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Article: Structural definition of a conserved neutralization epitope on HIV-1 gp120

TitleStructural definition of a conserved neutralization epitope on HIV-1 gp120
Authors
Issue Date2007
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/nature
Citation
Nature, 2007, v. 445 n. 7129, p. 732-737 How to Cite?
AbstractThe remarkable diversity, glycosylation and conformational flexibility of the human immunodeficiency virus type 1 (HIV-1) envelope (Env), including substantial rearrangement of the gp120 glycoprotein upon binding the CD4 receptor, allow it to evade antibody-mediated neutralization. Despite this complexity, the HIV-1 Env must retain conserved determinants that mediate CD4 binding. To evaluate how these determinants might provide opportunities for antibody recognition, we created variants of gp120 stabilized in the CD4-bound state, assessed binding of CD4 and of receptor-binding-site antibodies, and determined the structure at 2.3 Å resolution of the broadly neutralizing antibody b12 in complex with gp120. b12 binds to a conformationally invariant surface that overlaps a distinct subset of the CD4-binding site. This surface is involved in the metastable attachment of CD4, before the gp120 rearrangement required for stable engagement. A site of vulnerability, related to a functional requirement for efficient association with CD4, can therefore be targeted by antibody to neutralize HIV-1. ©2007 Nature Publishing Group.
Persistent Identifierhttp://hdl.handle.net/10722/157474
ISSN
2015 Impact Factor: 38.138
2015 SCImago Journal Rankings: 21.936
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhou, Ten_US
dc.contributor.authorXu, Len_US
dc.contributor.authorDey, Ben_US
dc.contributor.authorHessell, AJen_US
dc.contributor.authorVan Ryk, Den_US
dc.contributor.authorXiang, SHen_US
dc.contributor.authorYang, Xen_US
dc.contributor.authorZhang, MYen_US
dc.contributor.authorZwick, MBen_US
dc.contributor.authorArthos, Jen_US
dc.contributor.authorBurton, DRen_US
dc.contributor.authorDimitrov, DSen_US
dc.contributor.authorSodroski, Jen_US
dc.contributor.authorWyatt, Ren_US
dc.contributor.authorNabel, GJen_US
dc.contributor.authorKwong, PDen_US
dc.date.accessioned2012-08-08T08:50:17Z-
dc.date.available2012-08-08T08:50:17Z-
dc.date.issued2007en_US
dc.identifier.citationNature, 2007, v. 445 n. 7129, p. 732-737en_US
dc.identifier.issn0028-0836en_US
dc.identifier.urihttp://hdl.handle.net/10722/157474-
dc.description.abstractThe remarkable diversity, glycosylation and conformational flexibility of the human immunodeficiency virus type 1 (HIV-1) envelope (Env), including substantial rearrangement of the gp120 glycoprotein upon binding the CD4 receptor, allow it to evade antibody-mediated neutralization. Despite this complexity, the HIV-1 Env must retain conserved determinants that mediate CD4 binding. To evaluate how these determinants might provide opportunities for antibody recognition, we created variants of gp120 stabilized in the CD4-bound state, assessed binding of CD4 and of receptor-binding-site antibodies, and determined the structure at 2.3 Å resolution of the broadly neutralizing antibody b12 in complex with gp120. b12 binds to a conformationally invariant surface that overlaps a distinct subset of the CD4-binding site. This surface is involved in the metastable attachment of CD4, before the gp120 rearrangement required for stable engagement. A site of vulnerability, related to a functional requirement for efficient association with CD4, can therefore be targeted by antibody to neutralize HIV-1. ©2007 Nature Publishing Group.en_US
dc.languageengen_US
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/natureen_US
dc.relation.ispartofNatureen_US
dc.subject.meshAntigens, Cd4 - Chemistry - Metabolismen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshConserved Sequenceen_US
dc.subject.meshEpitopes - Chemistry - Immunologyen_US
dc.subject.meshHiv Antibodies - Immunology - Pharmacologyen_US
dc.subject.meshHiv Envelope Protein Gp120 - Chemistry - Immunology - Metabolismen_US
dc.subject.meshHiv-1 - Chemistry - Drug Effects - Immunology - Physiologyen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshMolecular Weighten_US
dc.subject.meshNeutralization Testsen_US
dc.subject.meshProtein Conformationen_US
dc.titleStructural definition of a conserved neutralization epitope on HIV-1 gp120en_US
dc.typeArticleen_US
dc.identifier.emailZhang, MY:zhangmy@hku.hken_US
dc.identifier.authorityZhang, MY=rp01409en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1038/nature05580en_US
dc.identifier.pmid17301785-
dc.identifier.scopuseid_2-s2.0-33847101745en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33847101745&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume445en_US
dc.identifier.issue7129en_US
dc.identifier.spage732en_US
dc.identifier.epage737en_US
dc.identifier.isiWOS:000244205200037-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.f10001066083-
dc.identifier.scopusauthoridZhou, T=7402989717en_US
dc.identifier.scopusauthoridXu, L=7404744597en_US
dc.identifier.scopusauthoridDey, B=15922105600en_US
dc.identifier.scopusauthoridHessell, AJ=6506631419en_US
dc.identifier.scopusauthoridVan Ryk, D=6603677582en_US
dc.identifier.scopusauthoridXiang, SH=7101805952en_US
dc.identifier.scopusauthoridYang, X=7408598686en_US
dc.identifier.scopusauthoridZhang, MY=35316639300en_US
dc.identifier.scopusauthoridZwick, MB=8105899100en_US
dc.identifier.scopusauthoridArthos, J=6603796858en_US
dc.identifier.scopusauthoridBurton, DR=7401577043en_US
dc.identifier.scopusauthoridDimitrov, DS=7202564539en_US
dc.identifier.scopusauthoridSodroski, J=7102286559en_US
dc.identifier.scopusauthoridWyatt, R=7402848241en_US
dc.identifier.scopusauthoridNabel, GJ=7103259116en_US
dc.identifier.scopusauthoridKwong, PD=7006992407en_US
dc.identifier.citeulike1107226-

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