Cleavage of translation initiation factor 4AI (eIF4AI) but not eIF4AII by foot‐and‐mouth disease virus 3C protease: identification of the eIF4AI cleavage site

FEBS Letters

Belsham, Graham J.¹  Ross-Smith, Natalie¹  Li, Wei²  Proud, Christopher G.² 

[1] BBSRC Institute for Animal Health, Pirbright, Woking, Surrey GU24 ONF, UK;School of Life Sciences, MSI/WTB Complex, University of Dundee, Dundee DD1 5EH, UK

关键词: Picornavirus;    Translation initiation factor eIF4A;    Protein synthesis;    3C protease;    Foot-and-mouth disease virus;    FMDV;    foot-and-mouth disease virus;    IRES;    internal ribosome entry site;    PV;    poliovirus;    EMCV;    encephalomyocarditis virus;    IPTG;    isopropyl β-D-thiogalactoside;    PCR;    polymerase chain reaction;   

DOI  :  10.1016/S0014-5793(01)02885-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The translation initiation factor eIF4A is cleaved within mammalian cells infected by foot-and-mouth disease virus (FMDV). The FMDV 3C protease cleaves eIF4AI (between residues E143 and V144), but not the closely related eIF4AII. Modification of eIF4AI, to produce a sequence identical to eIF4AII around the cleavage site, blocked proteolysis. Alignment of mammalian eIF4AI onto the three-dimensional structure of yeast eIF4A located the scissile bond within an exposed, flexible portion of the molecule. The N- and C-terminal cleavage products of eIF4AI generated by FMDV 3C dissociate. Cleavage of eIF4AI by FMDV 3C is thus expected to inactivate it.

【 授权许可】

Unknown