Site-specific mutagenesis of the human fibroblast interferon gene.
Human fibroblast interferon has three cysteine residues, located at amino acid positions 17, 31, and 141. Using the technique of site-specific mutagenesis with a synthetic oligonucleotide primer, we changed the codon for cysteine-17 to a codon for serine. The resulting interferon, IFN-beta Ser-17, retains the antiviral, natural killer cell activation, and antiproliferative activities of native fibroblast interferon. The purified IFN-beta Ser-17 protein has an antiviral specific activity of 2 X 10(8) units/mg, similar to that of purified native fibroblast interferon. In addition, the purified protein is stable to long-term storage at -70 degrees C.
D000595:Amino Acid Sequence; D001483:Base Sequence; D002460:Cell Line; D003001:Cloning, Molecular; D003545:Cysteine; D005796:Genes; D006801:Humans; D007370:Interferon Type I / Q000235:genetics* / Q000633:toxicity; D007694:Killer Cells, Natural / Q000187:drug effects / Q000276:immunology; D008213:Lymphocyte Activation; D009154:Mutation; D009838:Oligodeoxyribonucleotides / Q000633:toxicity; D010957:Plasmids; D012867:Skin; D014721:Vesicular stomatitis Indiana virus / Q000187:drug effects
D007370:Interferon Type I; D009838:Oligodeoxyribonucleotides; D003545:Cysteine