Structure of the transmembrane domain of HIV-1 envelope glycoprotein.

Bing Chen, James J Chou

Journal: The FEBS journal 2017;284(8):1171-1177

PMID: 27868386

Abstract

HIV-1 envelope spike (Env) is a heavily glycosylated, type I membrane protein that mediates fusion of viral and cell membranes to initiate infection. It is also a primary target of neutralizing antibodies and thus an important candidate for vaccine development. We have recently reported a nuclear magnetic resonance structure of the transmembrane (TM) domain of HIV-1 Env reconstituted in a membrane-like environment. Taking HIV-1 as an example, we discuss here how a TM domain can anchor, stabilize, and modulate a viral envelope spike and how its high-resolution structure can contribute to understanding viral membrane fusion and to immunogen design.

© 2016 Federation of European Biochemical Societies.

Address: Division of Molecular Medicine, Department of Pediatrics, Boston Children's Hospital, Harvard Medical School, Boston, MA, USA.; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA.
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