ReportStructural Biology

Structural basis for membrane anchoring of HIV-1 envelope spike

+ See all authors and affiliations

Science  23 Jun 2016:
aaf7066
DOI: 10.1126/science.aaf7066

You are currently viewing the abstract.

View Full Text

Abstract

HIV-1 envelope spike (Env) is a type I membrane protein that mediates viral entry. We use NMR to determine an atomic structure of the transmembrane (TM) domain of HIV-1 Env reconstituted in bicelles that mimic a lipid bilayer. The TM forms a well-ordered trimer that protects a conserved membrane-embedded arginine. An N-terminal coiled-coil and a C-terminal hydrophilic core stabilize the trimer. Individual mutations of conserved residues did not disrupt the TM trimer and minimally affected membrane fusion and infectivity. Major changes in the hydrophilic core, however, altered the antibody sensitivity of Env. These results show how a TM domain anchors, stabilizes and modulates a viral envelope spike and suggest that its influence on Env conformation is an important consideration for HIV-1 immunogen design.

View Full Text