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J Virol, June 1998, p. 5189-5197, Vol. 72, No. 6
McArdle Laboratory for Cancer Research,
University of Wisconsin Medical School, Madison, Wisconsin
53706,1 and
Verna and Marrs McLean
Department of Biochemistry, Baylor College of Medicine, Houston, Texas
770302
Received 19 November 1997/Accepted 19 February 1998
Viral protein U (Vpu) is a protein encoded by human
immunodeficiency virus type 1 (HIV-1) that promotes the degradation of the virus receptor, CD4, and enhances the release of virus particles from cells. We isolated a cDNA that encodes a novel cellular protein that interacts with Vpu in vitro, in vivo, and in yeast cells. This
Vpu-binding protein (UBP) has a molecular mass of 41 kDa and is
expressed ubiquitously in human tissues at the RNA level. UBP is a
novel member of the tetratricopeptide repeat (TPR) protein family
containing four copies of the 34-amino-acid TPR motif. Other proteins
that contain TPR motifs include members of the immunophilin
superfamily, organelle-targeting proteins, and a protein phosphatase.
UBP also interacts directly with HIV-1 Gag protein, the principal
structural component of the viral capsid. However, when Vpu and Gag are
coexpressed, stable interaction between UBP and Gag is diminished.
Furthermore, overexpression of UBP in virus-producing cells resulted in
a significant reduction in HIV-1 virion release. Taken together, these
data indicate that UBP plays a role in Vpu-mediated enhancement of
particle release.
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Functional Interaction of Human Immunodeficiency
Virus Type 1 Vpu and Gag with a Novel Member of the
Tetratricopeptide Repeat Protein Family
*
Corresponding author. Mailing address: McArdle
Laboratory for Cancer Research, University of Wisconsin Medical School,
1400 University Ave., Madison, WI 53706. Phone: (608) 263-7820. Fax: (608) 262-2824. E-mail: Panganiban{at}oncology.wisc.edu.
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