Proteolysis of monomeric recombinant rotavirus VP4 yields an oligomeric VP5* core.

@article{Dormitzer2001ProteolysisOM,
  title={Proteolysis of monomeric recombinant rotavirus VP4 yields an oligomeric VP5* core.},
  author={Philip Ralph Dormitzer and Harry B Greenberg and Stephen C Harrison},
  journal={Journal of virology},
  year={2001},
  volume={75 16},
  pages={7339-50}
}
Rotavirus particles are activated for cell entry by trypsin cleavage of the outer capsid spike protein, VP4, into a hemagglutinin, VP8*, and a membrane penetration protein, VP5*. We have purified rhesus rotavirus VP4, expressed in baculovirus-infected insect cells. Purified VP4 is a soluble, elongated monomer, as determined by analytical ultracentrifugation. Trypsin cleaves purified VP4 at a number of sites that are protected on the virion and yields a heterogeneous group of protease-resistant… CONTINUE READING
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