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

Print ISSN : 0970-2822.

P-18. Effect of viral genome-linked protein (VPg) on protease function of nuclear inclusion- a (NIa) protein of pepper vein banding virus

Chhavi Mathur, Roy Anindya, Savithri H.S.

Department of Biochemistry, 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.


In the Indian subcontinent, a major bottleneck in cultivation of pepper has been the crop loss due to viral infection, particularly by pepper vein banding virus (PVBV). PVBV, like other members of Potyvirus group (Family: Potyviridae), forms flexous, non-enveloped, rod-shaped virus particles. Its 9.7 kb long genome is translated into ∼300 kDa polyprotein that is proteolytically processed to give ten individual proteins. This processing is largely carried out by the NIa (Nuclear Inclusion-a) protein. This protein has two domains: the N-terminal VPg (Viral genome-linked protein) and the C-terminal NIa protease. In this study, we aim to investigate the effect of VPg on the protease activity of NIa protease. The protease activity of the NIa protease was studied using an in vitro bead- attached GFP assay. Kinetic parameters of the enzyme were determined. The VPgNIa ORF was amplified using appropriate primers. The PCR product was cloned and over expressed in E. coli. Most of the VPgNIa was seen as cleaved products, VPg and NIa protease, on SDS-PAGE. The cleavage was abolished by mutation of the cleavage site glutamate, and the full length VPgNIa was obtained. The protease activity of VPgNIa was compared with that of NIa protease using the in vitro bead- attached GFP assay. Preliminary results suggest that the presence of VPg at the N-terminus renders the NIa protease more active.


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