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Involvement of serine proteinase in infectious pancreatic necrosis virus capsid protein maturation and NS proteinase cleavage in CHSE‐214 cells
Author(s) -
Wu JL,
Hong JR,
Chang CY,
Hui CF,
Liao CF,
Hsu YL
Publication year - 1998
Publication title -
journal of fish diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.819
H-Index - 85
eISSN - 1365-2761
pISSN - 0140-7775
DOI - 10.1046/j.1365-2761.1998.00097.x
Subject(s) - capsid , biology , serine proteinase inhibitors , serine , infectious pancreatic necrosis virus , cleavage (geology) , proteinase 3 , virus , serine protease , microbiology and biotechnology , enzyme , virology , biochemistry , protease , antibody , immunology , paleontology , fracture (geology) , autoantibody
An investigation of virus‐specific protein maturation in infectious pancreatic necrosis virus (IPNV) infected Chinook salmon embryo cells (CHSE‐214) was undertaken. The precursor protein (pVP2–1) of the major mature capsid protein (VP2) was processed sequentially from pVP2–1 to pVP2–2 and VP2. Experiments using serine proteinase inhibitors showed that the maturation of the VP2 was blocked in the pVP2–1 post‐translational cleavage steps. A protinin, a potent proteinase inhibitor, at 800 μg ml –1 blocked pVP2–2 to VP2 and the cleavage of VP4 (28 kDa) to VP4–1 (25 kDa). Therefore, our data showed that the maturation of the capsid protein (VP2) and cleavage of VP4 (NS proteinase) can be blocked by serine proteinase inhibitors.