PARAMYXOVIRUS PHOSPHOPROTEINS FORM HOMOTRIMERS AS DETERMINED BY AN EPITOPE DILUTION ASSAY, VIA PREDICTED COILED COILS
PARAMYXOVIRUS PHOSPHOPROTEINS FORM HOMOTRIMERS AS DETERMINED BY AN EPITOPE DILUTION ASSAY, VIA PREDICTED COILED COILS
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DOI：
10.1006/viro.1995.9946
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发表时间：
1995-12-01
期刊：
影响因子：
3.7
通讯作者：
KOLAKOFSKY, D
中科院分区：
文献类型：
--
作者：
CURRAN, J;BOECK, R;KOLAKOFSKY, D
当HA表位标记的和未标记的仙台病毒（SeV）P蛋白共表达并且产物与抗HA反应时，未标记的P蛋白也被选择，因为该蛋白被发现为寡聚体。通过共选择研究确定该寡聚体是同源三聚体，其中增加量的未标记蛋白与标记蛋白共表达，并且这些发现扩展到腮腺炎病毒，风疹病毒属的成员。负责寡聚化的SeV蛋白的区域定位于残基344-411。对数据库中的13种副粘病毒P蛋白的计算机分析显示，除了一种蛋白外，所有蛋白都被预测在该区域形成卷曲螺旋，这是整个病毒亚科中仅有的两个区域中的第一个。预测的卷曲螺旋区的麻疹病毒P蛋白，当嫁接到C-末端的正常单体的La蛋白，导致该报告蛋白的有效寡聚化。因此，这些P蛋白的预测卷曲螺旋区域似乎足以进行寡聚化。(C)出版社：Academic Press
When HA epitope-tagged and untagged Sendai Virus (SeV) P proteins are coexpressed and the products reacted with anti-HA, the untagged P protein is also selected because this protein is found as an oligomer. The oligomer was determined to be a homotrimer by coselection studies in which increasing amounts of untagged Versus tagged protein were coexpressed, and these findings were extended to mumps virus, a member of the rubulavirus genus. The region of the SeV protein responsible for the oligomerization was localized to residues 344-411. Computer analysis of the 13 Paramyxovirus P proteins in the database revealed that all but one are predicted to form coiled coils in this region, the first of only two regions that can be aligned throughout the entire virus subfamily. The predicted coiled-coil region of the measles virus P protein, when grafted onto the C-terminus of the normally monomeric La protein, led to the efficient oligomerization of this reporter protein. The predicted coiled-coil region of these P proteins thus appears to be sufficient for oligomerization. (C) 1995 Academic Press, Inc.