Structural Basis of Immune Evasion at the Site of CD4 Attachment on HIV-1 gp120-Reference-Cited by-同舟云学术

Structural Basis of Immune Evasion at the Site of CD4 Attachment on HIV-1 gp120

Published:2009-11-20 Issue:5956 Volume:326 Page:1123-1127
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Chen Lei¹,Do Kwon Young¹,Zhou Tongqing¹,Wu Xueling¹,O’Dell Sijy¹,Cavacini Lisa²,Hessell Ann J.³,Pancera Marie¹,Tang Min¹,Xu Ling¹,Yang Zhi-Yong¹,Zhang Mei-Yun⁴,Arthos James⁵,Burton Dennis R.³⁶,Dimitrov Dimiter S.⁴,Nabel Gary J.¹,Posner Marshall R.²,Sodroski Joseph⁷,Wyatt Richard¹,Mascola John R.¹,Kwong Peter D.¹

Affiliation:

1. Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

2. Head and Neck Oncology Program, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA.

3. Departments of Immunology and Microbial Science and International AIDS Vaccine Initiative Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA.

4. Center for Cancer Research, National Cancer Institute, Frederick, MD 21702, USA.

5. Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

6. Ragon Institute of Massachusetts General Hospital, Massachusetts Institute of Technology and Harvard University, Boston, MA 02114, USA.

7. Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA.

Abstract

Anti-HIV Antibody Constraints Despite significant efforts, an effective vaccine against the HIV-1 virus remains elusive. A site on the HIV-1 gp120 envelope glycoprotein that binds to the CD4 receptor on host cells is vulnerable to antibody, but only rarely are antibodies against this site broadly neutralizing. L. Chen et al. (p. 1123 ) have determined crystal structures for two weakly neutralizing antibodies in complex with gp120. The epitopes recognized by these antibodies were similar to those bound by CD4 or a broadly neutralizing antibody. However, small differences in recognition induced conformational shifts in gp120 that were incompatible with formation of a functional viral spike. Thus, the antibody-vulnerable site on HIV-1 is protected by conformational constraints.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference33 articles.

1. UNAIDS “2006 Report on the Global AIDS Epidemic” (Joint United Nations Programme on HIV/AIDS 2006); www.unaids.org/en/KnowledgeCentre/HIVData/GlobalReport/2006/..

2. Structural definition of a conserved neutralization epitope on HIV-1 gp120

3. Factors Associated with the Development of Cross-Reactive Neutralizing Antibodies during Human Immunodeficiency Virus Type 1 Infection

4. Profiling the Specificity of Neutralizing Antibodies in a Large Panel of Plasmas from Patients Chronically Infected with Human Immunodeficiency Virus Type 1 Subtypes B and C

5. Broad HIV-1 neutralization mediated by CD4-binding site antibodies

Cited by 262 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Membrane HIV-1 envelope glycoproteins stabilized more strongly in a pretriggered conformation than natural virus Envs;iScience;2024-07

2. Human CD4-binding site antibody elicited by polyvalent DNA prime-protein boost vaccine neutralizes cross-clade tier-2-HIV strains;Nature Communications;2024-05-21

3. Neutralizing antibodies to block viral entry and for identification of entry inhibitors;Antiviral Research;2024-04

4. Inhibition of human immunodeficiency virus (HIV-1) infectivity by expression of poorly or broadly neutralizing antibodies against Env in virus-producing cells;Journal of Virology;2024-02-20

5. Absolute quantitation of binding antibodies from clinical samples;npj Vaccines;2024-01-06