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J Gen Virol 65 (1984), 1631-1636; DOI 10.1099/0022-1317-65-9-1631
© 1984 Society for General Microbiology

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Identification of a Phosphorylated Non-structural Form of the P Protein of Newcastle Disease Virus and Analysis of P Multimers

Lawrence E. Hightower, Peter L. Collins{dagger} and Glenn W. Smith

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

{dagger} 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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Copyright © 1984 by the Society for General Microbiology.