Cryo-EM Structure of a Fully Glycosylated Soluble Cleaved HIV-1 Envelope Trimer-Reference-Cited by-同舟云学术

Cryo-EM Structure of a Fully Glycosylated Soluble Cleaved HIV-1 Envelope Trimer

Published:2013-12-20 Issue:6165 Volume:342 Page:1484-1490
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Lyumkis Dmitry¹²,Julien Jean-Philippe²³⁴,de Val Natalia²³,Cupo Albert⁵,Potter Clinton S.¹²,Klasse Per-Johan⁵,Burton Dennis R.³⁶⁷⁸,Sanders Rogier W.⁵⁹,Moore John P.⁵,Carragher Bridget¹²,Wilson Ian A.²³⁴⁶,Ward Andrew B.²³⁶

Affiliation:

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

2. Department of Integrative Structural and Computational Biology, 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. Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

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

6. International AIDS Vaccine Initiative (IAVI) Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA.

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

8. Ragon Institute of MGH, MIT, and Harvard, Cambridge, MA 02129, USA.

9. Department of Medical Microbiology, Academic Medical Center, 1105 AZ Amsterdam, Netherlands.

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

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