Amino acid substitutions in a conserved region in the stalk of the Newcastle disease virus HN glycoprotein spike impair its neuraminidase activity in the globular domain.
Amino acid substitutions in a conserved region in the stalk of the Newcastle disease virus HN glycoprotein spike impair its neuraminidase activity in the globular domain.
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DOI：
10.1099/0022-1317-80-3-749
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发表时间：
1999-03
期刊：
影响因子：
--
通讯作者：
Zhiyu Wang;R. M. Iorio
中科院分区：
文献类型：
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作者：
Zhiyu Wang;R. M. Iorio
副粘病毒血凝素神经氨酸酶 (HN) 糖蛋白刺突的胞外域可分为两个区域：近膜、茎状结构和末端球状结构域。后者包含蛋白质的所有抗体识别位点，以及其受体识别和神经氨酸酶（NA）活性位点。蛋白质的这两种活性可以通过单克隆抗体功能抑制研究和球状结构域的突变来区分。在此，我们发现新城疫病毒 HN 蛋白柄中几个保守残基的突变显着降低了其 NA 活性，但对受体识别没有显着影响。因此，远离球状结构域中的 NA 活性位点的茎中的突变也可以将附着和 NA 分开。这些结果增加了越来越多的证据表明该蛋白质的 NA 活性依赖于完整的茎结构。
The ectodomain of the paramyxovirus haemagglutinin-neuraminidase (HN) glycoprotein spike can be divided into two regions: a membrane-proximal, stalk-like structure and a terminal globular domain. The latter contains all the antibody recognition sites of the protein, as well as its receptor recognition and neuraminidase (NA) active sites. These two activities of the protein can be separated by monoclonal antibody functional inhibition studies and mutations in the globular domain. Herein, we show that mutation of several conserved residues in the stalk of the Newcastle disease virus HN protein markedly decrease its NA activity without a significant effect on receptor recognition. Thus, mutations in the stalk, distant from the NA active site in the globular domain, can also separate attachment and NA. These results add to an increasing body of evidence that the NA activity of this protein is dependent on an intact stalk structure.