AGGREGATION OF VSV M-PROTEIN IS REVERSIBLE AND MEDIATED BY NUCLEATION SITES - IMPLICATIONS FOR VIRAL ASSEMBLY
AGGREGATION OF VSV M-PROTEIN IS REVERSIBLE AND MEDIATED BY NUCLEATION SITES - IMPLICATIONS FOR VIRAL ASSEMBLY
复制标题
DOI：
10.1016/s0042-6822(95)80016-6
复制
发表时间：
1995-01-10
期刊：
影响因子：
3.7
通讯作者：
RUIGROK, RWH
中科院分区：
文献类型：
--
作者：
GAUDIN, Y;BARGE, A;RUIGROK, RWH
已报道纯化的VSV M蛋白在低NaCl浓度下聚集。利用光散射，分析离心，和电子显微镜（EM），我们已经研究了这一现象。我们的研究结果表明，M蛋白的自聚集可以通过增加盐浓度来逆转。低于250 mM NaCl时，聚集体和单体M蛋白之间存在平衡。最重要的是，我们证明，聚集只发生在成核网站的存在下，这些网站是敏感的胰蛋白酶。我们已经发现了条件下，这些成核位点可以被消除，之后M仍然可溶，即使在低盐浓度。最后，使用EM，我们表明，纯化的M蛋白的聚集体与先前描述的内部“雪茄”周围的核衣壳包裹有共同的结构方面。这些新的结果有助于解释为什么M在被感染细胞的细胞质中是一种可溶性蛋白质，直到它被整合到出芽的病毒体中。(C)出版社：Academic Press
Purified M protein of VSV has been reported to aggregate at low NaCl concentration. Using light scattering, analytical centrifugation, and electron microscopy (EM), we have studied this phenomenon. Our results demonstrate that self aggregation of M protein can be reversed by increasing the salt concentration. Below 250 mM NaCl, there is an equilibrium between aggregates and monomeric M protein. Most importantly, we demonstrate that aggregation only occurs in the presence of nucleation sites and that these sites are sensitive to trypsin. We have found conditions under which these nucleation sites can be eliminated, after which M remains soluble even at low salt concentration. Finally, using EM, we show that the aggregates of purified M protein share common structural aspects with the previously described internal ''cigar'' around which the nucleocapsid is wrapped. These new results help to explain why M is a soluble protein in the cytoplasm of the infected cell just up to the moment that it is integrated into the budding virion. (C) 1995 Academic Press, Inc.