Gag protein from human immunodeficiency virus type 1 assembles in the absence of cyclophilin A

Daniel N. Streblow, Moiz Kitabwalla, C. David Pauza

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

Human immunodeficiency virus type 1 (HIV-1) replication requires coordinated activities of host and viral factors. We reported previously that interactions of the host factor cyclophilin A with HIV-1 Gag polyproteins affected Gag processing and maturation of virus particles (Streblow et al., 1998. Virology 245, 197-202). We now use in vitro translation and physical analysis of Gag structures to refine our understanding of how cyclophilin A affects HIV-1 replication. Gag assembled into oligomeric structures in vitro in the presence or absence of cyclophilin A, and proteins synthesized under the two conditions were equally susceptible to cleavage by exogenous HIV-1 protease. These and previous data show that Cyclophilin A is required at a step between Gag assembly and Gag processing/virion morphogenesis. Cyclophilin A may be required for Gag conformational changes subsequent to assembly, that are required for efficient dimerization and activation of the viral protease.

Original languageEnglish (US)
Pages (from-to)228-234
Number of pages7
JournalVirology
Volume252
Issue number1
DOIs
StatePublished - Dec 5 1998

ASJC Scopus subject areas

  • Virology

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