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Journal of Virology, February 2007, p. 1297-1304, Vol. 81, No. 3
0022-538X/07/$08.00+0 doi:10.1128/JVI.01336-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Université Pierre et Marie Curie-Paris 6, UMR S 538, Paris F-75012, France,1 INSERM U538, CHU Saint-Antoine, 27 rue de Chaligny, Paris F-75571 Cedex 12, France,2 Instituto de Biotecnologia, UNAM, Avenida Universidad 2001, Colonia Chamilpa, Cuernavaca, Morelos 62210, Mexico,3 Département de Pathologie Animale, INRA, Jouy-en-Josas, France4
Received 26 June 2006/ Accepted 26 October 2006
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 small interfering RNA-Hsp70-transfected Caco-2 cells, we observed that Hsp70 silencing was associated with an increased virus protein level and 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 cells for virus morphogenesis.
Published ahead of print on 1 November 2006.
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