Protein composition of the structural components of vesicular stomatitis virus.
Digitonin, a sterol glycoside which complexes with cholesterol, stripped off the envelope of vesicular stomatitis (VS) virions and liberated two viral structural proteins, 83% of P6 and 53% of P4. Deoxycholate also disrupted VS virions but released nucleocapsid cores which could be identified by higher buoyant density, ratio of incorporated (3)H-uridine to (14)C-protein, and electron microscopy. The major nucleocapsid protein was P5 but varying amounts of the minor protein aggregate P2 were present, depending on the concentration of urea used for extraction. P2 appeared to be a polymer of P5. Two other minor structural proteins, P1 and P3, could not be located in the virion. From these data, we conclude that the three microscopically identifiable structures of VS virions are each composed primarily of a single major protein, as follows: P6 = envelope protein, P4 = protein of underlying "shell," and P5 = nucleocapsid protein.
D000596:Amino Acids / Q000378:metabolism; D001647:Bile Acids and Salts / Q000494:pharmacology; D002247:Carbon Isotopes; D002499:Centrifugation, Density Gradient; D004589:Electrophoresis, Disc; D006027:Glycosides / Q000494:pharmacology; D008854:Microscopy, Electron; D014316:Tritium; D014529:Uridine / Q000378:metabolism; D014721:Vesicular stomatitis Indiana virus / Q000032:analysis* / Q000187:drug effects; D014764:Viral Proteins / Q000032:analysis* / Q000302:isolation & purification
D000596:Amino Acids; D001647:Bile Acids and Salts; D002247:Carbon Isotopes; D006027:Glycosides; D014764:Viral Proteins; D014316:Tritium; D014529:Uridine