Journal article
Proteolytic Processing of the Human Immunodeficiency Virus Envelope Glycoprotein Precursor Decreases Conformational Flexibility
Journal of virology, Vol.87(3), pp.1884-1889
02/2013
DOI: 10.1128/JVI.02765-12
PMCID: PMC3554131
PMID: 23175369
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.
Details
- Title: Subtitle
- Proteolytic Processing of the Human Immunodeficiency Virus Envelope Glycoprotein Precursor Decreases Conformational Flexibility
- Creators
- Hillel Haim - Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, USAIgnacio Salas - Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, USAJoseph Sodroski - Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, USA
- Resource Type
- Journal article
- Publication Details
- Journal of virology, Vol.87(3), pp.1884-1889
- Publisher
- American Society for Microbiology
- DOI
- 10.1128/JVI.02765-12
- PMID
- 23175369
- PMCID
- PMC3554131
- ISSN
- 0022-538X
- eISSN
- 1098-5514
- Language
- English
- Date published
- 02/2013
- Academic Unit
- Microbiology and Immunology
- Record Identifier
- 9984083888302771
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