A recent field isolate of Sendai virus has a temperature-sensitive HN glycoprotein.
A recent field isolate of Sendai virus has a temperature-sensitive HN glycoprotein.
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最近野外分离的仙台病毒具有温度敏感的 HN 糖蛋白。
DOI：
10.1016/0042-6822(89)90285-7
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发表时间：
1989
期刊：
影响因子：
3.7
通讯作者：
Portner,A
中科院分区：
文献类型：
--
作者：
Gorman,WL;Portner,A
最近的仙台病毒现场分离株被发现具有温度敏感（ts）血凝素神经氨酸酶（HN）糖蛋白。表型表现为细胞结合丧失、复制减少以及在不允许的温度（38°）下生长后缺乏表面 HN 的病毒颗粒。神经氨酸酶活性低，并且现场分离株未能从红细胞表面的受体上去除唾液酸，表明在不允许的温度下现场分离株病毒体从红细胞中快速洗脱不是由于神经氨酸酶活性，而是由于 HN 分子中拟议的构象变化。由于野外分离株和 Enders 菌株之间的氨基酸数量差异，无法确定导致该表型的具体氨基酸。 HN 功能的热灭活和单克隆抗体抑制表明，该分离物的 HN 蛋白除此之外还是一种不稳定的分子。
A recent field isolate of Sendai virus was found to have a temperature-sensitive (ts) hemagglutinin-neuraminidase (HN) glycoprotein. Thetsphenotype was manifested as a loss of cell binding, reduced replication, and virions that were lacking surface HN after growth at the nonpermissive temperature (38°). Low neuraminidase activity and failure of the field isolate to remove sialic acid from receptors on the surface of erythrocytes indicated that rapid elution of the field isolate virions from erythrocytes at the nonpermissive temperature was not due to neuraminidase activity but to a proposed conformational change in the HN molecule. The specific amino acids responsible for the is phenotype could not be determined due to the number of amino acid differences between the field isolate and Enders strain. Heat inactivation and monoclonal antibody inhibition of HN functions indicated that the HN protein of this isolate was, in addition tots, an unstable molecule.