Proteolysis of Monomeric Recombinant Rotavirus VP4 Yields an Oligomeric VP5* Core

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

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 nu...

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Generation of recombinant rotavirus with an antigenic mosaic of cross-reactive neutralization epitopes on VP4.

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ژورنال

عنوان ژورنال: Journal of Virology

سال: 2001

ISSN: 0022-538X,1098-5514

DOI: 10.1128/jvi.75.16.7339-7350.2001