Protein synthesis initiation factor modifications during viral infections: implications for translational control.
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)-2 alpha 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 2 alpha phosphorylation. There were no reproducible, significant changes in eIF-4A, eIF-4B, or eIF-2 beta 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.
Duncan
R F
RF
School of Pharmacy, University of Southern California, Los Angeles 90033.
D000256:Adenoviridae / Q000502:physiology; D002477:Cells / Q000378:metabolism / Q000382:microbiology*; D002478:Cells, Cultured; D015180:Electrophoresis, Gel, Two-Dimensional; D015151:Immunoblotting; D010448:Peptide Initiation Factors / Q000378:metabolism; D010766:Phosphorylation; D014176:Protein Biosynthesis; D012087:Reoviridae / Q000502:physiology; D018406:Virus Physiological Phenomena
D010448:Peptide Initiation Factors