Lemm J A, Bergqvist A, Read C M, Rice C M
Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri 63110-1093, USA.
J Virol. 1998 Aug;72(8):6546-53. doi: 10.1128/JVI.72.8.6546-6553.1998.
Recent insights into the early events in Sindbis virus RNA replication suggest a requirement for either the P123 or P23 polyprotein, as well as mature nsP4, the RNA-dependent RNA polymerase, for initiation of minus-strand RNA synthesis. Based on this observation, we have succeeded in reconstituting an in vitro system for template-dependent initiation of SIN RNA replication. Extracts were isolated from cells infected with vaccinia virus recombinants expressing various SIN proteins and assayed by the addition of exogenous template RNAs. Extracts from cells expressing P123C>S, a protease-defective P123 polyprotein, and nsP4 synthesized a genome-length minus-sense RNA product. Replicase activity was dependent upon addition of exogenous RNA and was specific for alphavirus plus-strand RNA templates. RNA synthesis was also obtained by coexpression of nsP1, P23C>S, and nsP4. However, extracts from cells expressing nsP4 and P123, a cleavage-competent P123 polyprotein, had much less replicase activity. In addition, a P123 polyprotein containing a mutation in the nsP2 protease which increased the efficiency of processing exhibited very little, if any, replicase activity. These results provide further evidence that processing of the polyprotein inactivates the minus-strand initiation complex. Finally, RNA synthesis was detected when soluble nsP4 was added to a membrane fraction containing P123C>S, thus providing a functional assay for purification of the nsP4 RNA polymerase.
最近对辛德毕斯病毒RNA复制早期事件的深入了解表明,负链RNA合成的起始需要P123或P23多蛋白以及成熟的nsP4(RNA依赖性RNA聚合酶)。基于这一观察结果,我们成功重建了一个用于模板依赖性启动SIN RNA复制的体外系统。从感染了表达各种SIN蛋白的痘苗病毒重组体的细胞中分离提取物,并通过添加外源模板RNA进行检测。表达P123C>S(一种蛋白酶缺陷型P123多蛋白)和nsP4的细胞提取物合成了基因组长度的负义RNA产物。复制酶活性依赖于外源RNA的添加,并且对甲病毒正链RNA模板具有特异性。通过共表达nsP1、P23C>S和nsP4也能获得RNA合成。然而,表达nsP4和P123(一种具有切割活性的P123多蛋白)的细胞提取物的复制酶活性要低得多。此外,在nsP2蛋白酶中含有一个增加加工效率的突变的P123多蛋白,即使有复制酶活性也非常低。这些结果进一步证明了多蛋白的加工会使负链起始复合物失活。最后,当将可溶性nsP4添加到含有P123C>S的膜组分中时检测到了RNA合成,从而为纯化nsP4 RNA聚合酶提供了一种功能检测方法。