Efficient cleavage of p220 by poliovirus 2Apro expression in mammalian cells: effects on vaccinia virus.
Poliovirus protease 2A cleaves p220, a component of initiation factor eIF-4F. Polyclonal antibodies that recognize p220 and the cleaved products from different species have been raised. Transfection of several cell lines with poliovirus 2Apro cloned in different plasmids leads to efficient cleavage of p220 upon infection with VT7, a recombinant vaccinia virus that expresses the T7 RNA polymerase. Under these conditions vaccinia virus protein synthesis is severely inhibited, while expression of poliovirus protein 2C from a similar plasmid has no effect. These results show by the first time the effects of p220 cleavage on vaccinia virus translation in the infected cells.
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies; D002522:Chlorocebus aethiops; D006224:Cricetinae; D003546:Cysteine Endopeptidases / Q000096:biosynthesis / Q000378:metabolism*; D039562:Eukaryotic Initiation Factor-4F; D006367:HeLa Cells; D006801:Humans; D007668:Kidney; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis / Q000737:chemistry; D010448:Peptide Initiation Factors / Q000378:metabolism*; D010957:Plasmids; D011817:Rabbits / Q000276:immunology; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000378:metabolism; D015183:Restriction Mapping; D014162:Transfection; D014764:Viral Proteins
D000906:Antibodies; D039562:Eukaryotic Initiation Factor-4F; D010446:Peptide Fragments; D010448:Peptide Initiation Factors; D011994:Recombinant Proteins; D014764:Viral Proteins; D003546:Cysteine Endopeptidases; C057400:picornain 2A, Picornavirus