Disease relevance of SeMVgp2

• Sesbania mosaic virus (SeMV) polyprotein is processed by its N-terminal serine protease domain [1].
• Sesbania mosaic virus (SeMV) polyprotein was shown to undergo proteolytic processing when expressed in E. coli [2].
• It is suggested that SBMV follows the general expression strategy characteristic of other positive-strand RNA viruses containing 5'-terminal covalently linked proteins (VPg), i.e. generation of functional proteins by polyprotein processing [3].

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].

References