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 Harb, M.
Right arrow Articles by Poncet, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Harb, M.
Right arrow Articles by Poncet, D.

 Previous Article  |  Next Article 

Journal of Virology, November 2008, p. 11283-11293, Vol. 82, No. 22
0022-538X/08/$08.00+0     doi:10.1128/JVI.00872-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Nuclear Localization of Cytoplasmic Poly(A)-Binding Protein upon Rotavirus Infection Involves the Interaction of NSP3 with eIF4G and RoXaN{triangledown}

Maya Harb,1,# Michelle M. Becker,1,{dagger},# Damien Vitour,1,{ddagger} Carolina H. Baron,1 Patrice Vende,1 Spencer C. Brown,2 Susanne Bolte,2 Stefan T. Arold,3 and Didier Poncet1*

Virologie Moléculaire et Structurale INRA UMR 1157, CNRS UMR 2472, IFR 115, Avenue de la Terrasse, 91198 Gif sur Yvette, France,1 Institut des Sciences du Végétal, UPR CNRS 2355, IFR 87, 91198 Gif-sur-Yvette Cedex, France,2 Centre de Biochimie Structurale, INSERM UMR 554, CNRS UMR 5048, 34090 Montpellier Cedex, France3

Received 24 April 2008/ Accepted 5 September 2008

Rotavirus nonstructural protein NSP3 interacts specifically with the 3' end of viral mRNAs, with the eukaryotic translation initiation factor eIF4G, and with RoXaN, a cellular protein of yet-unknown function. By evicting cytoplasmic poly(A) binding protein (PABP-C1) from translation initiation complexes, NSP3 shuts off the translation of cellular polyadenylated mRNAs. We show here that PABP-C1 evicted from eIF4G by NSP3 accumulates in the nucleus of rotavirus-infected cells. Through modeling of the NSP3-RoXaN complex, we have identified mutations in NSP3 predicted to interrupt its interaction with RoXaN without disturbing the NSP3 interaction with eIF4G. Using these NSP3 mutants and a deletion mutant unable to associate with eIF4G, we show that the nuclear localization of PABP-C1 not only is dependent on the capacity of NSP3 to interact with eIF4G but also requires the interaction of NSP3 with a specific region in RoXaN, the leucine- and aspartic acid-rich (LD) domain. Furthermore, we show that the RoXaN LD domain functions as a nuclear export signal and that RoXaN tethers PABP-C1 with RNA. This work identifies RoXaN as a cellular partner of NSP3 involved in the nucleocytoplasmic localization of PABP-C1.

* Corresponding author. Mailing address: Virologie Moléculaire et Structurale INRA UMR 1157, CNRS UMR 2472, IFR 115, Avenue de la Terrasse, 91198 Gif sur Yvette, France. Phone: 33 169823835. Fax: 33 169824308. E-mail: poncet{at}vms.cnrs-gif.fr

{triangledown} Published ahead of print on 17 September 2008.

# These authors made equal contributions to this work.

{dagger} Present address: Pediatric Infectious Diseases, Vanderbilt University Medical School, Nashville, TN.

{ddagger} Present address: Institut Pasteur, Unité Hepacivirus, 75724 Paris Cedex 15, France.

Journal of Virology, November 2008, p. 11283-11293, Vol. 82, No. 22
0022-538X/08/$08.00+0     doi:10.1128/JVI.00872-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Blakqori, G., van Knippenberg, I., Elliott, R. M. (2009). Bunyamwera Orthobunyavirus S-Segment Untranslated Regions Mediate Poly(A) Tail-Independent Translation. J. Virol. 83: 3637-3646 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»