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Proteolytic processing of the human immunodeficiency virus envelope glycoprotein precursor decreases conformational flexibility.
- Source :
-
Journal of virology [J Virol] 2013 Feb; Vol. 87 (3), pp. 1884-9. Date of Electronic Publication: 2012 Nov 21. - Publication Year :
- 2013
-
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.
- Subjects :
- Antibodies, Neutralizing immunology
Antigens, Viral immunology
Epitopes immunology
HIV Antibodies immunology
HIV Envelope Protein gp160 immunology
Humans
Protein Conformation
Proteolysis
Antigens, Viral chemistry
Antigens, Viral metabolism
HIV Envelope Protein gp160 chemistry
HIV Envelope Protein gp160 metabolism
Protein Processing, Post-Translational
Subjects
Details
- Language :
- English
- ISSN :
- 1098-5514
- Volume :
- 87
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Journal of virology
- Publication Type :
- Academic Journal
- Accession number :
- 23175369
- Full Text :
- https://doi.org/10.1128/JVI.02765-12