Picornavirus Proteinase-Mediated Shutoff of Host Cell Translation: Direct Cleavage of a Cellular Initiation Factor

作者: Ernst Kuechler , Joachim Seipelt , Hans-Dieter Liebig , Wolfgang Sommergruber

DOI: 10.1128/9781555817916.CH24

关键词: Cleavage factorInitiation factorCleavage and polyadenylation specificity factorEIF4GBiologyProtein biosynthesisPicornavirusBiochemistryCleavage stimulation factorCleavage (embryo)

摘要: This chapter discusses the strategy used by picornaviruses belonging to genera of enteroviruses, rhinoviruses, and aphthoviruses interfere with host cell protein synthesis. First it describes mechanism initiation capped mRNA compares that uncapped mRNA. It then role viral proteinases their cellular targets. Finally focuses on effect specific proteolytic cleavage its function in There is ample evidence 2Apro proteinase responsible for eIF4G cleavage, which results inactivation cap-dependent translation leading shutoff In addition, based known sites HRV2 coxsackievirus B4 polyprotein, sequence comparisons allowed prediction three potential eIF4G. has recently been demonstrated using an vitro system newly synthesized highly efficient cleavage. The discrepancy was particularly dramatic when replication partially inhibited guanidine-HCl, 3-methyl quercetin, monensin, or nigericin. presence these inhibitors, found be essentially complete, whereas synthesis only inhibited. Furthermore, generally same factors are involved both types mRNAs.

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