The major surface glycoprotein of Simian Rotavirus (SA11) contains distinct epitopes

The polypeptide specificities on monoclonal antibodies previously derived against the SA11 simian, NIC bovine, and Wa human strains of rotavirus were determined by radio-immunoprecipitation of infected cell lysates. All the monoclonal antibodies derived using NIC and Wa were found to be directed aga...

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Veröffentlicht in:Virology (New York, N.Y.) N.Y.), 1984-04, Vol.134 (2), p.318-327
Hauptverfasser: Sonza, Secondo, Breschkin, Alan M., Holmes, Ian H.
Format: Artikel
Sprache:eng
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Zusammenfassung:The polypeptide specificities on monoclonal antibodies previously derived against the SA11 simian, NIC bovine, and Wa human strains of rotavirus were determined by radio-immunoprecipitation of infected cell lysates. All the monoclonal antibodies derived using NIC and Wa were found to be directed against the major component of the inner capsid, while most of the SAll monoclonas were directed against the major outer capsid glycoprotein. When several SAll glycoprotein-specific monoclonal antibodies were used in competitive binding studies, four distinct epitopes, which correlated with the functional activities of the antibodies, were defined. One epitope appeared most critical for virus neutralization, another was involved to a lesser extent, and the remaining two epitopes seemed to have no role. A possible topographical arrangement of these epitopes is suggested.
ISSN:0042-6822
1096-0341
DOI:10.1016/0042-6822(84)90300-3