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

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Date
2011-11-23
Authors
McLellan, JS
Pancera, M
Carrico, C
Gorman, J
Julien, JP
Khayat, R
Louder, R
Pejchal, R
Sastry, M
Dai, K
O'Dell, S
Patel, N
Shahzad ul Hussan, S
Yang, Y
Zhang, B
Zhou, T
Zhu, J
Boyington, JC
Chuang, GY
Diwanji, D
Georgiev, I
Kwon, YD
Lee, D
Louder, MK
Moquin, S
Schmidt, SD
Yang, ZY
Bonsignori, M
Crump, JA
Kapiga, SH
Sam, NE
Haynes, BF
Burton, DR
Koff, WC
Walker, LM
Phogat, S
Wyatt, R
Orwenyo, J
Wang, LX
Arthos, J
Bewley, CA
Mascola, JR
Nabel, GJ
Schief, WR
Ward, AB
Wilson, IA
Kwong, PD
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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.
Type
Journal article
Subject
AIDS Vaccines
Amino Acid Motifs
Amino Acid Sequence
Antibodies, Neutralizing
Antibody Affinity
Antibody Specificity
Antigen-Antibody Complex
Binding Sites, Antibody
Conserved Sequence
Crystallography, X-Ray
Epitopes
Glycopeptides
Glycosylation
HIV Antibodies
HIV Envelope Protein gp120
HIV-1
Hydrogen Bonding
Immune Evasion
Models, Molecular
Molecular Sequence Data
Polysaccharides
Protein Structure, Quaternary
Protein Structure, Tertiary
Permalink
https://hdl.handle.net/10161/13795
Published Version (Please cite this version)
10.1038/nature10696
Publication Info
McLellan, JS; Pancera, M; Carrico, C; Gorman, J; Julien, JP; Khayat, R; ... Kwong, PD (2011). Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9. Nature, 480(7377). pp. 336-343. 10.1038/nature10696. Retrieved from https://hdl.handle.net/10161/13795.
This is constructed from limited available data and may be imprecise. To cite this article, please review & use the official citation provided by the journal.
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Scholars@Duke

Bonsignori

Mattia Bonsignori

Associate Professor in Medicine
HIV vaccine development Study of B-cell immune responses in HIV positive individuals Determination of correlates of protective immunity to HIV Induction of broadly neutralizing antibodies to HIV Development of multiplex functional assays for the evaluation at a single-cell level of B-cell responses to vaccinations, infections and in vitro stimulation Epidemiology and characterization of bacterial resistance determinants (past) </do
This author no longer has a Scholars@Duke profile, so the information shown here reflects their Duke status at the time this item was deposited.
Crump

John Andrew Crump

Adjunct Professor in the Department of Medicine
I am based in northern Tanzania where I am Site Leader for Duke University&#8217;s collaborative research program based at Kilimanjaro Christian Medical Centre and Director of Tanzania Operations for the Duke Global Health Institute. I oversee the design and implementation of research studies on infectious diseases, particularly febrile illness, invasive bacterial disease, HIV-associated opportunistic infections, clinical trials of antiretroviral therapy and prevention of mother-to-child tr
Haynes

Barton Ford Haynes

Frederic M. Hanes Distinguished Professor of Medicine
Barton F. Haynes, M.D. is the Frederic M. Hanes Professor of Medicine and Immunology, and Director of the Duke Human Vaccine Institute. Prior to leading the DHVI, Dr. Haynes served as Chief of the Division of Rheumatology, Allergy and Clinical Immunology, and later as Chair of the Department of Medicine. As Director of the Duke Human Vaccine Institute, Bart Haynes is leading a team of investigators working on vaccines for emerging infections, including tuberculosis, pandemic influenza, emergi
Alphabetical list of authors with Scholars@Duke profiles.
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