This basic science study demonstrates that human rhinovirus 2 2A proteinase directly cleaves translation initiation factors eIF4GI and eIF4GII, rather than acting indirectly via cellular proteinases.
Supports direct 2A(pro) cleavage in rhinovirus models; leaves open human translation and therapeutic relevance.
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).
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Liebig et al. (2002) studied this question.
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