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  • Title: Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B.
    Author: Luban J, Bossolt KL, Franke EK, Kalpana GV, Goff SP.
    Journal: Cell; 1993 Jun 18; 73(6):1067-78. PubMed ID: 8513493.
    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, cyclophillins (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.
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