Phosphoprotein P of Rinderpest virus binds to plus sense leader RNA: regulation by phosphorylation

Virus Research
Tamal RahaM S Shaila

Abstract

The negative sense genome RNA of Rinderpest virus, a Paramyxoviridae, is encapsidated with the nucleocapsid protein N and serves as a template for the viral RNA dependent RNA polymerase for transcription and replication. The viral RNA polymerase consists of the large protein L and the phosphoprotein P functioning as the P-L complex. We provide in this report, evidences for specific binding of P protein of Rinderpest virus to the plus sense leader RNA depending on its phosphorylation status. We have also demonstrated that P protein is released from the le RNA:P protein complex upon phosphorylation in vitro. Finally, we have identified that the C-terminal 358-389 amino acid residues of P protein is involved in le RNA binding. The leader RNA binding may signify a hitherto unidentified role for P protein in the viral RNA synthesis. Moreover, our results indicate a possible role for P protein in the transcription-replication switch through leader RNA binding.

References

Jan 1, 1974·Medical Microbiology and Immunology·D W Kingsbury

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Citations

Jul 5, 2007·Bioscience Reports·Soumen BasakDhrubajyoti Chattopadhyay
Jun 23, 2012·Acta Tropica·Sunil MenghaniPramod Khedekar
Jan 1, 2021·The Journal of Immunology : Official Journal of the American Association of Immunologists·Pengfei LiHaixue Zheng

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