P
Peter D. Kwong
Researcher at National Institutes of Health
Publications - 490
Citations - 61386
Peter D. Kwong is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Epitope & Antibody. The author has an hindex of 108, co-authored 436 publications receiving 51150 citations. Previous affiliations of Peter D. Kwong include Vaccine Research Center & Columbia University.
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Journal ArticleDOI
Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
Peter D. Kwong,Richard T. Wyatt,James E. Robinson,Raymond W. Sweet,Joseph Sodroski,Wayne A. Hendrickson,Wayne A. Hendrickson +6 more
TL;DR: The structure reveals a cavity-laden CD4–gp120 interface, a conserved binding site for the chemokine receptor, evidence for a conformational change upon CD4 binding, the nature of a CD4-induced antibody epitope, and specific mechanisms for immune evasion.
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Antibody neutralization and escape by HIV-1
Xiping Wei,Julie M. Decker,Shuyi Wang,Huxiong Hui,John C. Kappes,Xiaoyun Wu,Jesus F. Salazar-Gonzalez,Maria G. Salazar,J. Michael Kilby,Michael S. Saag,Natalia L. Komarova,Martin A. Nowak,Beatrice H. Hahn,Peter D. Kwong,George M. Shaw +14 more
TL;DR: The detection of autologous Nab as early as 52 days after detection of HIV-specific antibodies is reported, indicating a new mechanism contributing to HIV-1 persistence in the face of an evolving antibody repertoire.
Journal ArticleDOI
Rational Design of Envelope Identifies Broadly Neutralizing Human Monoclonal Antibodies to HIV-1
Xueling Wu,Zhi Yong Yang,Yuxing Li,Carl Magnus Hogerkorp,William R. Schief,Michael S. Seaman,Tongqing Zhou,Stephen D. Schmidt,Lan Wu,Ling Xu,Nancy S. Longo,Krisha McKee,Sijy O'Dell,Mark K. Louder,Diane Wycuff,Yu Feng,Martha Nason,Nicole A. Doria-Rose,Mark Connors,Peter D. Kwong,Mario Roederer,Richard T. Wyatt,Gary J. Nabel,John R. Mascola +23 more
TL;DR: Three broadly neutralizing antibodies are identified, isolated from an HIV-1–infected individual, that exhibited great breadth and potency of neutralization and were specific for the co-receptor CD4-binding site of the glycoprotein 120 (gp120), part of the viral Env spike.
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Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7.
Pengfei Wang,Manoj S. Nair,Lihong Liu,Sho Iketani,Sho Iketani,Yang Luo,Yicheng Guo,Maple Wang,Jian Yu,Baoshan Zhang,Peter D. Kwong,Peter D. Kwong,Barney S. Graham,John R. Mascola,Jennifer Y Chang,Jennifer Y Chang,Michael T. Yin,Michael T. Yin,Magdalena E. Sobieszczyk,Magdalena E. Sobieszczyk,Christos A. Kyratsous,Lawrence Shapiro,Lawrence Shapiro,Zizhang Sheng,Yaoxing Huang,David D. Ho,David D. Ho +26 more
TL;DR: In this paper, the authors show that B.1.7 is refractory to neutralization by most monoclonal antibodies against the N-terminal domain of the spike protein and is relatively resistant to a few monoclanal antibody against the receptor-binding domain.
Journal ArticleDOI
The antigenic structure of the HIV gp120 envelope glycoprotein
Richard T. Wyatt,Peter D. Kwong,Elizabeth Desjardins,Raymond W. Sweet,James E. Robinson,Wayne A. Hendrickson,Joseph Sodroski +6 more
TL;DR: The spatial organization of conserved neutralization epitopes on gp120 is described, using epitope maps in conjunction with the X-ray crystal structure of a ternary complex that includes a gp120 core, CD4 and a neutralizing antibody.