Production of canine IFN-gamma in silkworm by recombinant baculovirus and characterization of the product.
Canine interferon-gamma (CaIFN-gamma) cDNA was expressed in silkworm by infecting recombinant baculovirus. Western blot analyses revealed that the resulting preparation contained various CaIFN-gamma protein molecules. Genetic engineering of CaIFN-gamma to remove potential glycosylation sites resulted in reduced components of the CaIFN-gamma, suggesting that one cause of this heterogeneity was glycosylation. Nonglycosylated CaIFN-gamma produced in silkworm still had several components that were deleted at the carboxy-terminal end. The major component was the CaIFN-gamma protein truncated 17 or 16 carboxy-terminal amino acid residues. CaIFN-gamma showed antiviral activity, class II major histocompatibility complex (MHC) expression-enhancing activity, and antiproliferation activity on tumor cells.
Okano
F
F
Toray Industries, Inc., Chemicals Research Laboratories, Nagoya 455-8502, Japan. Fumiyoshi_Okano@nts.toray.co.jp
Satoh
M
M
Ido
T
T
Okamoto
N
N
Yamada
K
K
D000818:Animals; D016367:Baculoviridae / Q000235:genetics*; D012831:Bombyx / Q000201:enzymology / Q000821:virology*; D002455:Cell Division; D004285:Dogs; D005822:Genetic Vectors; D006031:Glycosylation; D006458:Hemolymph / Q000201:enzymology; D000949:Histocompatibility Antigens Class II / Q000378:metabolism; D007371:Interferon-gamma / Q000235:genetics* / Q000302:isolation & purification / Q000502:physiology*; D010447:Peptide Hydrolases / Q000097:blood; D020033:Protein Isoforms / Q000235:genetics / Q000302:isolation & purification / Q000502:physiology; D011994:Recombinant Proteins / Q000302:isolation & purification; D014407:Tumor Cells, Cultured; D014721:Vesicular stomatitis Indiana virus / Q000187:drug effects
D000949:Histocompatibility Antigens Class II; D020033:Protein Isoforms; D011994:Recombinant Proteins; D007371:Interferon-gamma; D010447:Peptide Hydrolases