Abstract
The human group B rotavirus is a causative agent of severe adult diarrhea. In this study, we analyzed the NSP4 structure of a group B rotavirus strain, CAL-1, and determined whether enterotoxin activity was present in CAL-1 NSP4. CAL-1 NSP4 was comprised of 219 amino acids which was longer than group A and C rotavirus NSP4, and the primary structures of their sequences differed considerably. However, CAL-1 NSP4 had an enterotoxin-like sequence (residues 106-127) that was only 27% identical to the enterotoxin region of NSP4 of KUN (a group A rotavirus strain) at residues 114-135. Interestingly, both of the synthetic peptides, one (residues 99-128) containing the enterotoxin-like sequence and the other (residues 191-219) containing 29 C-terminal amino acids of CAL-1 NSP4, induced diarrhea in 5.5-day-old mice, but not in 17.5-day-old mice, when administered parenterally. Thus, rotavirus "enterotoxin" sequences could be considerably divergent.
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