bib0675","doi-asserted-by":"crossref","first-page":"1100","DOI":"10.4049\/jimmunol.1302515","article-title":"Antibodies VRC01 and 10E8 neutralize HIV-1 with high breadth and potency even with Ig-framework regions substantially reverted to germline","volume":"192","author":"Georgiev","year":"2014","journal-title":"J Immunol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0680","doi-asserted-by":"crossref","first-page":"E2083","DOI":"10.1073\/pnas.1208984109","article-title":"Structural basis for germline usage of a potent class of HIV-1 antibodies targeting the CD4 binding site","volume":"109","author":"West","year":"2012","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.coviro.2015.04.002_bib0685","doi-asserted-by":"crossref","first-page":"1593","DOI":"10.1126\/science.1207532","article-title":"Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing","volume":"333","author":"Wu","year":"2011","journal-title":"Science"},{"key":"10.1016\/j.coviro.2015.04.002_bib0690","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1038\/nature11371","article-title":"Structural and genetic basis for development of broadly neutralizing influenza antibodies","volume":"489","author":"Lingwood","year":"2012","journal-title":"Nature"},{"key":"10.1016\/j.coviro.2015.04.002_bib0695","doi-asserted-by":"crossref","first-page":"4047","DOI":"10.1128\/JVI.03422-13","article-title":"Flow cytometry reveals that H5N1 vaccination elicits cross-reactive stem-directed antibodies from multiple Ig heavy-chain lineages","volume":"88","author":"Whittle","year":"2014","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0700","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1038\/nature10696","article-title":"Structure of HIV-1 gp120 V1\/V2 domain with broadly neutralizing antibody PG9","volume":"480","author":"McLellan","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.coviro.2015.04.002_sbref0705","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1038\/nature13808","article-title":"Structure and immune recognition of trimeric pre-fusion HIV-1 Env","volume":"514","author":"Pancera","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.coviro.2015.04.002_bib0710","doi-asserted-by":"crossref","first-page":"1097","DOI":"10.1126\/science.1213256","article-title":"A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield","volume":"334","author":"Pejchal","year":"2011","journal-title":"Science"},{"key":"10.1016\/j.coviro.2015.04.002_bib0715","doi-asserted-by":"crossref","first-page":"14216","DOI":"10.1073\/pnas.1111497108","article-title":"Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin","volume":"108","author":"Whittle","year":"2011","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.coviro.2015.04.002_bib0720","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1038\/nature11414","article-title":"Cross-neutralization of influenza A viruses mediated by a single antibody loop","volume":"489","author":"Ekiert","year":"2012","journal-title":"Nature"},{"key":"10.1016\/j.coviro.2015.04.002_bib0725","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1038\/nsmb.2500","article-title":"A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin","volume":"20","author":"Xu","year":"2013","journal-title":"Nat Struct Mol Biol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0730","doi-asserted-by":"crossref","first-page":"17040","DOI":"10.1073\/pnas.1212371109","article-title":"Heterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidity","volume":"109","author":"Lee","year":"2012","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.coviro.2015.04.002_bib0735","doi-asserted-by":"crossref","first-page":"2426","DOI":"10.1128\/JVI.02837-13","article-title":"Structural basis for HIV-1 neutralization by 2F5-like antibodies m66 and m66.6","volume":"88","author":"Ofek","year":"2014","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0740","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.coviro.2015.04.002_bib0745","doi-asserted-by":"crossref","first-page":"10724","DOI":"10.1128\/JVI.78.19.10724-10737.2004","article-title":"Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope","volume":"78","author":"Ofek","year":"2004","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0750","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.immuni.2004.12.011","article-title":"Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41","volume":"22","author":"Cardoso","year":"2005","journal-title":"Immunity"},{"key":"10.1016\/j.coviro.2015.04.002_bib0755","doi-asserted-by":"crossref","first-page":"pe23532","DOI":"10.1371\/journal.pone.0023532","article-title":"Isolation of a human anti-HIV gp41 membrane proximal region neutralizing antibody by antigen-specific single B cell sorting","volume":"6","author":"Morris","year":"2011","journal-title":"PLoS ONE"},{"key":"10.1016\/j.coviro.2015.04.002_bib0760","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.immuni.2013.04.012","article-title":"Multidonor analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies","volume":"39","author":"Zhou","year":"2013","journal-title":"Immunity"},{"key":"10.1016\/j.coviro.2015.04.002_bib0765","doi-asserted-by":"crossref","first-page":"1105","DOI":"10.1128\/JVI.02905-14","article-title":"Two classes of broadly neutralizing antibodies within a single lineage directed to the high-mannose patch of HIV envelope","volume":"89","author":"Doores","year":"2015","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0770","doi-asserted-by":"crossref","first-page":"10275","DOI":"10.1073\/pnas.1409954111","article-title":"Affinity maturation in an HIV broadly neutralizing B-cell lineage through reorientation of variable domains","volume":"111","author":"Fera","year":"2014","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.coviro.2015.04.002_sbref0775","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/j.cell.2014.06.022","article-title":"Cooperation of B cell lineages in induction of HIV-1-broadly neutralizing antibodies","volume":"158","author":"Gao","year":"2014","journal-title":"Cell"},{"key":"10.1016\/j.coviro.2015.04.002_sbref0780","doi-asserted-by":"crossref","first-page":"1688","DOI":"10.1038\/nm.2985","article-title":"Evolution of an HIV glycan-dependent broadly neutralizing antibody epitope through immune escape","volume":"18","author":"Moore","year":"2012","journal-title":"Nat Med"},{"key":"10.1016\/j.coviro.2015.04.002_bib0785","doi-asserted-by":"crossref","first-page":"pe1003173","DOI":"10.1371\/journal.ppat.1003173","article-title":"Viral escape from neutralizing antibodies in early subtype A HIV-1 infection drives an increase in autologous neutralization breadth","volume":"9","author":"Murphy","year":"2013","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.coviro.2015.04.002_bib0790","doi-asserted-by":"crossref","first-page":"pe1003738","DOI":"10.1371\/journal.ppat.1003738","article-title":"Viral escape from HIV-1 neutralizing antibodies drives increased plasma neutralization breadth through sequential recognition of multiple epitopes and immunotypes","volume":"9","author":"Wibmer","year":"2013","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.coviro.2015.04.002_bib0795","doi-asserted-by":"crossref","first-page":"6144","DOI":"10.1038\/ncomms7144","article-title":"Antibody potency relates to the ability to recognize the closed, pre-fusion form of HIV Env","volume":"6","author":"Guttman","year":"2015","journal-title":"Nat Commun"},{"key":"10.1016\/j.coviro.2015.04.002_bib0800","doi-asserted-by":"crossref","first-page":"2294","DOI":"10.1128\/JVI.02717-12","article-title":"Outer domain of HIV-1 gp120: antigenic optimization, structural malleability, and crystal structure with antibody VRC-PG04","volume":"87","author":"Joyce","year":"2013","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0805","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1126\/science.1243283","article-title":"Structure-based design of a fusion glycoprotein vaccine for respiratory syncytial virus","volume":"342","author":"McLellan","year":"2013","journal-title":"Science"},{"key":"10.1016\/j.coviro.2015.04.002_bib0810","doi-asserted-by":"crossref","first-page":"3574","DOI":"10.1128\/JVI.06938-11","article-title":"HIV-1 virus-like particles bearing pure env trimers expose neutralizing epitopes but occlude nonneutralizing epitopes","volume":"86","author":"Tong","year":"2012","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0815","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1111\/imr.12075","article-title":"HIV-1 neutralizing antibodies: understanding nature's pathways","volume":"254","author":"Mascola","year":"2013","journal-title":"Immunol Rev"},{"key":"10.1016\/j.coviro.2015.04.002_bib0820","doi-asserted-by":"crossref","first-page":"6189","DOI":"10.1016\/j.vaccine.2008.09.080","article-title":"Deceptive imprinting and immune refocusing in vaccine design","volume":"26","author":"Tobin","year":"2008","journal-title":"Vaccine"},{"key":"10.1016\/j.coviro.2015.04.002_bib0825","doi-asserted-by":"crossref","first-page":"2310","DOI":"10.1128\/JVI.77.4.2310-2320.2003","article-title":"Changes in the immunogenic properties of soluble gp140 human immunodeficiency virus envelope constructs upon partial deletion of the second hypervariable region","volume":"77","author":"Srivastava","year":"2003","journal-title":"J Virol"},{"issue":"Pt 11","key":"10.1016\/j.coviro.2015.04.002_bib0830","doi-asserted-by":"crossref","first-page":"2723","DOI":"10.1099\/0022-1317-83-11-2723","article-title":"Truncated gp120 envelope glycoprotein of human immunodeficiency virus 1 elicits a broadly reactive neutralizing immune response","volume":"83","author":"Jeffs","year":"2002","journal-title":"J Gen Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0835","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.virol.2007.04.033","article-title":"A comparative immunogenicity study of HIV-1 virus-like particles bearing various forms of envelope proteins, particles bearing no envelope and soluble monomeric gp120","volume":"366","author":"Crooks","year":"2007","journal-title":"Virology"},{"key":"10.1016\/j.coviro.2015.04.002_bib0840","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1146\/annurev-immunol-030409-101256","article-title":"The role of antibodies in HIV vaccines","volume":"28","author":"Mascola","year":"2010","journal-title":"Annu Rev Immunol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0845","doi-asserted-by":"crossref","first-page":"4634","DOI":"10.1128\/JVI.76.9.4634-4642.2002","article-title":"Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin","volume":"76","author":"Yang","year":"2002","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0850","doi-asserted-by":"crossref","first-page":"7436","DOI":"10.1074\/jbc.M114.620534","article-title":"Immunosilencing a highly immunogenic protein trimerization domain","volume":"290","author":"Sliepen","year":"2015","journal-title":"J Biol Chem"},{"key":"10.1016\/j.coviro.2015.04.002_bib0855","doi-asserted-by":"crossref","first-page":"17","DOI":"10.2174\/1570162052772933","article-title":"HIV-1 prophylactic vaccine trials in Thailand","volume":"3","author":"Pitisuttithum","year":"2005","journal-title":"Curr HIV Res"},{"key":"10.1016\/j.coviro.2015.04.002_bib0860","doi-asserted-by":"crossref","first-page":"3380","DOI":"10.1128\/JVI.03473-14","article-title":"A native-like SOSIP.664 trimer based on a HIV-1 subtype B env gene","volume":"89","author":"Pugach","year":"2015","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_sbref0865","doi-asserted-by":"crossref","first-page":"e1003618","DOI":"10.1371\/journal.ppat.1003618","article-title":"A next-generation cleaved, soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies","volume":"9","author":"Sanders","year":"2013","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.coviro.2015.04.002_bib0870","doi-asserted-by":"crossref","first-page":"18256","DOI":"10.1073\/pnas.1314351110","article-title":"Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation","volume":"110","author":"Ringe","year":"2013","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.coviro.2015.04.002_bib0875","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\u2013gp120 interface on intact HIV-1 Env trimers","volume":"40","author":"Blattner","year":"2014","journal-title":"Immunity"},{"key":"10.1016\/j.coviro.2015.04.002_bib0880","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1038\/nature13601","article-title":"Broad and potent HIV-1 neutralization by a human antibody that binds the gp41\u2013gp120 interface","volume":"515","author":"Huang","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.coviro.2015.04.002_sbref0885","doi-asserted-by":"crossref","first-page":"1484","DOI":"10.1126\/science.1245627","article-title":"Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer","volume":"342","author":"Lyumkis","year":"2013","journal-title":"Science"},{"key":"10.1016\/j.coviro.2015.04.002_sbref0890","doi-asserted-by":"crossref","first-page":"1477","DOI":"10.1126\/science.1245625","article-title":"Crystal structure of a soluble cleaved HIV-1 envelope trimer","volume":"342","author":"Julien","year":"2013","journal-title":"Science"},{"key":"10.1016\/j.coviro.2015.04.002_sbref0895","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1126\/science.1234150","article-title":"Rational HIV immunogen design to target specific germline B cell receptors","volume":"340","author":"Jardine","year":"2013","journal-title":"Science"},{"key":"10.1016\/j.coviro.2015.04.002_sbref0900","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.coviro.2015.04.002_bib0905","doi-asserted-by":"crossref","first-page":"16538","DOI":"10.1073\/pnas.1315295110","article-title":"HIV-1 suppression and durable control by combining single broadly neutralizing antibodies and antiretroviral drugs in humanized mice","volume":"110","author":"Horwitz","year":"2013","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.coviro.2015.04.002_sbref0910","doi-asserted-by":"crossref","first-page":"4201","DOI":"10.1128\/JVI.03608-14","article-title":"HIV-1 fitness cost associated with escape from the VRC01 class of CD4 binding site neutralizing antibodies","volume":"89","author":"Lynch","year":"2015","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0915","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.coviro.2015.04.002_bib0920","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1146\/annurev-med-120611-145115","article-title":"Toward a universal influenza virus vaccine: prospects and challenges","volume":"64","author":"Pica","year":"2013","journal-title":"Annu Rev Med"},{"issue":"2 Pt 1","key":"10.1016\/j.coviro.2015.04.002_bib0925","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/0092-8674(82)90135-0","article-title":"The antigenic structure of the influenza virus A\/PR\/8\/34 hemagglutinin (H1 subtype)","volume":"31","author":"Caton","year":"1982","journal-title":"Cell"},{"key":"10.1016\/j.coviro.2015.04.002_bib0930","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1146\/annurev.iy.08.040190.003513","article-title":"Structural basis of immune recognition of influenza virus hemagglutinin","volume":"8","author":"Wilson","year":"1990","journal-title":"Annu Rev Immunol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0935","doi-asserted-by":"crossref","first-page":"996","DOI":"10.1126\/science.1256427","article-title":"Antibody landscapes after influenza virus infection or vaccination","volume":"346","author":"Fonville","year":"2014","journal-title":"Science"},{"key":"10.1016\/j.coviro.2015.04.002_bib0940","doi-asserted-by":"crossref","first-page":"976","DOI":"10.1126\/science.1244730","article-title":"Substitutions near the receptor binding site determine major antigenic change during influenza virus evolution","volume":"342","author":"Koel","year":"2013","journal-title":"Science"},{"key":"10.1016\/j.coviro.2015.04.002_bib0945","doi-asserted-by":"crossref","first-page":"E2514","DOI":"10.1073\/pnas.1402766111","article-title":"Influenza hemagglutinin stem-fragment immunogen elicits broadly neutralizing antibodies and confers heterologous protection","volume":"111","author":"Mallajosyula","year":"2014","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.coviro.2015.04.002_bib0950","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1016\/j.coviro.2013.07.007","article-title":"Influenza virus hemagglutinin stalk-based antibodies and vaccines","volume":"3","author":"Krammer","year":"2013","journal-title":"Curr Opin Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0955","doi-asserted-by":"crossref","first-page":"6542","DOI":"10.1128\/JVI.00641-13","article-title":"Chimeric hemagglutinin influenza virus vaccine constructs elicit broadly protective stalk-specific antibodies","volume":"87","author":"Krammer","year":"2013","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0960","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1097\/COH.0000000000000057","article-title":"Development of broadly neutralizing antibodies from autologous neutralizing antibody responses in HIV infection","volume":"9","author":"Derdeyn","year":"2014","journal-title":"Curr Opin HIV AIDS"},{"key":"10.1016\/j.coviro.2015.04.002_bib0965","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1038\/nbt.2197","article-title":"B-cell-lineage immunogen design in vaccine development with HIV-1 as a case study","volume":"30","author":"Haynes","year":"2012","journal-title":"Nat Biotechnol"},{"key":"10.1016\/j.coviro.2015.04.002_sbref0970","doi-asserted-by":"crossref","first-page":"12949","DOI":"10.1128\/JVI.01812-14","article-title":"Envelope variants circulating as initial neutralization breadth developed in two HIV-infected subjects stimulate multiclade neutralizing antibodies in rabbits","volume":"88","author":"Malherbe","year":"2014","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0975","doi-asserted-by":"crossref","first-page":"5262","DOI":"10.1128\/JVI.02419-10","article-title":"Sequential immunization with a subtype B HIV-1 envelope quasispecies partially mimics the in vivo development of neutralizing antibodies","volume":"85","author":"Malherbe","year":"2011","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib0980","doi-asserted-by":"crossref","first-page":"5519","DOI":"10.1016\/j.vaccine.2012.06.042","article-title":"Motif-optimized subtype A HIV envelope-based DNA vaccines rapidly elicit neutralizing antibodies when delivered sequentially","volume":"30","author":"Pissani","year":"2012","journal-title":"Vaccine"},{"key":"10.1016\/j.coviro.2015.04.002_bib0985","doi-asserted-by":"crossref","first-page":"1663","DOI":"10.1172\/JCI41902","article-title":"Heterosubtypic neutralizing antibodies are produced by individuals immunized with a seasonal influenza vaccine","volume":"120","author":"Corti","year":"2010","journal-title":"J Clin Invest"},{"key":"10.1016\/j.coviro.2015.04.002_bib0990","doi-asserted-by":"crossref","first-page":"9047","DOI":"10.1073\/pnas.1118979109","article-title":"Pandemic H1N1 influenza vaccine induces a recall response in humans that favors broadly cross-reactive memory B cells","volume":"109","author":"Li","year":"2012","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.coviro.2015.04.002_bib0995","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1146\/annurev-med-052912-123749","article-title":"Lessons from the RV144 Thai Phase III HIV-1 vaccine trial and the search for correlates of protection","volume":"66","author":"Kim","year":"2015","journal-title":"Annu Rev Med"},{"key":"10.1016\/j.coviro.2015.04.002_bib1000","doi-asserted-by":"crossref","first-page":"pe87572","DOI":"10.1371\/journal.pone.0087572","article-title":"Vaccine-induced IgG antibodies to V1V2 regions of multiple HIV-1 subtypes correlate with decreased risk of HIV-1 infection","volume":"9","author":"Zolla-Pazner","year":"2014","journal-title":"PLoS ONE"},{"key":"10.1016\/j.coviro.2015.04.002_bib1005","doi-asserted-by":"crossref","first-page":"1275","DOI":"10.1056\/NEJMoa1113425","article-title":"Immune-correlates analysis of an HIV-1 vaccine efficacy trial","volume":"366","author":"Haynes","year":"2012","journal-title":"N Engl J Med"},{"key":"10.1016\/j.coviro.2015.04.002_bib1010","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1093\/infdis\/jiu444","article-title":"Infant HIV type 1 gp120 vaccination elicits robust and durable anti-V1V2 immunoglobulin G responses and only rare envelope-specific immunoglobulin A responses","volume":"211","author":"Fouda","year":"2015","journal-title":"J Infect Dis"},{"key":"10.1016\/j.coviro.2015.04.002_bib1015","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1016\/j.cell.2015.01.027","article-title":"Manipulating the selection forces during affinity maturation to generate cross-reactive HIV antibodies","author":"Wang","year":"2015","journal-title":"Cell"},{"key":"10.1016\/j.coviro.2015.04.002_bib1020","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1093\/infdis\/jiq093","article-title":"Safety and immunogenicity of influenza A H5 subunit vaccines: effect of vaccine schedule and antigenic variant","volume":"203","author":"Belshe","year":"2011","journal-title":"J Infect Dis"},{"key":"10.1016\/j.coviro.2015.04.002_bib1025","doi-asserted-by":"crossref","first-page":"1631","DOI":"10.1128\/JVI.01482-09","article-title":"Breadth of human immunodeficiency virus-specific neutralizing activity in sera: clustering analysis and association with clinical variables","volume":"84","author":"Doria-Rose","year":"2010","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib1030","doi-asserted-by":"crossref","first-page":"10269","DOI":"10.1128\/JVI.01149-09","article-title":"Breadth of neutralizing antibody response to human immunodeficiency virus type 1 is affected by factors early in infection but does not influence disease progression","volume":"83","author":"Piantadosi","year":"2009","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib1035","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1128\/JVI.02036-08","article-title":"Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection","volume":"83","author":"Sather","year":"2009","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib1040","doi-asserted-by":"crossref","first-page":"9579","DOI":"10.1128\/JVI.00975-14","article-title":"CD40L-adjuvanted DNA\/modified vaccinia virus Ankara simian immunodeficiency virus SIV239 vaccine enhances SIV-specific humoral and cellular immunity and improves protection against a heterologous SIVE660 mucosal challenge","volume":"88","author":"Kwa","year":"2014","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib1045","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/j.nano.2006.07.009","article-title":"Adaptations of nanoscale viruses and other protein cages for medical applications","volume":"2","author":"Lee","year":"2006","journal-title":"Nanomedicine"},{"key":"10.1016\/j.coviro.2015.04.002_bib1050","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1038\/nature12202","article-title":"Self-assembling influenza nanoparticle vaccines elicit broadly neutralizing H1N1 antibodies","volume":"499","author":"Kanekiyo","year":"2013","journal-title":"Nature"},{"key":"10.1016\/j.coviro.2015.04.002_bib1055","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ymeth.2006.05.016","article-title":"Pathogen recognition and development of particulate vaccines: does size matter?","volume":"40","author":"Xiang","year":"2006","journal-title":"Methods"},{"key":"10.1016\/j.coviro.2015.04.002_bib1060","doi-asserted-by":"crossref","first-page":"6098","DOI":"10.1016\/j.biomaterials.2014.04.010","article-title":"Targeting and activation of antigen-specific B-cells by calcium phosphate nanoparticles loaded with protein antigen","volume":"35","author":"Temchura","year":"2014","journal-title":"Biomaterials"},{"key":"10.1016\/j.coviro.2015.04.002_bib1065","doi-asserted-by":"crossref","first-page":"1448","DOI":"10.1126\/science.8248784","article-title":"The influence of antigen organization on B cell responsiveness","volume":"262","author":"Bachmann","year":"1993","journal-title":"Science"},{"key":"10.1016\/j.coviro.2015.04.002_bib1070","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.1021\/cb400060x","article-title":"Boosting immunity to small tumor-associated carbohydrates with bacteriophage qbeta capsids","volume":"8","author":"Yin","year":"2013","journal-title":"ACS Chem Biol"},{"key":"10.1016\/j.coviro.2015.04.002_bib1075","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.coi.2009.01.004","article-title":"Mechanism of action of clinically approved adjuvants","volume":"21","author":"Lambrecht","year":"2009","journal-title":"Curr Opin Immunol"},{"key":"10.1016\/j.coviro.2015.04.002_bib1080","doi-asserted-by":"crossref","first-page":"1597","DOI":"10.1038\/nm.3409","article-title":"Key roles of adjuvants in modern vaccines","volume":"19","author":"Reed","year":"2013","journal-title":"Nat Med"},{"key":"10.1016\/j.coviro.2015.04.002_bib1085","doi-asserted-by":"crossref","first-page":"3641","DOI":"10.4049\/jimmunol.1101107","article-title":"Complement activation and complement receptors on follicular dendritic cells are critical for the function of a targeted adjuvant","volume":"187","author":"Mattsson","year":"2011","journal-title":"J Immunol"},{"key":"10.1016\/j.coviro.2015.04.002_bib1090","doi-asserted-by":"crossref","first-page":"1399","DOI":"10.4049\/jimmunol.1002881","article-title":"A unique role of the cholera toxin A1-DD adjuvant for long-term plasma and memory B cell development","volume":"186","author":"Bemark","year":"2011","journal-title":"J Immunol"},{"key":"10.1016\/j.coviro.2015.04.002_bib1095","doi-asserted-by":"crossref","first-page":"2488","DOI":"10.1128\/JVI.06259-11","article-title":"Targeting HIV-1 envelope glycoprotein trimers to B cells by using APRIL improves antibody responses","volume":"86","author":"Melchers","year":"2012","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib1100","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1016\/j.cell.2010.10.032","article-title":"Germinal center dynamics revealed by multiphoton microscopy with a photoactivatable fluorescent reporter","volume":"143","author":"Victora","year":"2010","journal-title":"Cell"},{"key":"10.1016\/j.coviro.2015.04.002_bib1105","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1038\/nature13300","article-title":"Clonal selection in the germinal centre by regulated proliferation and hypermutation","volume":"509","author":"Gitlin","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.coviro.2015.04.002_bib1110","doi-asserted-by":"crossref","first-page":"13990","DOI":"10.1128\/JVI.02273-14","article-title":"Activation of the RIG-I pathway during influenza vaccination enhances the germinal center reaction, promotes T follicular helper cell induction, and provides a dose-sparing effect and protective immunity","volume":"88","author":"Kulkarni","year":"2014","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib1115","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1084\/jem.20101352","article-title":"Broadly cross-reactive antibodies dominate the human B cell response against 2009 pandemic H1N1 influenza virus infection","volume":"208","author":"Wrammert","year":"2011","journal-title":"J Exp Med"},{"key":"10.1016\/j.coviro.2015.04.002_bib1120","doi-asserted-by":"crossref","first-page":"6778","DOI":"10.1038\/srep06778","article-title":"Toward a more accurate view of human B-cell repertoire by next-generation sequencing, unbiased repertoire capture and single-molecule barcoding","volume":"4","author":"He","year":"2014","journal-title":"Sci Rep"},{"key":"10.1016\/j.coviro.2015.04.002_bib1125","doi-asserted-by":"crossref","first-page":"3637","DOI":"10.4049\/jimmunol.1303334","article-title":"Single-cell and deep sequencing of IgG-switched macaque B cells reveal a diverse Ig repertoire following immunization","volume":"192","author":"Sundling","year":"2014","journal-title":"J Immunol"},{"key":"10.1016\/j.coviro.2015.04.002_bib1130","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1093\/intimm\/2.9.813","article-title":"Somatic mutations in antibodies expressed by germinal centre B cells early after primary immunization","volume":"2","author":"Apel","year":"1990","journal-title":"Int Immunol"},{"key":"10.1016\/j.coviro.2015.04.002_bib1135","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1038\/354389a0","article-title":"Intraclonal generation of antibody mutants in germinal centres","volume":"354","author":"Jacob","year":"1991","journal-title":"Nature"},{"key":"10.1016\/j.coviro.2015.04.002_bib1140","doi-asserted-by":"crossref","first-page":"5155","DOI":"10.4049\/jimmunol.158.11.5155","article-title":"Somatic mutation leads to efficient affinity maturation when centrocytes recycle back to centroblasts","volume":"158","author":"Oprea","year":"1997","journal-title":"J Immunol"},{"key":"10.1016\/j.coviro.2015.04.002_bib1145","doi-asserted-by":"crossref","first-page":"7788","DOI":"10.1128\/JVI.00555-11","article-title":"Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopes","volume":"85","author":"McLellan","year":"2011","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.04.002_bib1150","doi-asserted-by":"crossref","first-page":"1838","DOI":"10.1126\/science.1093155","article-title":"The structure and receptor binding properties of the 1918 influenza hemagglutinin","volume":"303","author":"Gamblin","year":"2004","journal-title":"Science"}],"container-title":["Current Opinion in Virology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1879625715000516?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1879625715000516?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2023,8,9]],"date-time":"2023-08-09T19:20:45Z","timestamp":1691608845000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1879625715000516"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,4]]},"references-count":115,"alternative-id":["S1879625715000516"],"URL":"https:\/\/doi.org\/10.1016\/j.coviro.2015.04.002","relation":{},"ISSN":["1879-6257"],"issn-type":[{"value":"1879-6257","type":"print"}],"subject":[],"published":{"date-parts":[[2015,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Strategies to guide the antibody affinity maturation process","name":"articletitle","label":"Article Title"},{"value":"Current Opinion in Virology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.coviro.2015.04.002","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Published by Elsevier B.V.","name":"copyright","label":"Copyright"}]}}