The synthesis of polypeptides in influenza C virus-infected cells.
The synthesis of polypeptides in influenza C virus-infected cells.
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丙型流感病毒感染细胞中多肽的合成。
DOI：
10.1016/0042-6822(83)90121-6
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发表时间：
1983
期刊：
影响因子：
3.7
通讯作者：
M. Homma
中科院分区：
文献类型：
--
作者：
Masashi Yokota;Kiyoto Nakamura;K. Sugawara;M. Homma
研究了甲型流感病毒JJ/50株感染MDCK细胞后病毒特异性多肽的合成。除了gp88、NP和M三种主要结构蛋白外，在感染细胞中还合成了5种分子量为29,500 （C1）、27,500 （C2）、24,000 （C3）、19,000 （C4）和14,000 （C5）的多肽。在用抗病毒血清处理感染细胞裂解物后获得的病毒粒子或免疫沉淀物中均未检测到这些多肽，这表明它们不是病毒结构蛋白。在感染不同C型流感病毒株的MDCK细胞和感染C/JJ/50的不同宿主细胞中均可合成多肽C1c5。此外，观察到在高渗条件下细胞蛋白质合成大大减少，而C1c5的合成相对不受影响。这些结果表明多肽C1c5是病毒编码的而不是宿主细胞编码的。肽图谱研究表明，多肽C3、C4和c5的肽组成与M蛋白相似。感染细胞中合成的c2量不足以进行定位。然而，这种多肽在脉冲追踪实验中被发现迅速消失，这表明c2可能不是唯一的，而是与其他一种蛋白质有生物合成关系。与这些多肽相比，多肽c1显示的图谱与任何主要结构多肽都有很大的不同。因此，c1很可能是C型流感病毒的一种非结构蛋白，类似于a型和B型流感病毒的ns1蛋白。
The synthesis of virus-specific polypeptides was analyzed in MDCK cells infected with the JJ/50 strain of influenza C virus. In addition to three major structural proteins gp88, NP, and M, the synthesis of five polypeptides with molecular weights of 29,500 (C1), 27,500 (C2), 24,000 (C3), 19,000 (C4), and 14,000 (C5) was found in infected cells. None of these polypeptides were detected either in virions or in immunoprecipitates obtained after treatment of infected cell lysates with antiviral serum, suggesting that they are not viral structural proteins. Polypeptides C1C5were found to be synthesized in MDCK cells infected with different influenza C virus strains as well as in different host cell types infected with C/JJ/50. Further, it was observed that cellular protein synthesis was greatly reduced under hypertonic conditions, whereas the synthesis of C1C5was relatively unaffected. These results suggest that polypeptides C1C5are virus coded rather than host cell coded. Peptide mapping studies showed that each of polypeptides C3, C4, and C5had a peptide composition similanto the M protein. The amount of C2synthesized in infected cells was insufficient for mapping. This polypeptide was, however, found to rapidly disappear in pulse-chase experiments, suggesting that C2is probably not unique but biosynthetically related to one of the other proteins. In contrast to these polypeptides, polypeptide C1showed a map which is largely different from any major structural polypeptide. It therefore appears likely that C1is a nonstructural protein of influenza C virus similar to the NS1protein of influenza A and B viruses.