J Gen Virol Tips for Better Browsing
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


J Gen Virol 85 (2004), 3291-3303; DOI 10.1099/vir.0.80198-0

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 CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mueller, S. M.
Right arrow Articles by Lang, S. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mueller, S. M.
Right arrow Articles by Lang, S. M.
Agricola
Right arrow Articles by Mueller, S. M.
Right arrow Articles by Lang, S. M.
© 2004 Society for General Microbiology

Vpx proteins of SIVmac239 and HIV-2ROD interact with the cytoskeletal protein {alpha}-actinin 1

Sandra M. Mueller, Ronny Jung{dagger}, Sigrid Weiler{ddagger} and Sabine M. Lang§

Institute of Clinical and Molecular Virology, University of Erlangen-Nuernberg, Schlossgarten 4, D-91054 Erlangen, Germany

Correspondence
Sabine M. Lang
sabine.lang{at}yale.edu

vpx genes of human immunodeficiency virus type 2 (HIV-2) and immunodeficiency viruses from macaques (SIVmac), sooty mangabeys (SIVsm) and red-capped mangabeys (SIVrcm) encode a 112 aa protein that is packed into virion particles via interaction with the p6 domain of p55gag. Vpx localizes to the nucleus when expressed in the absence of other viral proteins. Moreover, Vpx is necessary for efficient nuclear import of the pre-integration complex (PIC) and critical for virus replication in quiescent cells, such as terminally differentiated macrophages and memory T cells. Vpx does not contain sequence elements that are homologous to previously characterized nuclear localization signals (NLSs). Therefore, it is likely that Vpx-dependent import of the PIC is mediated by interaction of Vpx with cellular proteins that do not belong to the classical import pathways. By using a yeast two-hybrid screen, {alpha}-actinin 1, a cytoskeletal protein, was identified to interact with SIVmac239 Vpx. Interestingly, deletion of the proline-rich C-terminal domain (aa 101–112) of Vpx, which is important for nuclear localization, resulted in loss of interaction with {alpha}-actinin 1. These findings suggest that the interaction with {alpha}-actinin 1 may play an important role in the transport of Vpx to the nucleus and in Vpx-mediated nuclear import of the PIC.

{dagger}Present address: Department of Pediatrics and Adolescent Medicine, University of Erlangen-Nuernberg, Loschgestr. 15, D-91054 Erlangen, Germany.

{ddagger}Present address: Institute for Microbiology, Biochemistry and Genetics, Department of Biotechnology, Henkestrasse 91, D-91052 Erlangen, Germany.

§Present address: Yale University School of Medicine, Department of Pathology, PO Box 208023, 310 Cedar St, New Haven, CT 06520-8023, USA.




This article has been cited by other articles:


Home page
J. Virol.Home page
X. Cheng, M. Belshan, and L. Ratner
Hsp40 Facilitates Nuclear Import of the Human Immunodeficiency Virus Type 2 Vpx-Mediated Preintegration Complex
J. Virol., February 1, 2008; 82(3): 1229 - 1237.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2004 by the Society for General Microbiology.