Double-stranded RNA-dependent protein kinase and 2-5A system are both activated in interferon-treated, encephalomyocarditis virus-infected HeLa cells.
Activation of the interferon-inducible, double-stranded RNA-dependent protein kinase was monitored in monolayer cultures of control and interferon-treated HeLa cells infected with encephalomyocarditis virus. The extent of phosphorylation in the intact cell of the alpha-subunit of eucaryotic protein synthesis initiation factor eIF2 by the kinase was determined for the first time in this type of system, using a two-dimensional immunoblot technique. Virus protein synthesis and the kinetics of activation of the ppp(A2'p)nA (n greater than or equal to 2) system were analyzed in parallel. Enhanced phosphorylation of eIF2-alpha was obvious at 9 h and increased by 12 h postinfection. ppp(A2'p)nA and ppp(A2'p)nA-mediated rRNA cleavage were observed from 6 h. No viral protein synthesis was detected in cells in which a general inhibition of protein synthesis developed with time. It can be concluded that both the kinase and ppp(A2'p)nA system are active in interferon-treated, encephalomyocarditis virus-infected HeLa cells.
Rice
A P
AP
Duncan
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R
Hershey
J W
JW
Kerr
I M
IM
D004686:Encephalomyocarditis virus / Q000378:metabolism*; D004789:Enzyme Activation; D006367:HeLa Cells; D006801:Humans; D007372:Interferons / Q000494:pharmacology*; D009713:Nucleotidyltransferases / Q000032:analysis*; D011062:Polynucleotide Adenylyltransferase / Q000032:analysis*; D011494:Protein Kinases / Q000032:analysis*; D012330:RNA, Double-Stranded / Q000494:pharmacology*; D014764:Viral Proteins / Q000096:biosynthesis
D012330:RNA, Double-Stranded; D014764:Viral Proteins; D007372:Interferons; D011494:Protein Kinases; D009713:Nucleotidyltransferases; D011062:Polynucleotide Adenylyltransferase