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J Virol. 2013 Feb;87(3):1884-9. doi: 10.1128/JVI.02765-12. Epub 2012 Nov 21.

Proteolytic processing of the human immunodeficiency virus envelope glycoprotein precursor decreases conformational flexibility.

Author information

1
Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, USA.

Abstract

The mature envelope glycoprotein (Env) spike on the surface of human immunodeficiency virus type 1 (HIV-1) virions is derived by proteolytic cleavage of a trimeric gp160 glycoprotein precursor. Remarkably, proteolytic processing of the HIV-1 Env precursor results in changes in Env antigenicity that resemble those associated with glutaraldehyde fixation. Apparently, proteolytic processing of the HIV-1 Env precursor decreases conformational flexibility of the Env trimeric complex, differentially affecting the integrity/accessibility of epitopes for neutralizing and nonneutralizing antibodies.

PMID:
23175369
PMCID:
PMC3554131
DOI:
10.1128/JVI.02765-12
[Indexed for MEDLINE]
Free PMC Article

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