Sendai virus P protein is constitutively phosphorylated at serine249: high phosphorylation potential of the P protein

Virology
S ByrappaK C Gupta

Abstract

Previously we showed that the Sendai virus P protein (568 aa) in virus-infected cells and in virions was primarily and constitutively phosphorylated on serine(s) in a single tryptic phosphopeptide TP1. By two-dimensional thin-layer electrophoresis and chromatography analysis of tryptic phosphopeptides of several deletion and point mutants of the P protein, we now show that the sole phosphorylation site in TP1 is serine249. Interestingly, when serine249 was deleted or mutagenized alternate potential serine sites were more heavily phosphorylated. A similar effect was observed when the deletion was very close to serine249 (delta 208-236). Mutagenesis of proline250 to alanine abrogated phosphorylation at serine249 suggesting that proline250 is essential for the primary phosphorylation of the P protein. Conceivably, serine249 phosphorylation is mediated by a proline-directed protein kinase. This finding is unusual because a majority of the P proteins from other negative-strand RNA viruses have been shown to be phosphorylated primarily by casein kinase II. Our results demonstrate that the P protein has a strong potency to remain phosphorylated. Based on our previous and present results, we suggest that the phosphorylation sites on P ...Continue Reading

Citations

Jul 25, 2009·PLoS Pathogens·Dengyun SunBiao He
Dec 22, 2009·Future Microbiology·Sandra M FuentesBiao He
Apr 4, 2009·Journal of Molecular Biology·Francine C A GerardMarc Jamin
Oct 8, 2008·Immunological Reviews·Judith M FontanaPaul A Rota
Mar 26, 1998·Virology·C DelendaD Kolakofsky
Jun 27, 1997·The Journal of Biological Chemistry·C C HuntleyA K Banerjee
Dec 4, 2003·The Journal of General Virology·David KarlinSonia Longhi
Dec 6, 2000·The Journal of Biological Chemistry·H VihinenL Kääriäinen

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