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Virology. 1994 Nov 15;205(1):104-11.

Requirement of casein kinase II-mediated phosphorylation for the transcriptional activity of human respiratory syncytial viral phosphoprotein P: transdominant negative phenotype of phosphorylation-defective P mutants.

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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 transcription complex of the human respiratory syncytial virus was biochemically dissected and reconstituted in vitro with purified viral macromolecules. The minimal complex consisted of the viral N-RNA template, viral phosphoprotein (P), and the large protein (L) along with host cellular factor(s), possibly actin. Active transcription could also be reconstituted using bacterially synthesized recombinant P protein provided the P protein was phosphorylated by cellular casein kinase II. Elimination of phosphorylation by inhibition of CKII or by mutation of the Ser residue at position 237 of the P protein also abrogated RSV transcription. In addition, the phosphorylation-defective P mutants exhibited a trans-dominant negative phenotype, consistent with the finding that the mutant proteins bound to the N-RNA template as efficiently as the wild type. Once engaged in transcription, however, the wild-type P protein became refractory to trans-inhibition by the mutant.

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