Disease relevance of Bluetongue

• A similar problem was encountered previously with bluetongue virus (BTV) VP7 (whose structure has been reported), showing that the connections between the top and the bottom domains are rather weak for these two distinct orbiviruses [1].
• Crystal structure of the top domain of African horse sickness virus VP7: comparisons with bluetongue virus VP7 [1].
• The bluetongue virus (BTV) core protein VP3 plays a crucial role in the virion assembly and replication process [2].
• Segment 2 of bluetongue virus (BTV) serotype 10, which encodes the outer capsid protein VP2, was tagged with the S-peptide fragment of RNase A and expressed by a recombinant baculovirus [3].
• A cDNA sequence of RNA segment 9 of bluetongue virus serotype 10 (BTV-10, an orbivirus member of the Reoviridae family) encoding a minor core protein (VP6) has been inserted into the BamHI site of the pAcYM1 transfer vector derived from AcNPV [4].

High impact information on Bluetongue

• The crystal structure of bluetongue virus VP7 [5].
• The overall fold is similar to that of protein VP7 from bluetongue virus, with the subunits wrapping about a central 3-fold axis [6].
• Capping and methylation of mRNA by purified recombinant VP4 protein of bluetongue virus [7].
• Sequence specificity in the interaction of Bluetongue virus non-structural protein 2 (NS2) with viral RNA [8].
• Complete sequence of the NS1 gene (S6 RNA) of US bluetongue virus serotype 17 [9].

Chemical compound and disease context of Bluetongue

• As demonstrated by stained polyacrylamide gel electrophoresis and by the use of bluetongue virus antibody, infected insect cells synthesized the largest protein of BTV-10 (VP1, 150 k Da) [10].
• Membrane organization of bluetongue virus nonstructural glycoprotein NS3 [11].
• Mutation of either of two cysteine residues or deletion of the amino or carboxy terminus of nonstructural protein NS1 of bluetongue virus abrogates virus-specified tubule formation in insect cells [12].
• To correct for the resolution dependent fall-off of the amplitudes derived from electron microscopic images, the rotavirus VP6 amplitudes were scaled to the bluetongue VP7 amplitudes derived from the atomic model by applying a B factor of -360 A-2 [13].
• In cytopathic effect inhibition studies, bluetongue virus was markedly inhibited by 3-deazaguanine and 3-deazauridine in Vero cells with moderate inhibition by the other agents [14].

Biological context of Bluetongue

• Nucleotide sequence of the VP4 core protein gene (M4 RNA) of US bluetongue virus serotype 10 [15].
• Genome segment 9 of bluetongue virus serotype 10 encodes the minor protein VP6 [16].
• Recombinant plasmids containing inserts representing genome segments 2, 5, 6, 8, and 9 of bluetongue virus (BTV) serotype 11, with tentative coding assignments for viral proteins P2, P5, NS1, NS2, and P6, respectively, have been used to study the genetic diversity within a BTV serotype using Northern blot hybridization [17].
• Morphogenesis of a bluetongue virus variant with an amino acid alteration at a neutralization site in the outer coat protein, VP2 [18].
• Comparison of the AHSV VP6 amino acid sequences with those of bluetongue virus serotype 10 VP6 revealed that it is 41 amino acids longer with an overall amino acid identity of 29 percent [19].

Anatomical context of Bluetongue

• In vitro translation of bluetongue virus (BTV) double-stranded RNA in the rabbit reticulocyte lysate system has shown segment 10 (S10) to code for two related proteins, NS3 and NS3A [20].
• The bluetongue virus ssRNA-binding protein, NS2, is a phosphoprotein that forms viral inclusion bodies in infected cells [21].
• Seven monoclonal antibodies to the nonstructural protein NS1 of an Australian isolate of bluetongue virus (BTV) have been used in immunofluoresence and immunogold procedures to locate NS1 in virus-infected cells and cytoskeletons [22].
• Baculovirus-expressed nonstructural protein NS2 of bluetongue virus induces a cytotoxic T-cell response in mice which affords partial protection [23].
• A single chain fragment variable (scFv) antibody gene was isolated from hybridoma cell line secreting monoclonal antibody (MAb) 20E9 that recognises bluetongue virus (BTV) VP7 [24].

Gene context of Bluetongue

• The complete sequence of the RNA which encodes the major outer-shell-neutralizing antigen (VP2) of bluetongue virus serotype 10 was determined from overlapping cDNA clones inserted into pBR322 [25].
• Nonstructural protein 3 of bluetongue virus assists virus release by recruiting ESCRT-I protein Tsg101 [26].
• Comparison of the AHSV-4 VP7 sequence with that of bluetongue virus serotype 10 revealed an overall similarity of 44%, with the amino- and carboxy-terminal regions exhibiting the greatest levels of homology [27].
• Completion of the sequence of bluetongue virus serotype 10 by the characterization of a structural protein, VP6, and a non-structural protein, NS2 [28].
• Variation in the NS3 gene and protein in South African isolates of bluetongue and equine encephalosis viruses [29].

Analytical, diagnostic and therapeutic context of Bluetongue

• In Western blots, this monoclonal antibody reacted only with the VP2 of bluetongue virus 13, but not with any of the other US BTV serotypes [30].
• Immunoelectron microscopy has been used to confirm that the core protein VP7 is accessible on the surface of bluetongue virus (BTV) particles [31].
• Yeast-expressed VP7 antigen and a monoclonal antibody were used in a blocking ELISA to distinguish sera raised against bluetongue virus serotypes from those generated to viruses of the epizootic haemorrhagic disease serogroup [32].
• In addition, this capture bluetongue virus PCR procedure does not require a lengthy phenol extraction or the use of the highly toxic methyl mercury hydroxide denaturant [33].
• Comparative sequence analyses of the cognate structural protein VP6 genes of five US bluetongue viruses [34].

References