Mikhejeva A V, Ghendon Y Z
J Gen Virol. 1983 Feb;64 (Pt 2):305-12. doi: 10.1099/0022-1317-64-2-305.
The effect of proteins soluble in acidic chloroform-methanol (ACMS proteins) on the transcriptase activity of virus ribonucleoproteins (RNPs) in vitro has been studied. Experiments with ACMS membrane (M) proteins from type A and B orthomyxoviruses, as well as from vesicular stomatitis virus, showed that inhibition of the viral RNP transcriptase activity occurred when they interacted with M proteins isolated from viruses of a different serotype, or even of a different family. The presence of ACMS proteins capable of inhibiting the transcriptase activity of orthomyxovirus RNP in vitro was also detected in human blood plasma and among proteins produced by human leukocytes. Determination of the minimum concentration of M protein inhibiting the RNP transcriptase activity, and analysis of the fowl plague virus M protein-RNP complex formed in the in vitro system, showed that the M protein was capable of inhibiting RNP transcriptase activity at a M:RNP ratio of 0.1 to 0.2:1.
研究了可溶于酸性氯仿 - 甲醇的蛋白质（ACMS蛋白质）对病毒核糖核蛋白（RNP）体外转录酶活性的影响。对甲型和乙型正粘病毒以及水疱性口炎病毒的ACMS膜（M）蛋白进行的实验表明，当它们与从不同血清型甚至不同家族的病毒中分离出的M蛋白相互作用时，病毒RNP转录酶活性会受到抑制。在人血浆和人白细胞产生的蛋白质中也检测到了能够在体外抑制正粘病毒RNP转录酶活性的ACMS蛋白质。测定抑制RNP转录酶活性的M蛋白的最低浓度，并分析体外系统中形成的禽瘟病毒M蛋白 - RNP复合物，结果表明，M蛋白能够以0.1至0.2:1的M:RNP比例抑制RNP转录酶活性。
