Mapping out the intricate relationship of the HIV envelope protein and the membrane environment.

Yoel A Klug, Etai Rotem, Roland Schwarzer, Yechiel Shai

Journal: Biochimica et biophysica acta. Biomembranes 2017;1859(4):550-560

PMID: 27793589

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Abstract

The HIV gp160 envelope fusion protein is situated in the viral membrane and mediates virus entry into its host cell. Increasing evidence suggests that virtually all parts of the HIV envelope are structurally and functionally dependent on membranes. Protein-lipid interactions and membrane properties influence the dynamics of a manifold of gp160 biological activities such as membrane fusion, immune suppression and gp160 incorporation into virions during HIV budding and assembly. In the following we will summarize our current understanding of this interdependence between membrane interaction, structural conformation and functionality of the different gp160 domains. This article is part of a Special Issue entitled: Lipid order/lipid defects and lipid-control of protein activity edited by Dirk Schneider.

Address: Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel.

DOI: 10.1016/j.bbamem.2016.10.012

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MeSH Terms: Amino Acid Sequence, Gene Expression, HIV Envelope Protein gp120, HIV Envelope Protein gp160, HIV Envelope Protein gp41, HIV-1, Host-Pathogen Interactions, Humans, Membrane Fusion, Membrane Microdomains, Protein Conformation, Receptors, Antigen, T-Cell, Sphingomyelins, T-Lymphocytes, Virus Assembly, Virus Release