Mikheeva A V, Leneva I A, Ghendon Y Z
Virus Res. 1985 Nov;3(4):353-65. doi: 10.1016/0168-1702(85)90435-6.
The ability of the fowl plague virus (FPV) M protein to form a complex with FPV RNP and to inhibit the RNP transcriptase activity in vitro depended on NaCl concentration and did not depend on the concentration of nonionic detergents. The results obtained indicate that the M protein-RNP links formed were of an electrostatic rather than a hydrophobic nature. As demonstrated using individual RNP components, vRNA and RNA-free protein structures, M protein formed complexes only with vRNA, and the complex formation was salt-dependent. Analysis of products formed in the in vitro system containing RNP of FPV in the presence of the M protein showed impairment in the transcription of all RNA segments. The degree of inhibition correlated with the size of a segment, transcription of high molecular weight RNA segments being inhibited significantly more than that of low molecular weight RNA segments.
禽瘟病毒（FPV）M蛋白与FPV核糖核蛋白（RNP）形成复合物并在体外抑制RNP转录酶活性的能力取决于氯化钠浓度，而不取决于非离子去污剂的浓度。所得结果表明，形成的M蛋白-RNP连接是静电性质而非疏水性质。正如使用单个RNP组分、病毒RNA（vRNA）和无RNA的蛋白质结构所证明的那样，M蛋白仅与vRNA形成复合物，且复合物的形成依赖于盐。在M蛋白存在的情况下，对含有FPV RNP的体外系统中形成的产物进行分析，结果显示所有RNA片段的转录均受到损害。抑制程度与片段大小相关，高分子量RNA片段的转录受到的抑制明显大于低分子量RNA片段。
