ArticleJournal of virology2003
Blotched snakehead virus is a new aquatic birnavirus that is slightly more related to avibirnavirus than to aquabirnavirus.
Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 59 citations in OpenAlex.
- Genomic Characterization and Pathogenicity of a Novel Birnavirus Strain Isolated from Mandarin Fish (Genes · 2025Article
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- Structure of the T=13 capsid of infectious pancreatic necrosis virus (IPNV)-a salmonid birnavirus.Journal of virology · 2025Article
- Expanding the Genetic Code ofACS chemical biology · 2024Article
- Engineering Small Molecule Switches of Protein Function in Zebrafish Embryos.Journal of the American Chemical Society · 2023Article
- Small-Molecule Phosphine Activation of Protein Function in Zebrafish Embryos with an Expanded Genetic Code.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Determination and Characterization of a Novel Birnavirus Associated with Massive Mortality in Largemouth Bass.Microbiology spectrum · 2022Article
- Article
- Human land use impacts viral diversity and abundance in a New Zealand river.Virus evolution · 2022Article
- Discrete Virus Factories Form in the Cytoplasm of Cells Coinfected with Two Replication-Competent Tagged Reporter Birnaviruses That Subsequently Coalesce over Time.Journal of virology · 2020Article
- Article
- Detection and characterization of a novel marine birnavirus isolated from Asian seabass in Singapore.Virology journal · 2019Article
- Avibirnavirus VP4 Protein Is a Phosphoprotein and Partially Contributes to the Cleavage of Intermediate Precursor VP4-VP3 Polyprotein.PloS one · 2015Article
- Isolation of Streptococcus agalactiae and an aquatic birnavirus from doctor fish Garra rufa L.Irish veterinary journal · 2013Article
- Crystal structures of yellowtail ascites virus VP4 protease: trapping an internal cleavage site trans acyl-enzyme complex in a native Ser/Lys dyad active site.The Journal of biological chemistry · 2013Article
- Host proteolytic activity is necessary for infectious bursal disease virus capsid protein assembly.The Journal of biological chemistry · 2012Article
- Crystal structure of a viral protease intramolecular acyl-enzyme complex: insights into cis-cleavage at the VP4/VP3 junction of Tellina birnavirus.The Journal of biological chemistry · 2011Article
- Expression, purification and crystallization of VP4 protease from Tellina virus 1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Crystal structure of an Aquabirnavirus particle: insights into antigenic diversity and virulence determinism.Journal of virology · 2010Article
- Self-guanylylation of birnavirus VP1 does not require an intact polymerase activity site.Virology · 2009Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
By different approaches, we characterized the birnavirus blotched snakehead virus (BSNV). The sequence of genomic segment A revealed the presence of two open reading frames (ORFs): a large ORF with a 3,207-bp-long nucleotide sequence and a 417-nucleotide-long small ORF located within the N-terminal half of the large ORF, but in a different reading frame. The large ORF was found to encode a polyprotein cotranslationally processed by the viral protease VP4 to generate pVP2 (the VP2 precursor), a 71-amino-acid-long peptide ([X]), VP4, and VP3. The two cleavage sites at the [X]-VP4 and VP4-VP3 junctions were identified by N-terminal sequencing. We showed that the processing of pVP2 generated VP2 and several small peptides (amino acids [aa] 418 to 460, 461 to 467, 468 to 474, and 475 to 486). Two of these peptides (aa 418 to 460 and 475 to 486) were positively identified in the viral particles with 10 additional peptides derived from further processing of the peptide aa 418 to 460. The results suggest that VP4 cleaves multiple Pro-X-Ala downward arrow Ala motifs, with the notable exception of the VP4-VP3 junction. Replacement of the members of the predicted VP4 catalytic dyad (Ser-692 and Lys-729) confirmed their indispensability in the polyprotein processing. The genomic segment B sequence revealed a single large ORF encoding a putative polymerase, VP1. Our results demonstrate that BSNV should be considered a new aquatic birnavirus species, slightly more related to IBDV than to IPNV.
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