Differences in biological activity and structural protein VP1 phosphorylation of polyomavirus progeny resulting from infection of primary mouse kidney and primary mouse embryo cell cultures.
Both primary mouse kidney and primary mouse embryo cells in culture were used for polyomavirus progeny production. Examination of polyomavirus virion structural integrity revealed that mouse embryo cell progeny contained a threefold greater population of unstable particles when compared with mouse kidney cell progeny. Differences in biological activity between these two progeny virion types were also shown. Mouse kidney cell progeny compared with mouse embryo cell progeny exhibited a 10-fold greater ability to agglutinate guinea pig erythrocytes, a 3-fold lower ability to become internalized into monopinocytotic vesicles, and a 2-fold lower ability to initiate a productive infection based on positive nuclear immunofluorescence when mouse embryo host cell cultures were used. The mouse kidney progeny were also found to bind to host cells less specifically than the mouse embryo cell progeny. When these two progeny virion types were labeled in vivo with 32P and subjected to isoelectric focusing followed by sodium dodecyl sulfate-polyacrylamide gel electrophroesis in the second dimension, differences in the phosphorylation pattern of the major virus-encoded structural protein VP1 species were observed. It was revealed that species D and E of mouse kidney cell progeny were phosphorylated to the same degree, while mouse embryo cell progeny species E and F were phosphorylated equally. These data suggest that the host cells play a role in modulating the biological activity of the virus by affecting the degree and site-specific phosphorylation of the major capsid protein VP1 which may influence the recognition of virus attachment proteins for specific cellular receptors.
D000818:Animals; D002471:Cell Transformation, Neoplastic; D002478:Cells, Cultured; D004622:Embryo, Mammalian; D006386:Hemagglutination Tests; D007668:Kidney; D051379:Mice; D010766:Phosphorylation; D011120:Polyomavirus / Q000235:genetics*; D014764:Viral Proteins / Q000502:physiology*; D015678:Viral Structural Proteins; D014771:Virion / Q000235:genetics*
D014764:Viral Proteins; D015678:Viral Structural Proteins