The HN glycoprotein of Sendai virus: analysis of site(s) involved in hemagglutinating and neuraminidase activities.
The HN glycoprotein of Sendai virus: analysis of site(s) involved in hemagglutinating and neuraminidase activities.
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仙台病毒的 HN 糖蛋白：参与血凝和神经氨酸酶活性的位点分析。
DOI：
10.1016/0042-6822(81)90118-5
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发表时间：
1981
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：
Portner,A
副粘病毒的 HN 糖蛋白负责与红细胞和宿主细胞受体的附着以及神经氨酸酶活性。本报告中提出的几条证据与以下概念一致：副粘病毒、仙台病毒和新城疫病毒的 HN 糖蛋白的血凝和神经氨酸酶活性涉及该分子的两个不同位点。首先，仙台病毒突变体在 38° 下对血凝和附着于宿主细胞的温度敏感（ts），但对神经氨酸酶活性不敏感，表明不同的位点可能参与这些活动。其次，使用 HN 蛋白的单克隆抗体来选择抗原变体。然后使变体与抗体反应并测试神经氨酸酶和血凝活性。结果表明，一些变体的血凝作用受到抑制，但神经氨酸酶活性不受抑制。最后，N-乙酰神经氨酸的类似物（2-脱氧-2,3-脱氢-N-乙酰神经氨酸）在10−4M时抑制仙台病毒和新城疫病毒的神经氨酸酶活性>95%。然而，在 10−2 至 10−4M 范围内，该类似物不会抑制任何一种病毒的血凝作用，尽管它抑制了 NDV 和仙台病毒从凝集红细胞中的洗脱。后一个观察结果表明，该类似物不会抑制病毒颗粒与红细胞受体的结合，但会抑制负责洗脱过程的神经氨酸酶活性。总而言之，这些数据与 HN 分子上的独立位点可能参与宿主细胞附着和神经氨酸酶活性的概念是一致的。然而，不排除单个活性位点可能参与这两种活动的可能性。
The HN glycoprotein of paramyxoviruses is responsible for attachment to red cell and host cell receptors and for neuraminidase activity. Several lines of evidence presented in this report are consistent with the concept that hemagglutinating and neuraminidase activities of the HN glycoprotein of the paramyxoviruses, Sendai and Newcastle disease virus, involve two distinct sites of the molecule. First, a Sendai virus mutant, temperature-sensitive (ts) at 38° for hemagglutination and attachment to host cells was nottsfor neuraminidase activity, indicating that different sites may be involved in these activities. Second, monoclonal antibodies to the HN protein were used to select antigenic variants. The variants were then reacted with antibody and tested for neuraminidase and hemagglutinating activities. The results showed that some variants were inhibited in hemagglutination but not in neuraminidase activity. Finally, an analog ofN-acetylneuraminic acid (2-deoxy-2,3-dehydro-N-acetlyneuraminic acid) inhibited neuraminidase activity of Sendai virus and Newcastle disease virus by >95% at 10−4M. However, at 10−2to 10−4M, the analog did not inhibit hemagglutination by either virus, although it inhibited the elution of NDV and Sendai virus from agglutinated red cells. This latter observation shows that the analog does not inhibit virion binding to red cell receptors, but does inhibit the neuraminidase activity responsible for the elution process. Taken together, these data are consistent with the concept that independent sites on the HN molecule may be involved in attachment to host cells and neuraminidase activity. However, the possibility that a single active site may be involved in both activities has not been excluded.