Journal
JOURNAL OF VIROLOGY
Volume 87, Issue 3, Pages 1884-1889Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.02765-12
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Funding
- NRSA [NIH T32 AI007386]
- National Institutes of Health [AI24755, AI67854, AI060354]
- International AIDS Vaccine Initiative
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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.
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