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Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9.

dc.contributor.author McLellan, JS
dc.contributor.author Pancera, M
dc.contributor.author Carrico, C
dc.contributor.author Gorman, J
dc.contributor.author Julien, JP
dc.contributor.author Khayat, R
dc.contributor.author Louder, R
dc.contributor.author Pejchal, R
dc.contributor.author Sastry, M
dc.contributor.author Dai, K
dc.contributor.author O'Dell, S
dc.contributor.author Patel, N
dc.contributor.author Shahzad ul Hussan, S
dc.contributor.author Yang, Y
dc.contributor.author Zhang, B
dc.contributor.author Zhou, T
dc.contributor.author Zhu, J
dc.contributor.author Boyington, JC
dc.contributor.author Chuang, GY
dc.contributor.author Diwanji, D
dc.contributor.author Georgiev, I
dc.contributor.author Kwon, YD
dc.contributor.author Lee, D
dc.contributor.author Louder, MK
dc.contributor.author Moquin, S
dc.contributor.author Schmidt, SD
dc.contributor.author Yang, ZY
dc.contributor.author Bonsignori, M
dc.contributor.author Crump, JA
dc.contributor.author Kapiga, SH
dc.contributor.author Sam, NE
dc.contributor.author Haynes, BF
dc.contributor.author Burton, DR
dc.contributor.author Koff, WC
dc.contributor.author Walker, LM
dc.contributor.author Phogat, S
dc.contributor.author Wyatt, R
dc.contributor.author Orwenyo, J
dc.contributor.author Wang, LX
dc.contributor.author Arthos, J
dc.contributor.author Bewley, CA
dc.contributor.author Mascola, JR
dc.contributor.author Nabel, GJ
dc.contributor.author Schief, WR
dc.contributor.author Ward, AB
dc.contributor.author Wilson, IA
dc.contributor.author Kwong, PD
dc.coverage.spatial England
dc.date.accessioned 2017-03-02T19:25:40Z
dc.date.available 2017-03-02T19:25:40Z
dc.date.issued 2011-11-23
dc.identifier https://www.ncbi.nlm.nih.gov/pubmed/22113616
dc.identifier nature10696
dc.identifier.uri https://hdl.handle.net/10161/13795
dc.description.abstract Variable regions 1 and 2 (V1/V2) of human immunodeficiency virus-1 (HIV-1) gp120 envelope glycoprotein are critical for viral evasion of antibody neutralization, and are themselves protected by extraordinary sequence diversity and N-linked glycosylation. Human antibodies such as PG9 nonetheless engage V1/V2 and neutralize 80% of HIV-1 isolates. Here we report the structure of V1/V2 in complex with PG9. V1/V2 forms a four-stranded β-sheet domain, in which sequence diversity and glycosylation are largely segregated to strand-connecting loops. PG9 recognition involves electrostatic, sequence-independent and glycan interactions: the latter account for over half the interactive surface but are of sufficiently weak affinity to avoid autoreactivity. The structures of V1/V2-directed antibodies CH04 and PGT145 indicate that they share a common mode of glycan penetration by extended anionic loops. In addition to structurally defining V1/V2, the results thus identify a paradigm of antibody recognition for highly glycosylated antigens, which-with PG9-involves a site of vulnerability comprising just two glycans and a strand.
dc.language eng
dc.publisher Springer Science and Business Media LLC
dc.relation.ispartof Nature
dc.relation.isversionof 10.1038/nature10696
dc.subject AIDS Vaccines
dc.subject Amino Acid Motifs
dc.subject Amino Acid Sequence
dc.subject Antibodies, Neutralizing
dc.subject Antibody Affinity
dc.subject Antibody Specificity
dc.subject Antigen-Antibody Complex
dc.subject Binding Sites, Antibody
dc.subject Conserved Sequence
dc.subject Crystallography, X-Ray
dc.subject Epitopes
dc.subject Glycopeptides
dc.subject Glycosylation
dc.subject HIV Antibodies
dc.subject HIV Envelope Protein gp120
dc.subject HIV-1
dc.subject Hydrogen Bonding
dc.subject Immune Evasion
dc.subject Models, Molecular
dc.subject Molecular Sequence Data
dc.subject Polysaccharides
dc.subject Protein Structure, Quaternary
dc.subject Protein Structure, Tertiary
dc.title Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9.
dc.type Journal article
duke.contributor.id Bonsignori, M|0383217
duke.contributor.id Crump, JA|0231646
duke.contributor.id Haynes, BF|0114780
pubs.author-url https://www.ncbi.nlm.nih.gov/pubmed/22113616
pubs.begin-page 336
pubs.end-page 343
pubs.issue 7377
pubs.organisational-group Basic Science Departments
pubs.organisational-group Clinical Science Departments
pubs.organisational-group Duke
pubs.organisational-group Duke Cancer Institute
pubs.organisational-group Duke Human Vaccine Institute
pubs.organisational-group Global Health Institute
pubs.organisational-group Immunology
pubs.organisational-group Institutes and Centers
pubs.organisational-group Institutes and Provost's Academic Units
pubs.organisational-group Medicine
pubs.organisational-group Medicine, Duke Human Vaccine Institute
pubs.organisational-group Medicine, Infectious Diseases
pubs.organisational-group Pathology
pubs.organisational-group School of Medicine
pubs.organisational-group University Institutes and Centers
pubs.publication-status Published online
pubs.volume 480
dc.identifier.eissn 1476-4687
duke.contributor.orcid Bonsignori, M|0000-0003-2973-2101


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