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The Rotavirus Enterotoxin Nsp4 Directly Interacts With The Caveolar Structural Protein Caveolin-1, Rebecca D. Parr, Stephen M. Storey, Deanne M. Mitchell, Avery Mcintosh, Minglong Zhou, Kiran D. Mir, Judith M. Ball
The Rotavirus Enterotoxin Nsp4 Directly Interacts With The Caveolar Structural Protein Caveolin-1, Rebecca D. Parr, Stephen M. Storey, Deanne M. Mitchell, Avery Mcintosh, Minglong Zhou, Kiran D. Mir, Judith M. Ball
Faculty Publications
Rotavirus nonstructural protein 4 (NSP4) is known to function as an intracellular receptor at the endoplasmic reticulum (ER) critical to viral morphogenesis and is the first characterized viral enterotoxin. Exogenously added NSP4 induces diarrhea in rodent pups and stimulates secretory chloride currents across intestinal segments as measured in Ussing chambers. Circular dichroism studies further reveal that intact NSP4 and the enterotoxic peptide (NSP4114-135) that is located within the extended, C-terminal amphipathic helix preferentially interact with caveola-like model membranes. We now show colocalization of NSP4 and caveolin-1 in NSP4-transfected and rotavirus-infected mammalian cells in reticular structures surrounding the nucleus …