Structure of the transmembrane domain of HIV‐1 envelope glycoprotein. (20th November 2016)

• Record Type: Journal Article
• Authors: Chen, Bing; Chou, James J.
• Is Part Of: FEBS journal. Volume 284:Number 8(2017)
• Page Start: 1171
• Page End: 1177
• Publication Date: 2016-11-20
• Subjects: envelope -- HIV -- nuclear magnetic resonance -- transmembrane; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pathology, Molecular -- Periodicals; 572
• DOI: 10.1111/febs.13954
• Languages: English
• ISSNs: 1742-464X

Abstract

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. Abstract : HIV‐1 envelope spike mediates viral entry to initiate infection. It is also a major viral antigen and thus an important candidate for vaccine development. We have recently reported a structure of the transmembrane (TM) domain of HIV‐1 envelope reconstituted in a membrane‐like environment. This structural snapshot discusses how a TM domain anchors, stabilizes, and modulates a viral envelope spike.