Mapping the Interaction Domain of NSP4 With the Caveolin Chaperon Complex Components

Rotaviruses are a leading cause of gastroenteritis in children worldwide. Rotavirus non-structural protein 4 (NSP4), a protein coded for by the viral genome, is known to play a key role in viral production and has been found to be able to escape the cell without being part of the virus. Being highly communicable, rotaviruses are transmitted fecal-orally, and in food and water. Symptoms accompanying disease include fever, vomiting and diarrhea, resulting in dehydration and the loss of electrolytes in the absence of hydrating fluids. Non-structural protein 4 (NSP4), encoded by the viral genome segment 10, is known to contribute to this pathogenicity as a viral enterotoxin, causing secretory diarrhea in the absence of histological alterations. NSP4 has recently been shown to traffic from the ER to the plasma membrane (PM) and to subsequently exit the cell. Discerning how NSP4 traffics to the PM and released is a focus of the laboratory. To date, several domains have been mapped to the C-terminus of NSP4. This study has begun to elucidate the transport domain responsible for transport of NSP4 to the PM. Using this knowledge, more effective therapeutics and vaccines can be developed