Waxham M N, Wolinsky J S
Virology. 1986 Jun;151(2):286-95. doi: 10.1016/0042-6822(86)90050-4.
A fusing variant of the nonfusing O'Take strain of mumps virus was obtained by growing virus under the selective pressure of the competitive neuraminidase inhibitor 2-deoxy-2,3-dehydro-N-acetylneuraminic acid (DANA). The variant virus, O'Take(DANA)v1, causes extensive syncytial formation in CV-1 cell cultures in contrast to the relatively noncytopathic infection caused by the O'Take virus parent. Neuraminidase assays indicate that O'Take(DANA)v1 has no detectable neuraminidase activity using either fetuin or neuraminlactose as substrate. In addition, the O'Take(DANA)v1 virus can agglutinate red blood cells but cannot elute from these cells once adsorbed. No differences were detected in the biochemical or antigenic structure of the hemagglutinin-neuraminidase (HN) proteins from O'Take virus and O'Take(DANA)v1. These results indicate that the neuraminidase enzyme of the mumps virus HN glycoprotein is involved in modulating the cell fusion cytopathology of mumps virus infections.
在竞争性神经氨酸酶抑制剂2-脱氧-2,3-脱氢-N-乙酰神经氨酸（DANA）的选择压力下培养腮腺炎病毒，从而获得了非融合性大竹株腮腺炎病毒的融合变体。与亲本大竹病毒引起的相对无细胞病变感染相比，变体病毒大竹（DANA）v1在CV-1细胞培养物中会导致广泛的合胞体形成。神经氨酸酶测定表明，以胎球蛋白或神经氨酸乳糖为底物时，大竹（DANA）v1没有可检测到的神经氨酸酶活性。此外，大竹（DANA）v1病毒可以凝集红细胞，但一旦吸附就无法从这些细胞上洗脱。在大竹病毒和大竹（DANA）v1的血凝素-神经氨酸酶（HN）蛋白的生化或抗原结构上未检测到差异。这些结果表明，腮腺炎病毒HN糖蛋白的神经氨酸酶参与调节腮腺炎病毒感染的细胞融合细胞病变。
