Identification of a phosphorylated non-structural form of the P protein of Newcastle disease virus and analysis of P multimers.
Two phosphorylated and two non-phosphorylated variants of P protein isolated from Newcastle disease virions are known. Here, a fifth form of P was identified using two-dimensional polyacrylamide gel electrophoresis and peptide mapping. P form 5 was phosphorylated; however, unlike the four known variants of P, the new form was not a major protein in virions, which suggested an intracellular function. The subunit composition of four electrophoretically distinct, disulphide-linked multimers of P from virions was determined. Each homomultimer was composed of at least three molecules of a different one of the four virion-associated P variants.
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008970:Molecular Weight; D009522:Newcastle disease virus / Q000378:metabolism*; D010750:Phosphoproteins / Q000096:biosynthesis / Q000302:isolation & purification*; D010766:Phosphorylation; D013462:Sulfur Radioisotopes; D014764:Viral Proteins / Q000096:biosynthesis / Q000302:isolation & purification*; D014771:Virion / Q000032:analysis
D010750:Phosphoproteins; D013462:Sulfur Radioisotopes; D014764:Viral Proteins