Disease relevance of Vesiculovirus

• A comparison of the matrix (M) and nucleocapsid (N) proteins of four members of the Vesiculovirus group by this procedure suggests considerable conservation of tryptophan number and location in the four serotypes examined [1].
• However, compared to vesiculoviruses that are composed of the five core genes, all plant rhabdoviruses encode more than these five genes, at least one of which is inserted between the P and M genes in the rhabdoviral genome [2].
• The N protein of sigma virus showed no significant homology with its counterpart in SYNV or IHNV and VSHV; it did, however, show sequence homology with the N of four vesiculoviruses and two lyssaviruses [3].
• Chandipura (CHP) virus, a member of the vesiculovirus genus within the Rhabdoviridae family, was first isolated from human patients in India. The full length phosphoprotein P gene of CHP have been cloned and expressed in Escherichia coli using the T7 polymerase-based pET-3 series of expression vectors [4].

High impact information on Vesiculovirus

• In all cases where transport was merely slowed by the M proteins, the chandipura virus M protein had the strongest inhibitory activity [5].
• Additionally, we observed recall and heightened memory responses after boosting animals with a single-cycle vector complemented with G protein from a different vesiculovirus [6].
• Linear mapping of tryptophan residues in Vesiculovirus M and N proteins by partial chemical cleavage [1].
• P-protein of Chandipura virus is an N-protein-specific chaperone that acts at the nucleation stage [7].
• We took Chandipura virus, a member of the Rhabdoviridae family, as our model system to demonstrate that Phosphoprotein P, besides Nucleocapsid protein N, also acts as a leader RNA-binding protein in its unphosphorylated form, whereas CKII-mediated phosphorylation totally abrogates its RNA-binding ability [8].

Chemical compound and disease context of Vesiculovirus

• Structure and expression of the glycoprotein gene of Chandipura virus [9].
• Single serine phosphorylation within the acidic domain of Chandipura virus P protein regulates the transcription in vitro [10].
• The glycoproteins prepared from 7 Vesiculoviruses were differentiated by their electrophoretic mobilities in polyacrylamide gels and by reactions with anti-viral and anti-glycoprotein sera [11].
• Meanwhile, flies inoculated with Chandipura virus present a distinctive feature: below a definite temperature the flies do not become CO2 sensitive although it is still possible to observe a slight multiplication [12].

Biological context of Vesiculovirus

• Leader RNA binding ability of Chandipura virus P protein is regulated by its phosphorylation status: a possible role in genome transcription-replication switch [8].

Anatomical context of Vesiculovirus

• Forty-five vesiculovirus isolates were systematically compared for their capacity to induce interferon (IFN) in chick embryo cells under conditions such that the maximum (quantum) yield of IFN per cell and the titer of IFN-inducing particles (IFP) could validly be determined [13].

Gene context of Vesiculovirus

• This extent of conservation of the N protein sequences underscores the high rate of mutability of the NS protein sequences among the vesiculoviruses [14].
• Matrix protein of Chandipura virus inhibits transcription from an RNA polymerase II promoter [15].
• Effect of melittin on transcription by vesiculovirus mutant and wild-type viruses [16].

References