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Literature summary for 3.1.31.1 extracted from

  • Zhou, B.; Liu, K.; Wei, J.C.; Mao, X.; Chen, P.Y.
    Inhibition of replication of classical swine fever virus in a stable cell line by the viral capsid and Staphylococcus aureus nuclease fusion protein (2010), J. Virol. Methods, 167, 79-83.
    View publication on PubMed

Application

Application Comment Organism
medicine capsid-targeted viral inactivation as an antiviral strategy against classical swine fever infection, the fusion protein Cap-SNase can inhibit effectively the production of classical swine fever virus, resulting in a reduction in infectious titers Staphylococcus aureus

Cloned(Commentary)

Cloned (Comment) Organism
a plasmid pcDNA-Cap-SNase is constructed for expressing a fusion protein of classical swine fever virus capsid Cap and staphylococcal nuclease, a mammalian cell line PK-15 expressing stably the fusion protein Cap-SNase Staphylococcus aureus

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activity is Ca2+ dependent, 10 mM are included in assay buffer Staphylococcus aureus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
17000
-
molecular weight is calculated by amino acid sequence, the Cap-SNase fusion protein with a molecular weight of 31000 Da is determines by SDS-PAGE and Western blot analysis Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
antiviral efficacy: in PK-15/Cap-SNase cells and normal PK-15 cells, infected with the classical swine fever virus Shimen strain, the virus titer produced by PK-15/Cap-SNase cells is 100 times lower than that of normal PK-15 cells 5 days after infection, after 6 days, a greater antiviral effect is observed in the PK15/Cap-SNase cells which produced a virus titer that is 3500times lower than the control Staphylococcus aureus
additional information
-
the activity of the 5 microl cell lysate containing Cap-SNase is similar to that of 0.5 pg of a standard preparation of SNase, while the linearized plasmid DNA can not be digested when removing Ca2+ by EDTA treatment, indicating that the expressed Cap-SNase retains a good Ca2+-dependent nuclease activity Staphylococcus aureus

Synonyms

Synonyms Comment Organism
SNase
-
Staphylococcus aureus
staphylococcal nuclease
-
Staphylococcus aureus
staphylococcus aureus nuclease
-
Staphylococcus aureus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Staphylococcus aureus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
assay at Staphylococcus aureus