Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B.
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.
Department of Medicine, Columbia University, College of Physicians and Surgeons, New York, New York 10032.
J
J
Luban
K L
KL
Bossolt
E K
EK
Franke
G V
GV
Kalpana
S P
SP
Goff
D000591:Amino Acid Isomerases / Q000378:metabolism*; D000595:Amino Acid Sequence; D001483:Base Sequence; D002352:Carrier Proteins / Q000378:metabolism*; D021983:Cyclophilins; D015683:Gene Products, gag / Q000378:metabolism*; D015497:HIV-1 / Q000378:metabolism / Q000472:pathogenicity*; D006801:Humans; D008969:Molecular Sequence Data; D019696:Peptidylprolyl Isomerase; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000378:metabolism
D002352:Carrier Proteins; D015683:Gene Products, gag; D011993:Recombinant Fusion Proteins; C081786:cyclophilin B; D000591:Amino Acid Isomerases; D021983:Cyclophilins; D019696:Peptidylprolyl Isomerase