Cooperative neuraminidase activity in a paramyxovirus.
Cooperative neuraminidase activity in a paramyxovirus.
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副粘病毒中的协同神经氨酸酶活性。
DOI：
10.1006/viro.1995.1564
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发表时间：
1995
期刊：
影响因子：
--
通讯作者：
Iorio,RM
中科院分区：
文献类型：
--
作者：
Mahon,PJ;Deng,R;Mirza,AM;Iorio,RM
副粘病毒具有神经氨酸酶（NA）活性，即，从膜结合和可溶性糖缀合物中裂解唾液酸的能力。这种活性与一种称为血凝素-神经氨酸酶的同源四聚体表面糖蛋白刺突有关。该结构还介导病毒与含唾液酸的受体的附着，并构成病毒的主要中和抗原。已经证明了副粘病毒之一纽卡斯尔病病毒分离株的NA活性的协同性。尽管所有已知的病毒NA蛋白都是同源寡聚的，但这是该蛋白家族中协同性的首次证明。通过逃避被认为与NA活性位点紧密结合的单克隆抗体的中和而选择的变异病毒已经失去了协同性。向非合作状态的转化与细胞受体亲和力和融合活性的增加相关。
Paramyxoviruses possess neuraminidase (NA) activity, i.e., the ability to cleave sialic acid from membrane-bound and soluble glycoconjugates. The activity is associated with a homotetrameric, surface glycoprotein spike, called the hemagglutinin-neuraminidase. This structure also mediates viral attachment to sialic acid-containing receptors and constitutes the major neutralizing antigen for the virus. Cooperativity has been demonstrated for the NA activity of an isolate of one of the paramyxoviruses, Newcastle disease virus. Although all known viral NA proteins are homooligomeric, this is the first demonstration of cooperativity in this family of proteins. A variant virus, selected by escape from neutralization by a monoclonal antibody thought to bind close to the NA active site, has lost cooperativity. Conversion to the noncooperative state correlates with increases in both avidity for cellular receptors and fusogenic activity.