HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 GAG PROTEIN BINDS TO CYCLOPHILIN-A AND CYCLOPHILIN-B

被引：701

作者：

LUBAN, J ^{[1
]}

BOSSOLT, KL ^{[1
]}

FRANKE, EK ^{[1
]}

KALPANA, GV ^{[1
]}

GOFF, SP ^{[1
]}

机构：

[1] COLUMBIA UNIV COLL PHYS & SURG,DEPT BIOCHEM & MOLEC BIOPHYS,NEW YORK,NY 10032

来源：

CELL | 1993年 / 73卷 / 06期

关键词：

D O I：

10.1016/0092-8674(93)90637-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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, cyclophilins (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.

引用

页码：1067 / 1078

页数：12

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