Tryptic peptide analysis of outer capsid polypeptides of mammalian reovirus serotypes 1, 2, and 3.
We studied the structural relationships among the outer capsid polypeptides of prototype strains of mammalian reovirus serotypes 1, 2, and 3 by tryptic peptide mapping. The micron1C polypeptide showed an extraordinary degree of conservation of its methionine-containing tryptic peptides. In contrast, the most abundant viral polypeptide, sigma 3, contained both conserved and unique methionine-containing tryptic peptides. The viral type-specific antigen, the sigma 1 polypeptide, contained both conserved and unique methionine- and tyrosine-containing tryptic peptides. These results suggested that the mammalian reovirus genome segments encoding each of the viral outer capsid polypeptides were derived from common ancestral segments which have diverged to different degrees.
D000956:Antigens, Viral / Q000032:analysis*; D002213:Capsid / Q000032:analysis* / Q000302:isolation & purification; D006389:Hemagglutinins, Viral / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D012087:Reoviridae / Q000032:analysis* / Q000276:immunology; D014357:Trypsin; D014764:Viral Proteins / Q000032:analysis*
D000956:Antigens, Viral; D006389:Hemagglutinins, Viral; D010446:Peptide Fragments; D014764:Viral Proteins; D014357:Trypsin