Structural components of influenza C virions.
The genome RNA species of influenza type C virions were analyzed by polyacrylamide gel electrophoresis. The pattern obtained was found to resemble those of other influenza viruses. Six RNA species were resolved, with estimated sizes ranging from 0.37 X 10(6) to 1.25 X 10(6) daltons. The internal ribonucleoproteins of influenza C virions were found to sediment heterogeneously in glycerol velocity gradients as demonstrated previously with influenza A/WSN virus. The ribonucleoproteins possessed diameters of 12 to 15 nm, with lengths ranging from 30 to 100 nm. Of the three major virion polypeptides (molecular weights, 88,000, 66,000, and 26,000), only the largest is glycosylated. Similar polypeptide species were present in influenza C virions of five different strains. All three major proteins of influenza C virions possess electrophoretic mobilities distinguishable from those of the major polypeptides of influenza A/WSN. The 66,000-dalton protein is associated with the ribonucleoprotein components. Two additional glycosylated polypeptides, with estimated molecular weights of 65,000 and 30,000, were detected in virions grown in embryonated eggs, but not in virus particles obtained from chicken embryo fibroblasts.
D006023:Glycoproteins / Q000032:analysis; D009980:Influenza A virus / Q000032:analysis; D008970:Molecular Weight; D009975:Orthomyxoviridae / Q000032:analysis* / Q000648:ultrastructure; D010455:Peptides / Q000032:analysis; D012367:RNA, Viral / Q000032:analysis*; D014764:Viral Proteins / Q000032:analysis*
D006023:Glycoproteins; D010455:Peptides; D012367:RNA, Viral; D014764:Viral Proteins