NSP4 Enterotoxin of Rotavirus Induces Paracellular Leakage in Polarized Epithelial Cells
AUTOR(ES)
Tafazoli, Farideh
FONTE
American Society for Microbiology
RESUMO
The nonstructural NSP4 protein of rotavirus has been described as the first viral enterotoxin. In this study we have examined the effect of NSP4 on polarized epithelial cells (MDCK-1) grown on permeable filters. Apical but not basolateral administration of NSP4 was found to cause a reduction in the transepithelial electrical resistance, redistribution of filamentous actin, and an increase in paracellular passage of fluorescein isothiocyanate-dextran. Significant effects on transepithelial electrical resistance were noted after a 20- to 30-h incubation with 1 nmol of NSP4. Most surprisingly, the epithelium recovered its original integrity and electrical resistance upon removal of NSP4. Preincubation of nonconfluent MDCK-1 cells with NSP4 prevented not only development of a permeability barrier but also lateral targeting of the tight-junction-associated Zonula Occludens-1 (ZO-1) protein. Taken together, these data indicate new and specific effects of NSP4 on tight-junction biogenesis and show a novel effect of NSP4 on polarized epithelia.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=114059Documentos Relacionados
- A Functional NSP4 Enterotoxin Peptide Secreted from Rotavirus-Infected Cells
- Rotavirus nonstructural glycoprotein NSP4 alters plasma membrane permeability in mammalian cells.
- The Molecular Chaperone Calnexin Interacts with the NSP4 Enterotoxin of Rotavirus In Vivo and In Vitro
- Rotavirus Enterotoxin NSP4 Binds to the Extracellular Matrix Proteins Laminin-β3 and Fibronectin
- Diarrhea-Inducing Activity of Avian Rotavirus NSP4 Glycoproteins, Which Differ Greatly from Mammalian Rotavirus NSP4 Glycoproteins in Deduced Amino Acid Sequence, in Suckling Mice