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Journal of Virology, April 1999, p. 2667-2674, Vol. 73, No. 4
Howard Hughes Medical
Institute2 and Departments of
Microbiology1 and
Medicine,3 University of Pennsylvania
School of Medicine, Philadelphia, Pennsylvania 19104-6148
Received 30 July 1998/Accepted 9 December 1998
The Vif protein of human immunodeficiency virus type 1 (HIV-1) is a
potent regulator of viral infectivity. Current data posit that Vif
functions late in replication to modulate assembly, budding, and/or
maturation. Consistent with this model, earlier indirect immunofluorescence analyses of HIV-1-infected cells demonstrated that
Vif and Gag colocalize to a substantial degree (J. H. M. Simon, R. A. M. Fouchier, T. E. Southerling, C. B. Guerra, C. K. Grant, and M. H. Malim, J. Virol.
71:5259-5267, 1997). Here, we describe a series of subcellular
fractionation studies which indicate that Vif and the
p55Gag polyprotein are present in membrane-free cytoplasmic
complexes that copurify in sucrose density gradients and are stable in
nonionic detergents. Both Vif and Gag are targeted to these complexes
independent of each other, and their association with them appears to
be mediated by protein-protein interactions. We propose that these
complexes may represent viral assembly intermediates and that Vif is
appropriately localized to influence the final stages of the viral life
cycle and, therefore, the infectivity of progeny virions.
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Vif and the p55Gag Polyprotein of Human
Immunodeficiency Virus Type 1 Are Present in Colocalizing Membrane-Free
Cytoplasmic Complexes
*
Corresponding author. Mailing address: Departments of
Microbiology and Medicine, University of Pennsylvania School of
Medicine, Clinical Research Bldg., Room 347B, 415 Curie Blvd.,
Philadelphia, PA 19104-6148. Phone: (215) 573-3493. Fax: (215)
573-2172. E-mail: malim{at}mail.med.upenn.edu.
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