Proteolytic enhancement of rotavirus infectivity: molecular mechanisms.

@article{Estes1981ProteolyticEO,
  title={Proteolytic enhancement of rotavirus infectivity: molecular mechanisms.},
  author={Mary K. Estes and David Y Graham and B. B. Mason},
  journal={Journal of virology},
  year={1981},
  volume={39 3},
  pages={
          879-88
        }
}
The polypeptide compositions of single-shelled and double-shelled simian rotavirus particles were modified by exposure to proteolytic enzymes. Specifically, a major outer capsid polypeptide (VP3) having a molecular weight of 88,000 in double-shelled particles was cleaved by trypsin to yield two polypeptides, VP5* and VP8* (molecular weights, 60,000 and 28,000, respectively). The cleavage of VP3 by enzymes that enhanced infectivity (trypsin, elastase, and pancreatin) yielded different products… CONTINUE READING
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