EVIDENCE FOR AN INTERACTION BETWEEN THE MEMBRANE-PROTEIN OF A PARAMYXOVIRUS AND ACTIN
EVIDENCE FOR AN INTERACTION BETWEEN THE MEMBRANE-PROTEIN OF A PARAMYXOVIRUS AND ACTIN
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DOI：
10.1128/jvi.42.3.963-968.1982
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发表时间：
1982-01-01
影响因子：
5.4
通讯作者：
TYRRELL, DLJ
中科院分区：
文献类型：
--
作者：
GIUFFRE, RM;TOVELL, DR;TYRRELL, DLJ
通过3种不同的技术获得了纽卡斯尔病病毒和仙台病毒的膜（M）蛋白与兔肌肉细胞肌动蛋白相互作用的证据。连接到Sepharose 4 B的M蛋白被发现结合肌动蛋白，但不结合肌红蛋白或牛血清白蛋白，并选择性地从这3种蛋白质的混合物中除去肌动蛋白。M蛋白和F-肌动蛋白的混合物通过蔗糖梯度沉降导致M蛋白与肌动蛋白的沉降。对照蛋白，牛血清白蛋白和细胞色素c，没有沉淀与肌动蛋白。在圆二色性研究中，以1：1复合物的形式将M蛋白加入肌动蛋白导致在220 nm处负椭圆率的显著增加，这对应于α-螺旋和β-结构和无规卷曲。这表明M蛋白和肌动蛋白之间存在相互作用。肌动蛋白在许多包膜病毒中的频繁鉴定显然可以归因于肌动蛋白与M蛋白或其等价物的相互作用。
Evidence for an interaction of the membrane (M) protein of Newcastle disease and Sendai viruses with rabbit muscle cellular actin was obtained by 3 different techniques. M protein linked to Sepharose 4B was found to bind actin, but not myoglobin or bovine serum albumin, and to selectively remove actin from a mixture of these 3 proteins. Sedimentation of a mixture of M protein and F-actin through a sucrose gradient resulted in sedimentation of M protein with actin. Control proteins, bovine serum albumin and cytochrome c, did not sediment with actin. In circular dichroism studies, M protein added to actin in a 1:1 complex resulted in a significant increase in negative ellipticity at 220 nm, which corresponds to an increase in .alpha.-helix and a decrease in .beta.-structure and random coil. This is indicative of an interaction between M protein and actin. The frequent identification of cellular actin in a number of enveloped viruses apparently may be attributed to the interaction of actin and M protein or its equivalent.