Expression of nonstructural rotavirus protein NSP4 mimics Ca2+ homeostasis changes induced by rotavirus infection in cultured cells. - Université Pierre et Marie Curie Accéder directement au contenu
Article Dans Une Revue Journal of Virology Année : 2008

Expression of nonstructural rotavirus protein NSP4 mimics Ca2+ homeostasis changes induced by rotavirus infection in cultured cells.

Yuleima Díaz
  • Fonction : Auteur
Maria Elena Chemello
  • Fonction : Auteur
Franshelle Peña
  • Fonction : Auteur
Olga Carolina Aristimuño
  • Fonction : Auteur
Jose Luis Zambrano
  • Fonction : Auteur
Hector Rojas
  • Fonction : Auteur
Fulvia Bartoli
  • Fonction : Auteur
Leiria Salazar
  • Fonction : Auteur
Serge Chwetzoff
  • Fonction : Auteur
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Catherine Sapin
  • Fonction : Auteur
Fabian Michelangeli
  • Fonction : Auteur
Marie Christine Ruiz
  • Fonction : Auteur

Résumé

Rotavirus infection modifies Ca(2+) homeostasis, provoking an increase in Ca(2+) permeation, the cytoplasmic Ca(2+) concentration ([Ca(2+)](cyto)), and total Ca(2+) pools and a decrease in Ca(2+) response to agonists. A glycosylated viral protein(s), NSP4 and/or VP7, may be responsible for these effects. HT29 or Cos-7 cells were infected by the SA11 clone 28 strain, in which VP7 is not glycosylated, or transiently transfected with plasmids coding for NSP4-enhanced green fluorescent protein (EGFP) or NSP4. The permeability of the plasma membrane to Ca(2+) and the amount of Ca(2+) sequestered in the endoplasmic reticulum released by carbachol or ATP were measured in fura-2-loaded cells at the single-cell level under a fluorescence microscope or in cell suspensions in a fluorimeter. Total cell Ca(2+) pools were evaluated as (45)Ca(2+) uptake. Infection with SA11 clone 28 induced an increase in Ca(2+) permeability and (45)Ca(2+) uptake similar to that found with the normally glycosylated SA11 strain. These effects were inhibited by tunicamycin, indicating that inhibition of glycosylation of a viral protein other than VP7 affects the changes of Ca(2+) homeostasis induced by infection. Expression of NSP4-EGFP or NSP4 in transfected cells induced the same changes observed with rotavirus infection, whereas the expression of EGFP or EGFP-VP4 showed the behavior of uninfected and untransfected cells. Increased (45)Ca(2+) uptake was also observed in cells expressing NSP4-EGFP or NSP4, as evidenced in rotavirus infection. These results indicate that glycosylated NSP4 is primarily responsible for altering the Ca(2+) homeostasis of infected cells through an initial increase of cell membrane permeability to Ca(2+).

Domaines

Chimie organique

Dates et versions

hal-00866399 , version 1 (26-09-2013)

Identifiants

Citer

Yuleima Díaz, Maria Elena Chemello, Franshelle Peña, Olga Carolina Aristimuño, Jose Luis Zambrano, et al.. Expression of nonstructural rotavirus protein NSP4 mimics Ca2+ homeostasis changes induced by rotavirus infection in cultured cells.. Journal of Virology, 2008, 82 ((22)), pp.11331-43. ⟨10.1128/JVI.00577-08⟩. ⟨hal-00866399⟩
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