JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by BouHamdan, M.
Right arrow Articles by Duan, L.-X.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by BouHamdan, M.
Right arrow Articles by Duan, L.-X.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J Biol Chem, Vol. 273, Issue 14, 8009-8016, April 3, 1998

Diversity of HIV-1 Vpr Interactions Involves Usage of the WXXF Motif of Host Cell Proteins

Mohamad BouHamdanDagger , YanNing XueDagger , Yves Baudat, Baocheng HuDagger , Josephine Sire, Roger J. PomerantzDagger , and Ling-Xun DuanDagger

From the Dagger  The Dorrance H. Hamilton Laboratories, Center for Human Virology, Division of Infectious Diseases, Department of Medicine, Jefferson Medical College, Thomas Jefferson University, Philadelphia, Pennsylvania 19107 and  INSERM U372, Pathogenie des infections a lentivirus, BP 178, 13276 Marseille-Cedex 9, France

Targeting protein or RNA moieties to specific cellular compartments may enhance their desired functions and specificities. Human immunodeficiency virus type I (HIV-1) encodes proteins in addition to Gag, Pol, and Env that are packaged into virus particles. One such retroviral-incorporated protein is Vpr, which is present in all primate lentiviruses. Vpr has been implicated in different roles within the HIV-1 life cycle. In testing a new hypothesis in which viral proteins are utilized as docking sites to incorporate protein moieties into virions, we used the peptide phage display approach to search for Vpr-specific binding peptides. In the present studies, we demonstrate that most of the peptides that bind to Vpr have a common motif, WXXF. More importantly, we demonstrate that the WXXF motif of uracil DNA glycosylase is implicated in the interaction of uracil DNA glycosylase with Vpr intracellularly. Finally, a dimer of the WXXF motif was fused to the chloramphenicol acetyl transferase (CAT) gene, and it was demonstrated that the WXXF dimer-CAT fusion protein construct produces CAT activity within virions in the presence of Vpr as a docking protein. This study provides a novel potential strategy in the targeting of anti-viral agents to interfere with HIV-1 replication.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
N. A. Begum, N. Izumi, M. Nishikori, H. Nagaoka, R. Shinkura, and T. Honjo
Requirement of Non-canonical Activity of Uracil DNA Glycosylase for Class Switch Recombination
J. Biol. Chem., January 5, 2007; 282(1): 731 - 742.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
B. Schrofelbauer, Q. Yu, S. G. Zeitlin, and N. R. Landau
Human Immunodeficiency Virus Type 1 Vpr Induces the Degradation of the UNG and SMUG Uracil-DNA Glycosylases
J. Virol., September 1, 2005; 79(17): 10978 - 10987.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. Chen, E. Le Rouzic, J. A. Kearney, L. M. Mansky, and S. Benichou
Vpr-mediated Incorporation of UNG2 into HIV-1 Particles Is Required to Modulate the Virus Mutation Rate and for Replication in Macrophages
J. Biol. Chem., July 2, 2004; 279(27): 28419 - 28425.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
X.-J. Yao, J. Lemay, N. Rougeau, M. Clement, S. Kurtz, P. Belhumeur, and E. A. Cohen
Genetic Selection of Peptide Inhibitors of Human Immunodeficiency Virus Type 1 Vpr
J. Biol. Chem., December 6, 2002; 277(50): 48816 - 48826.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
R. Chen, H. Wang, and L. M. Mansky
Roles of uracil-DNA glycosylase and dUTPase in virus replication
J. Gen. Virol., October 1, 2002; 83(10): 2339 - 2345.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
S. P. Singh, B. Tomkowicz, D. Lai, M. Cartas, S. Mahalingam, V. S. Kalyanaraman, R. Murali, and A. Srinivasan
Functional Role of Residues Corresponding to Helical Domain II (Amino Acids 35 to 46) of Human Immunodeficiency Virus Type 1 Vpr
J. Virol., November 15, 2000; 74(22): 10650 - 10657.
[Abstract] [Full Text]

Home page
 J. Virol.Home page
M. A. Accola, A. A. Bukovsky, M. S. Jones, and H. G. Göttlinger
A Conserved Dileucine-Containing Motif in p6gag Governs the Particle Association of Vpx and Vpr of Simian Immunodeficiency Viruses SIVmac and SIVagm
J. Virol., December 1, 1999; 73(12): 9992 - 9999.
[Abstract] [Full Text]

Home page
 BloodHome page
J. Kulkosky, A. Laptev, S. Shetty, A. Srinivasan, M. BouHamdan, D. J. Prockop, and R. J. Pomerantz
Human Immunodeficiency Virus Type 1 Vpr Alters Bone Marrow Cell Function
Blood, March 15, 1999; 93(6): 1906 - 1915.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
K. E. Willetts, F. Rey, I. Agostini, J.-M. Navarro, Y. Baudat, R. Vigne, and J. Sire
DNA Repair Enzyme Uracil DNA Glycosylase Is Specifically Incorporated into Human Immunodeficiency Virus Type 1 Viral Particles through a Vpr-Independent Mechanism
J. Virol., February 1, 1999; 73(2): 1682 - 1688.
[Abstract] [Full Text]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.