Wilson T, Lenard J
Biochemistry. 1981 Mar 3;20(5):1349-54. doi: 10.1021/bi00508a048.
We have characterized the interactions between mutant or wild-type M protein and nucleocapsids of vesicular stomatitis virus (VSV) by assaying for inhibition of in vitro transcriptase activity. The interactions are primarily electrostatic in nature: high concentrations of NaCl or poly(L-glutamic acid) reverse the inhibition. These interactions are much weaker in each of the four M protein mutants (complementation group III) tested than in wild-type VSV. Temperature-sensitive revertants were selected from each of the M protein mutants studied. The salt-dependent inhibitory profiles of all the revertants resemble that of wild-type VSV, suggesting that M-nucleocapsid interactions are integrally related to the temperature-sensitive phenotype of group III mutants. These results are discussed in relation to the accompanying paper [Reidler, J.A., Keller, P.M., Elson, E.L., & Lenard, J. (1981) Biochemistry (preceding paper in this issue)] which shows that interaction between M protein and infected cell membranes is increased in all group III mutants studied.
我们通过检测体外转录酶活性的抑制情况，对水泡性口炎病毒（VSV）的突变型或野生型M蛋白与核衣壳之间的相互作用进行了表征。这些相互作用主要是静电性质的：高浓度的NaCl或聚（L-谷氨酸）可逆转这种抑制作用。在所测试的四个M蛋白突变体（互补组III）中，每一个的这些相互作用都比野生型VSV中的弱得多。从所研究的每个M蛋白突变体中筛选出温度敏感回复体。所有回复体的盐依赖性抑制谱都与野生型VSV的相似，这表明M-核衣壳相互作用与III组突变体的温度敏感表型密切相关。将结合随附论文[Reidler, J.A., Keller, P.M., Elson, E.L., & Lenard, J. (1981) Biochemistry（本期前一篇论文）]讨论这些结果，该论文表明在所有研究的III组突变体中，M蛋白与感染细胞膜之间的相互作用都增强了。
