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SPECIFIC INCORPORATION OF CYCLOPHILIN-A INTO HIV-1 VIRIONS
Author(s): FRANKE EK, YUAN HEH, LUBAN J
Source: NATURE    Volume: 372    Issue: 6504    Pages: 359-362    Published: NOV 24 1994  
Times Cited: 397     References: 26     
Abstract: LITTLE is known about host factors necessary for retroviral virion assembly or uncoating. We have previously shown that the principal structural protein of the human immunodeficiency virus HIV-1, the Gag polyprotein, binds the cyclophilin peptidyl-prolyl isomerases(1); cyclophilins catalyse a rate-limiting step in protein folding(2) and protect cells from heat shock(3). Here we demonstrate that cyclophilin A is specifically incorporated into HIV-1 virions but not into virions of other primate immunodeficiency viruses. A proline-rich region conserved in all HIV-1 Gag polyproteins is required for cyclophilin A binding and incorporation. Disruption of a single proline blocks the Gag-cyclophilin interaction in vitro, prevents cyclophilin A incorporation into virions, and inhibits HIV-1 replication. Our results indicate that the interaction of Gag with cyclophilin A is necessary for the formation of infectious HIV-1 virions.
Document Type: Article
Language: English
Reprint Address: FRANKE, EK (reprint author), COLUMBIA UNIV, COLL PHYS & SURG, DEPT MED, 701 W 168TH ST, NEW YORK, NY 10032 USA
Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW
Subject Category: Multidisciplinary Sciences
IDS Number: PU287
ISSN: 0028-0836
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