Peptide mimic of the HIV envelope gp120-gp41 interface

Journal of Molecular Biology
Sunghwan KimM S Kay

Abstract

The human immunodeficiency virus envelope glycoprotein (Env) is composed of surface (gp120) and transmembrane (gp41) subunits, which are noncovalently associated on the viral surface. Human immunodeficiency virus Env mediates viral entry after undergoing a complex series of conformational changes induced by interaction with cellular CD4 and a chemokine coreceptor. These changes propagate from gp120 to gp41 via the gp120-gp41 interface, ultimately exposing gp41 and allowing it to form the trimer-of-hairpins structure that provides the driving force for membrane fusion. Key unresolved questions about the gp120-gp41 interface include the specific regions of gp41 and gp120 involved, the mechanism by which receptor and coreceptor-binding-induced conformational changes in gp120 are communicated to gp41, how trimer-of-hairpins formation is prevented in the prefusogenic gp120-gp41 complex, and, ultimately, the structure of the prefusion gp120-gp41 complex. Here, we develop a biochemical model system that mimics a key portion of the gp120-gp41 interface in the prefusogenic state. We find that a gp41 fragment containing the disulfide bond loop and C-peptide region binds primarily to the gp120 C5 region and that this interaction is incomp...Continue Reading

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Citations

Dec 4, 2009·PLoS Pathogens·Kristen M KahleMichael J Root
Jan 25, 2013·Viruses·Christopher J De Feo, Carol D Weiss
Mar 8, 2011·Trends in Microbiology·Michael Caffrey
Jan 1, 2009·Drug Discovery Today. Technologies
Sep 20, 2008·Protein Science : a Publication of the Protein Society·Debra M EckertMichael S Kay
Jan 1, 2012·Pharmaceuticals·Ramachandran Murali, Mark I Greene

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