Structural Analysis Of The Rotavirus Hemagglutinin Following Proteolysis Shaw, A. L., Rothnagel, R., Chen, D., Ramig, R. F., Estes, M. K., Prasad, B. V. V. Department of Biochemistry and Division of Molecular Virology, Baylor College of Medicine Rotavirus is a significant cause of infantile gastroenteritis worldwide. The structural change in the VP4 spike appears to depend on the stage at which trypsinization occurs.
Significant change occurs when trypsinization follows progeny release in vivo .
However, a novel VP4 structure indicating gross molecular movement, is observed when trypsinized progeny are treated with trypsin. Similar structural changes in the VP4 spike of another rotavirus species, SA11, are observed, confirming that our observations reflect a global mechanism for the structural basis of trypsin-enhanced infectivity. All together, our results suggest that a functional domain, necessary for cell entry and productive infection, is exposed due to conformational changes of the VP4 spike following trypsin cleavage.