Poliovirus proteins associated with the replication complex in infected cells.
Viral polypeptides associated with the membrane-free replication complex of poliovirus RNA were multiple in nature. The structural protein precursors [VP0, VP1, VP3] predominated, and because they were found in a cytoplasmic component with the same S value and density as the replication complex are likely to be attached to it in vivo. They were not present in the form of empty capsids. The electrophoretic polypeptide pattern of the membrane-bound replication complex was similar but showed a predominance of NCVPX or VP1, unless the cells were slightly depleted in amino acids when the non-structural polypeptide NCVP2 became important. Cystine was the only amino acid capable of reversing this depletion effect on its own.
D000596:Amino Acids / Q000378:metabolism; D002460:Cell Line; D003553:Cystine / Q000378:metabolism; D010452:Peptide Biosynthesis; D010455:Peptides / Q000032:analysis; D017955:Poliovirus / Q000032:analysis* / Q000254:growth & development / Q000378:metabolism; D011498:Protein Precursors / Q000032:analysis; D012367:RNA, Viral / Q000032:analysis; D012270:Ribosomes / Q000032:analysis; D014764:Viral Proteins / Q000032:analysis* / Q000096:biosynthesis; D014779:Virus Replication
D000596:Amino Acids; D010455:Peptides; D011498:Protein Precursors; D012367:RNA, Viral; D014764:Viral Proteins; D003553:Cystine