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Protein synthesis initiation factor modifications during viral infections: Implications for translational control
Author(s) -
Duncan Roger F.
Publication year - 1990
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150110305
Subject(s) - vesicular stomatitis virus , virus , virology , biology , vaccinia , initiation factor , picornaviridae , poliovirus , picornavirus , cell culture , rhinovirus , protein biosynthesis , poxviridae , microbiology and biotechnology , rna , ribosome , recombinant dna , biochemistry , genetics , gene
Infection of tissue culture cells with certain viruses results in the shutoff of host cell protein synthesis. We have examined virally infected cell lysates using two‐dimensional gel electrophoresis and immunoblotting to ascertain whether initiation factor protein modifications are correlated with translational repression. Moderate increases in eukaryotic initiation factor (eIF)‐2α phosphorylation are detected in reovirus‐ and adenovirus‐infected cells, as reported previously (Samuel et al. , 1984; O'Malley et al. , 1989). Neither vesicular stomatitis virus, vaccinia virus, frog virus III, rhinovirus, nor encephalomyocarditis virus caused significantly increased 2α phosphorylation. There were no reproducible, significant changes in eIF‐4A, eIF‐4B, or eIF‐2β in cells infected by any of these viruses. The cleavage of eIF‐4F subunit p220, such as has been previously demonstrated to occur in poliovirus (Etchison et al. , 1982) and rhinovirus (Etchison and Fout, 1985), was not detected in any of the other virus infections analyzed.