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A thermosensitive mutant of HRV2 2A proteinase: evidence for direct cleavage of eIF4GI and eIF4GII
Author(s) -
Liebig Hans-Dieter,
Seipelt Joachim,
Vassilieva Elena,
Gradi Alessandra,
Kuechler Ernst
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02933-2
Subject(s) - cleavage (geology) , eif4g , mutant , rhinovirus , chemistry , hela , cleavage stimulation factor , microbiology and biotechnology , biology , virology , cleavage factor , virus , in vitro , biochemistry , translation (biology) , messenger rna , gene , paleontology , fracture (geology)
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 .