The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

SeMVgp2  -  protease; Vpg; replicase

Sesbania mosaic virus

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of SeMVgp2


High impact information on SeMVgp2

  • In Sesbania mosaic virus, open reading frame-2 codes for a polyprotein that is cleaved into different functional proteins in cis by the N-terminal serine protease domain [4].
  • Polyprotein processing is a major strategy used by many plant and animal viruses to maximize the number of protein products obtainable from a single open reading frame [4].
  • The residues of the S1-binding pocket, H298, T279 and N308 were mutated to alanine in the DeltaN70-Protease-VPg polyprotein, and the cis-cleavage activity was examined [1].
  • The putative replicase of CfMV is produced as a part of the polyprotein from ORF2b by the -1 ribosomal frameshifting mechanism [5].
  • The cleavage site between VPg and RNA dependent RNA polymerase was predicted to be E445-T446 based on the amino acid sequence analysis of the polyprotein from different sobemoviruses [6].

Biological context of SeMVgp2

  • ORF 2 encodes a polyprotein containing the serine protease, genome linked viral protein (VPg) and RNA dependent RNA polymerase domains and shows 78% identity with SBMV-Ark [6].

Associations of SeMVgp2 with chemical compounds

  • Mutational analysis of the proposed catalytic triad residues (H181, D216, and S284) present in the N-terminal serine protease domain of the polyprotein showed that the protease was indeed responsible for this processing [2].


  1. Crystal structure of the serine protease domain of Sesbania mosaic virus polyprotein and mutational analysis of residues forming the S1-binding pocket. Gayathri, P., Satheshkumar, P.S., Prasad, K., Nair, S., Savithri, H.S., Murthy, M.R. Virology (2006) [Pubmed]
  2. Polyprotein processing: cis and trans proteolytic activities of Sesbania mosaic virus serine protease. Satheshkumar, P.S., Lokesh, G.L., Savithri, H.S. Virology (2004) [Pubmed]
  3. Sobemovirus genome appears to encode a serine protease related to cysteine proteases of picornaviruses. Gorbalenya, A.E., Koonin, E.V., Blinov, V.M., Donchenko, A.P. FEBS Lett. (1988) [Pubmed]
  4. "Natively unfolded" VPg is essential for Sesbania mosaic virus serine protease activity. Satheshkumar, P.S., Gayathri, P., Prasad, K., Savithri, H.S. J. Biol. Chem. (2005) [Pubmed]
  5. Regulation of -1 ribosomal frameshifting directed by cocksfoot mottle sobemovirus genome. Lucchesi, J., Mäkeläinen, K., Merits, A., Tamm, T., Mäkinen, K. Eur. J. Biochem. (2000) [Pubmed]
  6. Complete nucleotide sequence of Sesbania mosaic virus: a new virus species of the genus Sobemovirus. Lokesh, G.L., Gopinath, K., Satheshkumar, P.S., Savithri, H.S. Arch. Virol. (2001) [Pubmed]
WikiGenes - Universities