Cellular adsorption function of the sialoglycoprotein of vesicular stomatitis virus and its neuraminic acid.

摘要: Exposure of vesicular stomatitis (VS) virions to neuraminidase resulted in loss their ability agglutinate goose erythrocytes and attach L cells concomitant with hydrolysis sialic acid. These viral adsorptive functions were also destroyed by tryspsinization. Sialyl transferase resialylation vitro neuraminidase-treated VS restored hamagglutinating almost original levels. Erythrocyte cell receptors for attachment blocked fully sialylated fetuin sialoglycopeptides. Smaller glycopeptides generated extensive trypsinization less effective inhibitors hemagglutination than larger glycopeptides; neuraminic acid neuraminosyl lactose had no capacity inhibit hamagglutination or adsorption virus cells. data suggest that cellular recognize sialoglycopeptides a certain size. Neuraminidase desialylation did not significantly alter the isoelectric point virions. Cells exposed DEAE-dextran, trypsin, showed increased but desialylated cells, Chinese hamster ovary Madin-Darby bovine kidney enhanced susceptibility plaque formation virus.