Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer

Author:

Lee Jeong Hyun1,Ozorowski Gabriel1,Ward Andrew B.1

Affiliation:

1. Department of Integrative Structural and Computational Biology, Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, International AIDS Vaccine Initiative Neutralizing Antibody Center, and Collaboration for AIDS Vaccine Discovery, The Scripps Research Institute, La Jolla, CA 92037, USA.

Abstract

A more complete look at the HIV-1 envelope HIV-1 uses its envelope protein (Env), a large glycoprotein present on the viral surface, to enter target cells. Env forms trimers on the viral surface. Structural studies of solubilized Env trimers have provided important insights into viral entry and antibody binding, but soluble trimers lack several important insoluble regions of the native protein. Lee et al. used cryo–electron microscopy to solve the structure of a trimeric Env protein of HIV-1, missing only its cytoplasmic tail, in complex with broadly neutralizing antibodies. A more complete understanding of Env's structure may aid in vaccine design ef orts. Science , this issue p. 1043

Funder

NIH

Collaboration for AIDS Vaccine Discovery

California HIV/AIDS Research Program Dissertation Award

U.S. Agency for International Development (USAID)

Ministry of Foreign Affairs of the Netherlands

Bill and Melinda Gates Foundation

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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