Selective blockage of initiation of host protein synthesis in RNA-virus-infected cells.
Poliovirus mRNA and mRNA transcribed from vesicular stomatitis virus and reovirus genomes efficiently direct protein synthesis in vivo under experimental conditions where the initiation of host protein synthesis is selectively blocked. The selective blockage of host peptide chain initiation after exposure to hypertonic medium indicates that the translation of viral mRNA is more efficiently initiated than is the translation of host mRNA. It further suggests that virus directed suppression of host protein synthesis could proceed by a mechanism involving a nonspecific decrease in the rate of peptide chain initiation. Exposure of infected cells to hypertonic medium provides a unique tool with which to study early events in the infectious cycle by permitting the efficient unmasking of virus-specific poly-peptide synthesis.
D000818:Animals; D002460:Cell Line; D006224:Cricetinae; D004591:Electrophoresis, Polyacrylamide Gel; D006367:HeLa Cells / Q000378:metabolism; D007668:Kidney; D007930:Leucine / Q000378:metabolism; D008715:Methionine / Q000378:metabolism; D010442:Peptide Chain Initiation, Translational; D017955:Poliovirus / Q000378:metabolism*; D014176:Protein Biosynthesis; D012313:RNA / Q000096:biosynthesis; D012333:RNA, Messenger / Q000378:metabolism*; D012367:RNA, Viral / Q000378:metabolism*; D013997:Time Factors; D014529:Uridine / Q000378:metabolism; D014721:Vesicular stomatitis Indiana virus / Q000378:metabolism*
D012333:RNA, Messenger; D012367:RNA, Viral; D012313:RNA; D008715:Methionine; D007930:Leucine; D014529:Uridine