title: Proteolytic processing of the human immunodeficiency virus envelope glycoprotein precursor decreases conformational flexibility.
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.
authors.affiliation: Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, USA.
authors.forename: Hillel
authors.initials: H
authors.lastname: Haim
authors.forename: Ignacio
authors.initials: I
authors.lastname: Salas
authors.forename: Joseph
authors.initials: J
authors.lastname: Sodroski
mesh_terms: D057134:Antibodies, Neutralizing / Q000276:immunology; D000956:Antigens, Viral / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism*; D000939:Epitopes / Q000276:immunology; D015483:HIV Antibodies / Q000276:immunology; D019302:HIV Envelope Protein gp160 / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism*; D006801:Humans; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D059748:Proteolysis
chemical_list: D057134:Antibodies, Neutralizing; D000956:Antigens, Viral; D000939:Epitopes; D015483:HIV Antibodies; D019302:HIV Envelope Protein gp160; C514797:gp160 protein, Human immunodeficiency virus 1