This Article Full Text (PDF) Other Versions of this Article: JVI.00077-08v1 82/10/4762    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via Google Scholar Google Scholar Articles by CALLÉ, A. Articles by GRECO, A. Search for Related Content PubMed PubMed Citation Articles by CALLÉ, A. Articles by GRECO, A.

 Previous Article  |  Next Article 

J. Virol. doi:10.1128/JVI.00077-08
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Nucleolin is required for an efficient herpes simplex virus type 1 infection

Université de Lyon, Lyon, F-69003, France; Université Lyon 1, Lyon, F-69003, France; CNRS, UMR5534, Centre de Génétique Moléculaire et Cellulaire, 16 rue Dubois, Villeurbanne, F-69622, France; Université de Lyon, Ecole Normale Supérieure de Lyon, CNRS USR 3010, Laboratoire Joliot-Curie, 46 Allée d'Italie, Lyon, France, Laboratoire de Biologie Moléculaire de la Cellule, CNRS UMR 5239, IFR128 Biosciences, 46 Allée d'Italie, Lyon, France

^* To whom correspondence should be addressed. Email: greco{at}cgmc.univ-lyon1.fr.

	Abstract

Productive infection of herpes simplex virus type 1 (HSV-1), which occurs in the host cell nucleus, is accompanied by dramatic modifications of the nuclear architecture, including profound alterations of nucleoli morphology. Here, we show that the three more abundant nucleolar proteins- nucleolin, B23 and fibrillarin- are redistributed out of the nucleoli as a consequence of HSV-1 infection. We show that the amount of nucleolin increases progressively during the course of infection. We demonstrate for the first time that a nucleolar protein, i.e. nucleolin, co-localizes with ICP8 in the viral replication compartments, at the time when viral replication is effective, suggesting an involvement of nucleolin in the HSV-1 DNA replication process. At later times of infection, a granular form of nucleolin localizes to the cytoplasm, in structures that display the characteristic features of aggresomes, indicating that this form of nucleolin is very probably destined for degradation. The delocalization of nucleolin from the nucleoli requires the viral ICP4 protein, or factor(s) whose expression involves ICP4. Using siRNA technology, we show that viral replication requires high level of nucleolin expression, demonstrating for the first time a direct role of a nucleolar protein in herpes simplex virus biology.