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Virology. 1998 Dec 5;252(1):228-34.

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

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1
Department of Pathology and Laboratory Medicine, University of Wisconsin, Madison 53706, USA.

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.

PMID:
9875332
DOI:
10.1006/viro.1998.9468
[Indexed for MEDLINE]
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