Attachment of SA-11 rotavirus to erythrocyte receptors.
Treatment of human group O and sheep erythrocytes with receptor-destroying enzyme rendered them inagglutinable by simian rotavirus SA-11. The erythrocyte receptors were also removed by periodate oxidation and markedly reduced by incubation with a high concentration of trypsin, but they were not altered by infectivity-enhancing concentrations of trypsin, p-hydroxymercuribenzoate, or sodium sulfite (Na2SO3). Hemagglutinating activity of the virus particles was destroyed by periodate oxidation at 37 degrees C, p-hydroxymercuribenzoate, and a high concentration of trypsin and decreased by Na2SOa but was not altered by incubation with receptor-destroying enzyme, infectivity-enhancing concentrations of trypsin, or periodate oxidation at 4 degrees C. These results indicate that neuraminic acid-containing receptor substances are involved in the interaction of the virus with human and sheep erythrocytes, and suggest that SA-11-erythrocyte union involves carbohydrate on the surface of erythrocytes but not on the virion. Sensitivities of the SA-11 hemagglutinin to alcohols and repeated freeze-thaw cycles were also investigated.
D000818:Animals; D001665:Binding Sites; D004912:Erythrocytes / Q000276:immunology*; D005615:Freezing; D006384:Hemagglutination / Q000187:drug effects; D006385:Hemagglutination Inhibition Tests; D006801:Humans; D007700:Kinetics; D008252:Macaca fascicularis; D008253:Macaca mulatta; D010504:Periodic Acid / Q000494:pharmacology; D012087:Reoviridae; D012401:Rotavirus; D012756:Sheep; D014357:Trypsin / Q000494:pharmacology; D014734:Vibrio cholerae / Q000201:enzymology
D010504:Periodic Acid; D014357:Trypsin