Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B

Jeremy Luban, Karen Leigh Bossolt, Ettaly K. Franke, Ganjam V. Kalpana, Stephen P. Goff

Research output: Contribution to journalArticle

649 Scopus citations

Abstract

Retroviral Gag protein is capable of directing the assembly of virion particles independent of other retroviral elements and plays an important role early in the infection of a cell. Using the GAL4 two hybrid system, we screened a cDNA expression library and identified two host proteins, cyclophillns (CyPs) A and B, which interact specifically with the human immunodeficiency virus type 1 (HIV-1) Gag polyprotein Pr55gag. Glutathione S-transferase-CyP fusion proteins bind tightly to Pr55gag in vitro, as well as to the HIV-1 capsid protein p24. Cyclosporin A efficiently disrupts the Gag-CyPA interaction and less efficiently disrupts the Gag-CyPB interaction. The Gag-CyP interaction may be important for the HIV-1 life cycle and may be relevant to the pathology caused by this immunosuppressive virus.

Original languageEnglish (US)
Pages (from-to)1067-1078
Number of pages12
JournalCell
Volume73
Issue number6
DOIs
Publication statusPublished - Jun 18 1993
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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