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Literature summary for 3.4.21.115 extracted from

  • Imajoh, M.; Goto, T.; Oshima, S.
    Characterization of cleavage sites and protease activity in the polyprotein precursor of Japanese marine aquabirnavirus and expression analysis of generated proteins by a VP4 protease activity in four distinct cell lines (2007), Arch. Virol., 152, 1103-1114.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain BL21-DE3 using the pET-41b vector marine birnavirus

Protein Variants

Protein Variants Comment Organism
H681F amino acid substitutions generated in VP4 of MABV by site-directed mutagenesis marine birnavirus
I543G amino acid substitutions generated in VP4 of MABV by site-directed mutagenesis marine birnavirus
K674D amino acid substitutions generated in VP4 of MABV by site-directed mutagenesis marine birnavirus
S633P amino acid substitutions generated in VP4 of MABV by site-directed mutagenesis marine birnavirus
V686Q amino acid substitutions generated in VP4 of MABV by site-directed mutagenesis marine birnavirus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
240000
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SDS-PAGE, single band of VP4, same size of VP4 in all analyzed cell lines marine birnavirus

Organism

Organism UniProt Comment Textmining
marine birnavirus
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MABV strain Y-6, isolated from yellowtail Seriola quinqueradiata with ascites
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification specific enzymatic cleavages yield mature virus proteins marine birnavirus

Purification (Commentary)

Purification (Comment) Organism
gel filtration, native and recombinant proteins marine birnavirus

Source Tissue

Source Tissue Comment Organism Textmining
cell culture VP4 protease activity studied in the cell lines CHSE-214 and RSBK-2 that are susceptible to MABV infection, cell lines FHM and EPC resistant to MABV infection included as a control, infection of cell cultures with MABV at a multiplicity of infection of 0.1, respectively marine birnavirus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information cleavage sites of the MABV polyprotein at the pVP2-VP4 junction determined, VP4 protease activity determined, expression patterns of pVP2, VP4 and VP3 in four infected cell lines shown, VP4 protease activity determined marine birnavirus ?
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?

Synonyms

Synonyms Comment Organism
infectious pancreatic necrosis birnavirus Vp4 protease
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marine birnavirus
VP4
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marine birnavirus