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Literature DB >> 23175369

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

Hillel Haim¹, Ignacio Salas, Joseph Sodroski.

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.

Entities: Disease Gene Species

Mesh：

Substances：

Year: 2012 PMID： 23175369 PMCID： PMC3554131 DOI： 10.1128/JVI.02765-12

Source DB: PubMed Journal: J Virol ISSN： 0022-538X Impact factor: 5.103

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