Autor: |
Luban J; Department of Medicine, Columbia University, College of Physicians and Surgeons, New York, New York 10032., Bossolt KL, Franke EK, Kalpana GV, Goff SP |
Jazyk: |
angličtina |
Zdroj: |
Cell [Cell] 1993 Jun 18; Vol. 73 (6), pp. 1067-78. |
DOI: |
10.1016/0092-8674(93)90637-6 |
Abstrakt: |
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. |
Databáze: |
MEDLINE |
Externí odkaz: |
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