Asymmetric Structures and Conformational Plasticity of the Uncleaved Full-Length Human Immunodeficiency Virus Envelope Glycoprotein Trimer

Author:

Zhang Shijian12,Wang Kunyu3,Wang Wei Li134,Nguyen Hanh T.12,Chen Shuobing3,Lu Maolin5ORCID,Go Eden P.6,Ding Haitao7,Steinbock Robert T.1,Desaire Heather6,Kappes John C.78,Sodroski Joseph129ORCID,Mao Youdong134ORCID

Affiliation:

1. Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA

2. Department of Microbiology, Harvard Medical School, Boston, Massachusetts, USA

3. State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, School of Physics, Center for Quantitative Biology, Peking University, Beijing, China

4. Intel Parallel Computing Center for Structural Biology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA

5. Department of Microbial Pathogenesis, Yale University School of Medicine, New Haven, Connecticut, USA

6. Department of Chemistry, University of Kansas, Lawrence, Kansas, USA

7. Department of Medicine, University of Alabama at Birmingham, Alabama, USA

8. Birmingham Veterans Affairs Medical Center, Research Service, Birmingham, Alabama, USA

9. Department of Immunology and Infectious Disease, Harvard T.H. Chan School of Public Health, Boston, Massachusetts, USA

Abstract

The envelope glycoprotein (Env) trimers on the surface of human immunodeficiency virus (HIV-1) mediate the entry of the virus into host cells and serve as targets for neutralizing antibodies. The functional Env trimer is produced by cleavage of the gp160 precursor in the infected cell.

Funder

Natural Science Foundation of Beijing Municipality

HHS | National Institutes of Health

National Natural Science Foundation of China

amfAR, The Foundation for AIDS Research

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

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