Hsp70 negatively controls rotavirus protein bioavailability in caco-2 cells infected by the rotavirus RF strain
| Autor: | Germain Trugnan, Susana López, Alexis Broquet, Agnès Gardet, Ginette Thomas, Christelle Lenoir, Anne-Marie Jouniaux, Serge Chwetzoff, Catherine Sapin, Maria Bachelet |
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| Přispěvatelé: | Université Pierre et Marie Curie - Paris 6 (UPMC), Trafic Membranaire et Signalisation Dans les Cellules Epitheliales, Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), CHU Saint-Antoine [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU), Unité de recherche Virologie et Immunologie Moléculaires (VIM (UR 0892)), Institut National de la Recherche Agronomique (INRA), Instituto de Biotecnología, Universidad Nacional Autónoma de México = National Autonomous University of Mexico (UNAM), ProdInra, Migration, Universidad Nacional Autónoma de México (UNAM) |
| Rok vydání: | 2006 |
| Předmět: |
Gene Expression Regulation
Viral Rotavirus viruses Immunology Cell Biology medicine.disease_cause Microbiology Virus 03 medical and health sciences Viral Proteins Virology Heat shock protein medicine Gene silencing Humans HSP70 Heat-Shock Proteins 030304 developmental biology Regulation of gene expression [SDV.MP.VIR] Life Sciences [q-bio]/Microbiology and Parasitology/Virology 0303 health sciences 030302 biochemistry & molecular biology 3. Good health Hsp70 Virus-Cell Interactions medicine.anatomical_structure Proteasome Insect Science [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology Caco-2 Cells |
| Zdroj: | Journal of Virology Journal of Virology, American Society for Microbiology, 2007, 81 (3), pp.1297-1304. ⟨10.1128/JVI.01336-06⟩ Journal of Virology, 2007, 81 (3), pp.1297-1304. ⟨10.1128/JVI.01336-06⟩ |
| ISSN: | 0022-538X 1098-5514 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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