Structure of the transmembrane domain of HIV-1 envelope glycoprotein

FEBS J. 2017 Apr;284(8):1171-1177. doi: 10.1111/febs.13954. Epub 2016 Nov 20.

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.

Keywords: HIV; envelope; nuclear magnetic resonance; transmembrane.

Publication types

  • Review
  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • HIV Envelope Protein gp160 / chemistry*
  • HIV Envelope Protein gp160 / immunology
  • HIV Envelope Protein gp160 / physiology
  • HIV-1 / chemistry*
  • HIV-1 / physiology
  • Membrane Fusion / physiology
  • Models, Molecular
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Vaccines, Synthetic / chemistry

Substances

  • HIV Envelope Protein gp160
  • Vaccines, Synthetic