Structural basis for membrane anchoring of HIV-1 envelope spike-Reference-Cited by-同舟云学术

Structural basis for membrane anchoring of HIV-1 envelope spike

Published:2016-07-08 Issue:6295 Volume:353 Page:172-175
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Dev Jyoti¹²,Park Donghyun³,Fu Qingshan¹,Chen Jia³⁴,Ha Heather Jiwon³⁴,Ghantous Fadi⁵,Herrmann Tobias²,Chang Weiting³,Liu Zhijun⁶,Frey Gary³⁴,Seaman Michael S.⁵,Chen Bing³⁴,Chou James J.¹⁶

Affiliation:

1. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 250 Longwood Avenue, Boston, MA 02115, USA.

2. Virology Program, Harvard Medical School, 260 Longwood Avenue, Boston, MA 02115, USA.

3. Division of Molecular Medicine, Boston Children’s Hospital, 3 Blackfan Street, Boston, MA 02115, USA.

4. Department of Pediatrics, Harvard Medical School, 300 Longwood Avenue, Boston, MA 02115, USA.

5. Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, 330 Brookline Avenue, Boston, MA 02215, USA.

6. State Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai 200031, China.

Abstract

Env's transmembrane domain revealed HIV-1's envelope protein (Env) spans the viral membrane and grants the virus entry into host cells. Env is also the sole protein of HIV-1 that is targeted by antibodies, making it a key target for vaccine design. Dev et al. used nuclear magnetic resonance to determine an atomic-level structure of the membrane-spanning region of Env in a lipid bicelle. Env's transmembrane domain forms a well-ordered trimer, which includes a stabilizing C-terminal hydrophilic core. Disrupting this core alters the sensitivity of Env to broadly neutralizing antibodies, suggesting the potential importance of this region to vaccine design. Science , this issue p. 172

Funder

Collaboration for AIDS Vaccine Discovery (CAVD)

Bill and Melinda Gates Foundation

Chinese Academy of Sciences

NIH

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference49 articles.

1. Viral membrane fusion

2. Core Structure of gp41 from the HIV Envelope Glycoprotein