Abstract
Canine interferon-γ (CaIFN-γ) cDNA was expressed in silkworm by infecting recombinant baculovirus. Western blot analyses revealed that the resulting preparation contained various CaIFN-γ protein molecules. Genetic engineering of CaIFN-γ to remove potential glycosylation sites resulted in reduced components of the CaIFN-γ, suggesting that one cause of this heterogeneity was glycosylation. Nonglycosylated CaIFN-γ produced in silkworm still had several components that were deleted at the carboxy-terminal end. The major component was the CaIFN-γ protein truncated 17 or 16 carboxy-terminal amino acid residues. CaIFN-γ showed antiviral activity, class II major histocompatibility complex (MHC) expression-enhancing activity, and antiproliferation activity on tumor cells.
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