Schloemer R H, Wagner R R
J Virol. 1974 Aug;14(2):270-81. doi: 10.1128/JVI.14.2.270-281.1974.
Neuraminidase free of proteolytic activity substantially reduced the infectivity of vesicular stomatitis (VS) virus but less effectively than trypsin. The only sugar residue hydrolyzed by neuraminidase was N-acetyl neuraminic acid, approximately 89% of which was liberated from virion glycoprotein and the rest from virion glycolipid. Desialylation of virion glycoprotein but not of glycolipid resulted in progressive loss of infectivity. Sialyl transferase prepared and partially purified from BHK-21 cells catalyzed resialylation by CMP-[(14)C]sialic acid of the glycoprotein of neuraminidase-treated VS virions and supersialylation of unhydrolyzed VS viral glycoprotein. Resialylation of desialylated VS virions resulted in substantial (26-fold) restoration of their infectivity. We conclude that terminal neuraminic acids of VS viral sialoglycoprotein play an important role in initiation of infection with this virus.
无蛋白水解活性的神经氨酸酶可大幅降低水疱性口炎（VS）病毒的感染性，但效果不如胰蛋白酶。神经氨酸酶水解的唯一糖残基是N - 乙酰神经氨酸，其中约89%从病毒粒子糖蛋白释放，其余从病毒粒子糖脂释放。病毒粒子糖蛋白而非糖脂的去唾液酸化导致感染性逐渐丧失。从BHK - 21细胞制备并部分纯化的唾液酸转移酶催化经神经氨酸酶处理的VS病毒粒子糖蛋白由CMP - [（14）C]唾液酸进行再唾液酸化，以及未水解的VS病毒糖蛋白的超唾液酸化。去唾液酸化的VS病毒粒子的再唾液酸化导致其感染性大幅（26倍）恢复。我们得出结论，VS病毒唾液酸糖蛋白的末端神经氨酸在该病毒感染的起始中起重要作用。
