Heterogeneity in the structural glycoprotein (VP7) of simian rotavirus SA11

doi:10.1016/0042-6822(82)90372-5

Virology

Volume 122, Issue 1, 15 October 1982, Pages 8-14

https://doi.org/10.1016/0042-6822(82)90372-5 Get rights and content

Abstract

The polypeptides of cells infected with a series of plaque isolates of the simian rotavirus SA11 were analyzed by SDS-PAGE. Altered electrophoretic migration of the major outer capsid glycoprotein (VP7) was found with independent virus stocks exhibiting gene products of VP7 ranging in apparent molecular weight from 35.5K to 38K. Similar differences in electrophoretic migration in the polypeptide precursor of the glycoprotein (pVP7) suggested that the heterogeneity resulted from mutations in the gene encoding the glycoprotein. The glycoprotein phenotype was stable on passage; the phenotypes were unchanged for 10 passages at high and low multiplicity. The biologic consequences of heterogeneity in the polypeptide are discussed.

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Heterogeneity in the structural glycoprotein (VP7) of simian rotavirus SA11

Abstract

J. Biol. Chem.

FEBS Lett. 8

Virology

Virology

Virology

Virology

Virology

Gene protein products of SAll simian rotavirus genome

J. Virol.

A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels

Eur. J. Biochem.

Strategy for development of respiratory and gastrointestinal tract viral vaccines in the 1980s

J. Infect. Dis.

Temperature-sensitive mutants of reovirus type 3: Evidence for aberrant pl and p2 polypeptide species

J. Virol.

Viral glycoproteins in infectious disease processes

Rev. Infect. Dis.

Identification, synthesis and modifications of simian rotavirus SAll polypeptides in infected cells

J. Virol.

Structural polypeptides of simian rotavirus SA1l and the effect of trypsin

J. Virol.