Disease relevance of CuNVgp2

• This suggests that the CNV 92-kDa protein is the viral replicase and, furthermore, suggests a close evolutionary relationship between CNV, CarMV, and BYDV, members of the Tombus-, Carmo-, and Luteovirus groups, respectively [1].
• Characterization of the RNA-binding domains in the replicase proteins of tomato bushy stunt virus [2].
• Plus-strand RNA virus replication occurs via the assembly of viral replicase complexes involving multiple viral and host proteins [3].
• Since all genera in Tombusviridae encode comparable replicase proteins, these results may be relevant to other members of this large virus family [4].
• Further support for the selectivity of p33 binding in vitro was provided by the inability of the replicase proteins of the closely related Turnip crinkle virus and distantly related Hepatitis C virus to specifically recognize the TBSV IRE [4].

High impact information on CuNVgp2

• Proteomics analysis of the tombusvirus replicase: Hsp70 molecular chaperone is associated with the replicase and enhances viral RNA replication [3].
• Together, these results suggest that IRE activity is required in the cytosol at an early step in the viral replication process, such as template recruitment and/or replicase complex assembly [5].
• We found that the template activity of the tombusvirus replicase preparation was stimulated in trans by the REN, suggesting that the REN is a functional enhancer when located in the vicinity of the promoter [6].
• We found that this RNA sequence bound to the TBSV replicase proteins more efficiently than did control nonviral sequences, suggesting that it might be involved in replicase "landing" during the template switching events [7].
• The two proteins, which constitute the viral replicase, were correctly translated and integrated into membranes of the yeast cells [8].

Biological context of CuNVgp2

• Tomato bushy stunt virus (TBSV), a tombusvirus with a nonsegmented, plus-stranded RNA genome, codes for two essential replicase proteins [2].
• An additional plasmid was introduced in yeasts expressing the CIRV replicase, from which a defective interfering (DI) RNA (DI-7 RNA) could be transcribed under the control of the GAL1 promoter and terminated by the Tobacco ringspot virus satellite ribozyme, which cleaved 19 nucleotides downstream of the 3' end of DI RNA [8].
• In addition, intramolecular replicase-mediated events (i.e., rearrangements) can lead to the generation of replicable deleted forms of a viral genome, termed defective interfering (DI) RNAs [9].
• These results suggest that neither translation nor polymerase activity of the replicase proteins require pX gene sequences [10].
• The efficient replication of input DI RNA, which is incapable of autonomous replication, confirmed the biological activity of the expressed viral replicase [11].

Associations of CuNVgp2 with chemical compounds

• We suggest that the last 77 nt of the viral genome and either half of block C1 represent the complementary strand promoter sequence recognized by the viral replicase [12].

Analytical, diagnostic and therapeutic context of CuNVgp2

• In this work, we demonstrate that both replicase proteins bind to RNA in vitro based on gel mobility shift and surface plasmon resonance measurements [2].
• Mass spectrometry analysis of proteins resolved by two-dimensional gel electrophoresis revealed the presence of CNV p33 and p92 replicase proteins as well as four major host proteins in the CNV replicase [3].

References