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Microbiology Section, Biological Sciences Group, The University of Connecticut, Storrs, Connecticut 06268, U.S.A.
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.
Keywords: NDV, phosphoproteins, non-structural protein
Present address: Department of Microbiology and Immunology, University of North Carolina, Chapel Hill, North Carolina 27514, U.S.A.
Received 18 April 1984;
accepted 4 June 1984.
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