Carroll A R, Wagner R R
J Virol. 1979 Jan;29(1):134-42. doi: 10.1128/JVI.29.1.134-142.1979.
An endogenous transcriptase inhibitor active at high concentrations of vesicular stomatitis (VS) virus was present in trypsinized whole virions but was absent from ribonucleoprotein cores containing only the L, N, and NS proteins. Poly(L-glutamic acid) effectively reversed the transcriptase inhibition. Transcription under noninhibited, inhibited, and poly(L-glutamic acid)-reversed conditions did not appear to greatly affect the nature of the RNA transcription product. The VS virion matrix (M) protein was purified to greater than 98% homogeneity and was found to have an isoelectric point of approximately 9.0. Purified M protein inhibited transcription by ribonucleoprotein cores, an effect that was partially reversed by poly(L-glutamic acid). Two group III temperature-sensitive (ts) mutants of VS virus (tsO23 and ts G31) with lesions in the M protein exhibited little or no endogenous inhibitor activity compared with two wild-type strains and a group V mutant (tsO45) with a lesion in the G protein. The data presented strongly suggest that the virion M protein is responsible for the endogenous inhibition of in vitro RNA synthesis seen at high concentrations of VS virus.
在经胰蛋白酶处理的完整病毒粒子中存在一种在高浓度水疱性口炎病毒（VS）时具有活性的内源性转录酶抑制剂，但仅含有L、N和NS蛋白的核糖核蛋白核心中不存在该抑制剂。聚（L-谷氨酸）可有效逆转转录酶抑制作用。在未受抑制、受抑制以及聚（L-谷氨酸）逆转条件下的转录似乎并未对RNA转录产物的性质产生很大影响。VS病毒粒子基质（M）蛋白被纯化至纯度大于98%，并发现其等电点约为9.0。纯化的M蛋白抑制核糖核蛋白核心的转录，聚（L-谷氨酸）可部分逆转这一效应。与两个野生型毒株以及一个G蛋白有损伤的V组突变体（tsO45）相比，两个M蛋白有损伤的VS病毒III组温度敏感（ts）突变体（tsO23和ts G31）几乎没有或没有内源性抑制剂活性。所呈现的数据有力地表明，病毒粒子M蛋白是高浓度VS病毒时所见的体外RNA合成内源性抑制的原因。
