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Virology. 1994 Nov 15;205(1):93-103.

Bacterial expression of human respiratory syncytial viral phosphoprotein P and identification of Ser237 as the site of phosphorylation by cellular casein kinase II.

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Department of Biochemistry and Molecular Biology, College of Medicine, University of South Alabama, Mobile 36688-0002.

Erratum in

  • Virology 1995 May 10;209(1):284.


The phosphoprotein P gene of human respiratory syncytial virus has been cloned and the protein expressed in Escherichia coli. The expressed protein was soluble, unphosphorylated, and constituted approximately 10% of the total bacterial protein. Electrophoretic and antigenic analyses demonstrated the identity of the recombinant protein with viral P protein and P protein synthesized in reticulocyte lysates. Purified recombinant P protein was efficiently phosphorylated in vitro by purified native as well as recombinant casein kinase II (CKII) or by the CKII activity in uninfected cell extracts. Through deletions and site-directed mutagenesis, the site of CKII phosphorylation was mapped to a single serine residue (Ser237) near the C-terminal end of the P protein.

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