Crystal Structure of a Soluble Cleaved HIV-1 Envelope Trimer-Reference-Cited by-同舟云学术

Crystal Structure of a Soluble Cleaved HIV-1 Envelope Trimer

Published:2013-12-20 Issue:6165 Volume:342 Page:1477-1483
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Julien Jean-Philippe¹²³,Cupo Albert⁴,Sok Devin²³⁵,Stanfield Robyn L.¹²³,Lyumkis Dmitry¹⁶,Deller Marc C.⁷,Klasse Per-Johan⁴,Burton Dennis R.²³⁵⁸,Sanders Rogier W.⁴⁹,Moore John P.⁴,Ward Andrew B.¹²³,Wilson Ian A.¹²³⁷¹⁰

Affiliation:

1. Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

2. International AIDS Vaccine Initiative Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA.

3. Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, The Scripps Research Institute, La Jolla, CA 92037, USA.

4. Weill Medical College of Cornell University, New York, NY 10021, USA.

5. Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA.

6. National Resource for Automated Molecular Microscopy, The Scripps Research Institute, La Jolla, CA 92037, USA.

7. Joint Center for Structural Genomics, The Scripps Research Institute, La Jolla, CA 92037, USA.

8. Ragon Institute of Massachusetts General Hospital, Massachusetts Institute of Technology, and Harvard University, Cambridge, MA 02129, USA.

9. Department of Medical Microbiology, Academic Medical Center, Amsterdam, Netherlands.

10. Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

Abstract

Knowing the Enemy Infection of host cells by HIV-1 is mediated by an envelope glycoprotein (Env) trimeric spike on the surface of the virus. Proteins comprising the Env trimer must be cleaved for infectivity, and thus viral fusion involves three Env conformations. The flexibility of the Env trimer has made it a challenge to determine a high-resolution structure, although such a structure is key both for understanding trimer function and for guiding vaccine design. Lyumkis et al. (p. 1484 ) and Julien et al. (p. 1477 ) studied soluble cleaved trimers stabilized by specific mutations but that have kept a near-native antigenicity profile. Lyumkis et al. present a high-resolution structure of the trimer in complex with a broadly neutralizing antibody, and Julien et al. present a crystal structure of the trimer in complex with another broadly neutralizing antibody.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference70 articles.

1. Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120

2. Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops

3. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody

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

5. Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility

Cited by 765 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. Comprehensive Insights into the Molecular Basis of HIV Glycoproteins;Applied Sciences;2024-09-13

2. Rare twin cysteine residues in the HIV-1 envelope variable region 1 link to neutralization escape and breadth development;2024-09-10

3. Intermediate open state of CD4-bound HIV-1 env heterotrimers in asia CRFs;Biochemical and Biophysical Research Communications;2024-09

4. Design of soluble HIV-1 envelope trimers free of covalent gp120-gp41 bonds with prevalent native-like conformation;Cell Reports;2024-08

5. Cryo-electron microscopy in the study of virus entry and infection;Frontiers in Molecular Biosciences;2024-07-24