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J. Virol. doi:10.1128/JVI.01336-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

HSP70 NEGATIVELY CONTROLS ROTAVIRUS PROTEIN BIOAVAILABILITY IN CACO-2 CELLS INFECTED BY THE ROTAVIRUS RF STRAIN

Université Pierre et Marie Curie-Paris6 UMR S 538, Paris, F-75012, France; INSERM U538, CHU Saint-Antoine, 27 rue de Chaligny, Paris, F-75571 cedex 12, France; Instituto de Biotecnologia, UNAM, Avenida Universidad 2001, Colonia Chamilpa, Cuernavaca, Morelos 62210, Mexico

^* To whom correspondence should be addressed. Email: marie.bachelet{at}chusa.jussieu.fr,

	Abstract

Previous studies demonstrated that the induction of the heat shock protein Hsp70, in response to viral infection is highly specific and differs from one cell to another and for a given virus type. However, no clear consensus exists so far to explain the likely reasons for Hsp70 induction within host cells during viral infection. We show here that upon rotavirus infection of intestinal cells, Hsp70 is indeed rapidly, specifically and, transiently induced. Using siRNA-Hsp70 transfected Caco-2 cells, we observed that Hsp70 silencing was associated with an increased virus protein level and an enhanced progeny virus production. Upon Hsp70 silencing, we observed that the ubiquitination of the main rotavirus structural proteins was strongly reduced. In addition, the use of proteasome inhibitors in infected Caco-2 cells was shown to induce an accumulation of structural viral proteins. Together these results are consistent with a role of Hsp70 in the control of the bioavailability of viral proteins within the cells for virus morphogenesis.

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