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 Google Scholar
Google Scholar
Right arrow Articles by Nüesch, J. P. F.
Right arrow Articles by Rommelaere, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nüesch, J. P. F.
Right arrow Articles by Rommelaere, J.

 Previous Article  |  Next Article 

Journal of Virology, June 2009, p. 5854-5863, Vol. 83, No. 11
0022-538X/09/$08.00+0     doi:10.1128/JVI.00039-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Ezrin-Radixin-Moesin Family Proteins Are Involved in Parvovirus Replication and Spreading{triangledown}

Jürg P. F. Nüesch,* Séverine Bär, Sylvie Lachmann,{dagger} and Jean Rommelaere

Program Infection and Cancer, Abteilung F010 and Institut National de la Santé et de la Recherche Médicale U701, Deutsches Krebsforschungszentrum, Heidelberg, Germany

Received 8 January 2009/ Accepted 17 March 2009

The propagation of autonomous parvoviruses is strongly dependent on the phosphorylation of the major nonstructural protein NS1 by members of the protein kinase C (PKC) family. Minute virus of mice (MVM) replication is accompanied by changes in the overall phosphorylation pattern of NS1, which is newly modified at consensus PKC sites. These changes result, at least in part, from the ability of MVM to modulate the PDK-1/PKC pathway, leading to activation and redistribution of both PDK-1 and PKC{eta}. We show that proteins of the ezrin-radixin-moesin (ERM) family are essential for virus propagation and spreading through their functions as adaptors for PKC{eta}. MVM infection led to redistribution of radixin and moesin in the cell, resulting in increased colocalization of these proteins with PKC{eta}. Radixin was found to control the PKC{eta}-driven phosphorylation of NS1 and newly synthesized capsids in vivo. Conversely, radixin phosphorylation and activation were driven by the NS1/CKII{alpha} complex. Altogether, these data argue for ERM proteins being both targets and modulators of parvovirus infection.

* Corresponding author. Mailing address: Program Infection and Cancer, Abt. F010 and INSERM U701, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 242, D-69120 Heidelberg, Germany. Phone: (49) 6221 424982. Fax: (49) 6221 424962. E-mail: jpf.nuesch{at}dkfz-heidelberg.de

{triangledown} Published ahead of print on 25 March 2009.

{dagger} Present address: Protein Phosphorylation Laboratory, Cancer Research UK London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3PX, United Kingdom.

Journal of Virology, June 2009, p. 5854-5863, Vol. 83, No. 11
0022-538X/09/$08.00+0     doi:10.1128/JVI.00039-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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