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
Services
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 arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Watashi, K.
Right arrow Articles by Jeang, K.-T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Watashi, K.
Right arrow Articles by Jeang, K.-T.

 Previous Article  |  Next Article 

Journal of Virology, October 2008, p. 9928-9936, Vol. 82, No. 20
0022-538X/08/$08.00+0     doi:10.1128/JVI.01017-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Human Immunodeficiency Virus Type 1 Replication and Regulation of APOBEC3G by Peptidyl Prolyl Isomerase Pin1{triangledown}

Koichi Watashi,1 Mohammad Khan,2 Venkat R. K. Yedavalli,1 Man Lung Yeung,1 Klaus Strebel,2 and Kuan-Teh Jeang1*

Molecular Virology Section,1 Viral Biochemistry Section, Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 208922

Received 15 May 2008/ Accepted 31 July 2008

APOBEC3G (A3G) is a cytidine deaminase that restricts human immunodeficiency virus type 1 (HIV-1) replication. HIV-1 synthesizes a viral infectivity factor (Vif) to counter A3G restriction. Currently, it is poorly understood how A3G expression/activity is regulated by cellular factors. Here, we show that the prolyl isomerase Pin1 protein modulates A3G expression. Pin1 was found to be an A3G-interacting protein that reduces A3G expression and its incorporation into HIV-1 virion, thereby limiting A3G-mediated restriction of HIV-1. Intriguingly, HIV-1 infection modulates the phosphorylation state of Pin1, enhancing its ability to moderate A3G activity. These new findings suggest a potential Vif-independent way for HIV-1 to moderate the cellular action of A3G.


* Corresponding author. Mailing address: 9000 Rockville Pike, Building 4, Room 306, Bethesda, MD 20892. Phone: (301) 496-6680. Fax: (301) 480-3686. E-mail: kj7e{at}nih.gov

{triangledown} Published ahead of print on 6 August 2008.


Journal of Virology, October 2008, p. 9928-9936, Vol. 82, No. 20
0022-538X/08/$08.00+0     doi:10.1128/JVI.01017-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Peloponese, J.-M. Jr., Yasunaga, J., Kinjo, T., Watashi, K., Jeang, K.-T. (2009). Peptidylproline cis-trans-Isomerase Pin1 Interacts with Human T-Cell Leukemia Virus Type 1 Tax and Modulates Its Activation of NF-{kappa}B. J. Virol. 83: 3238-3248 [Abstract] [Full Text]  
  • Goila-Gaur, R., Khan, M. A., Miyagi, E., Strebel, K. (2009). Differential Sensitivity of "Old" versus "New" APOBEC3G to Human Immunodeficiency Virus Type 1 Vif. J. Virol. 83: 1156-1160 [Abstract] [Full Text]