Indian Journal of Virology
  • Year: 2008
  • Volume: 19
  • Issue: 1

S-58. RNA dependent RNA polymerase L protein of rinderpest virus exhibits in vitro transcription and capping activities

  • Author:
  • M. Gopinath, M.S. Shaila

Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore-560012, India.

Abstracts of the papers presented at the International Conference of Indian Virological Society on “Emerging and Re-emerging viral Diseases of the Tropics and Subtropics” at Indian Agricultural Research Institute, New Delhi, India, December 11–14, 2007.

Abstract

The nonsegmented negative strand RNA genome of paramyxoviruses is thghtly encapsidated by the nucleocapsid protein (N) to form a helical nucleocapsid (N-RNA). This N-RNA serves as a template for both mRNA synthesis and genome replication by the associated RNA polymerase. It is generally believed that the same polymerase compled of L and P proteins perform both transcription and replcaition of the genome. Employing recombinant baculoviruses expressing L and P proteins of Rinderpest virus, it has been shown that the L-P complex partially purified from insect cells faithfully synthesizes all viral mRNA in vitro. The requirements for such transcriptional activity wil be described.

Post-trnascriptional modifications of mRNA at the 5 end involve guanylyl transferase Catalysed reactions and subsequent methyl transferase activities. It has been shown for the first time that the recombinant L protein of Rinderpest virus also has capping enzyme activity. The occurrence of transguanylyation via a capping enzyme (L)-guanylate was demonstrated.