Giuffre R M, Tovell D R, Kay C M, Tyrrell D L
J Virol. 1982 Jun;42(3):963-8. doi: 10.1128/JVI.42.3.963-968.1982.
Evidence for an interaction of the membrane (M) protein of Newcastle disease and Sendai viruses with cellular actin was obtained by three 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 three 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. It is possible that the frequent identification of cellular actin in a number of enveloped viruses may be attributed to the interaction of actin and M protein or its equivalent.
通过三种不同技术获得了新城疫病毒和仙台病毒的膜（M）蛋白与细胞肌动蛋白相互作用的证据。连接到琼脂糖4B上的M蛋白被发现能结合肌动蛋白，但不结合肌红蛋白或牛血清白蛋白，并且能从这三种蛋白的混合物中选择性地去除肌动蛋白。M蛋白和F-肌动蛋白的混合物通过蔗糖梯度沉降，导致M蛋白与肌动蛋白一起沉降。对照蛋白牛血清白蛋白和细胞色素c不与肌动蛋白一起沉降。在圆二色性研究中，以1:1复合物形式添加到肌动蛋白中的M蛋白导致在220nm处负椭圆率显著增加，这对应于α-螺旋增加，β-结构和无规卷曲减少。这表明M蛋白与肌动蛋白之间存在相互作用。在许多包膜病毒中频繁鉴定到细胞肌动蛋白，可能归因于肌动蛋白与M蛋白或其等效物之间的相互作用。
