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脊髓灰质炎病毒感染后,帽结合蛋白复合体的p220组分的蛋白水解作用不足以完全抑制宿主细胞蛋白质合成。

Proteolysis of the p220 component of the cap-binding protein complex is not sufficient for complete inhibition of host cell protein synthesis after poliovirus infection.

作者信息

Bonneau A M, Sonenberg N

出版信息

J Virol. 1987 Apr;61(4):986-91. doi: 10.1128/JVI.61.4.986-991.1987.

Abstract

Infection of cells with poliovirus results in the complete shutoff of host protein synthesis. It is presumed that proteolysis of the p220 component of the cap-binding protein complex that is required for the translation of host mRNAs is responsible for the shutoff phenomenon. In this paper, we show that when cells are infected with poliovirus in the presence of guanidine or 3-methylquercetin, both inhibitors of poliovirus replication, complete cleavage of p220 occurs by 3.5 h postinfection. However, under these conditions only 55 to 77% of host protein synthesis is suppressed. Results obtained with extracts prepared from poliovirus-infected cells were similar to those obtained in vivo. These results suggest that complete inhibition of host protein synthesis after poliovirus infection requires at least one event in addition to proteolysis of p220. Thus, proteolysis of p220 is probably necessary but not sufficient for total suppression of host protein synthesis after poliovirus infection.

摘要

脊髓灰质炎病毒感染细胞会导致宿主蛋白质合成完全停止。据推测,宿主mRNA翻译所需的帽结合蛋白复合体的p220组分的蛋白水解是导致这种停止现象的原因。在本文中,我们表明,当细胞在存在胍或3 - 甲基槲皮素(这两种都是脊髓灰质炎病毒复制的抑制剂)的情况下被脊髓灰质炎病毒感染时,感染后3.5小时p220会完全裂解。然而,在这些条件下,只有55%至77%的宿主蛋白质合成受到抑制。从脊髓灰质炎病毒感染的细胞制备的提取物所获得的结果与体内获得的结果相似。这些结果表明,脊髓灰质炎病毒感染后宿主蛋白质合成的完全抑制除了p220的蛋白水解外还需要至少一个事件。因此,p220的蛋白水解可能是脊髓灰质炎病毒感染后完全抑制宿主蛋白质合成所必需的,但并不充分。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/12aa/254054/2b331f4eac62/jvirol00095-0051-a.jpg

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本文引用的文献

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Capped mRNAs with reduced secondary structure can function in extracts from poliovirus-infected cells.
Mol Cell Biol. 1982 Dec;2(12):1633-8. doi: 10.1128/mcb.2.12.1633-1638.1982.
5
Inactivation of cap-binding proteins accompanies the shut-off of host protein synthesis by poliovirus.
Proc Natl Acad Sci U S A. 1982 Jun;79(11):3447-51. doi: 10.1073/pnas.79.11.3447.

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