Hsp70 negatively controls rotavirus protein bioavailability in caco-2 cells infected by the rotavirus RF strain.

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 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

SUBMITTER: Broquet AH 

PROVIDER: S-EPMC1797523 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature