A thermosensitive mutant of HRV2 2A proteinase: evidence for direct cleavage of eIF4GI and eIF4GII

FEBS Letters

Kuechler, Ernst²  Gradi, Alessandra¹  Seipelt, Joachim²  Liebig, Hans-Dieter²  Vassilieva, Elena² 

[1] Department of Biochemistry and McGill Cancer Center, McGill University, Montreal, QC, Canada H3G 1Y6;Institute of Medical Biochemistry, Division of Biochemistry, University of Vienna, Dr. Bohrgasse 9/3, 1030 Vienna, Austria

关键词: Human rhinovirus;    Host cell shut-off;    Viral proteinase;    eIF4G cleavage;    eIF;    eukaryotic initiation factor;    HRV2;    human rhinovirus serotype 2;    2Apro;    2A proteinase;    pNA;    para-nitroanilide;    eIF4Gase;    cellular eIF4GI cleavage activity;    IRES;    internal ribosomal entry site;   

DOI  :  10.1016/S0014-5793(02)02933-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Infection of mammalian cells with picornaviruses like entero-, rhino-, and aphthoviruses leads to an inhibition of cap-dependent cellular protein synthesis by the cleavage of both translation initiation factors, eIF4GI and eIF4GII. In entero- and rhinovirus infection this cleavage process is mediated by the viral 2A proteinase (2A^pro). In order to discriminate between a direct mode of eIF4G cleavage and an indirect cleavage via activation of a cellular proteinase, a thermosensitive 2A^pro mutant (ts-2A^pro) of human rhinovirus 2 was employed. Temperature shift experiments of cytoplasmic HeLa cell extracts incubated with ts-2A^pro strongly support a direct mode of cleavage of eIF4GI and eIF4GII by the viral 2A^pro.

【 授权许可】

Unknown