![]() Recent studies show silencing NSP4 in RV-infected cells results in a 75% reduction in viral progeny and the redistribution of VP6 throughout the cell ( Lopez et al., 2005). A specific interaction between the C-terminus of NSP4 and the structural viral protein, VP6, facilitates the budding of immature particles into the ER ( Au et al., 1989 Bergmann et al., 1989). During RV maturation, NSP4 functions as an intracellular receptor at the ER to bind and deliver immature double-layered progeny into the ER lumen. RV non-structural protein 4 (NSP4) has been shown to be a multifunctional protein with key roles in viral assembly, replication and pathogenesis. ![]() Rotavirus (RV) is the major etiologic agent of virally induced gastroenteritis in children and infants worldwide, contributing to 440,000 pediatric deaths annually ( Parashar et al., 2003).
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