Genetic construction, expression, and melanoma-selective cytotoxicity of a diphtheria toxin-related alpha-melanocyte-stimulating hormone fusion protein.
The structural gene for diphtheria toxin, tox, has been modified at its Sph I site by the introduction of an oligonucleotide linker encoding a unique Pst I restriction endonuclease site and a synthetic oligonucleotide encoding alpha-melanocyte-stimulating hormone (alpha-MSH). The resulting fusion gene directs the expression of a diphtheria toxin-related alpha-MSH hybrid protein in which the diphtheria toxin receptor-binding domain has been replaced with alpha-MSH sequences. The chimeric toxin has been partially purified from periplasmic extracts of recombinant Escherichia coli K-12 and has been found to be selectively toxic for alpha-MSH receptor-positive human malignant melanoma NEL-M1 cells in vitro.
D036002:ADP Ribose Transferases; D000643:Ammonium Chloride / Q000494:pharmacology; D002460:Cell Line; D004167:Diphtheria Toxin / Q000235:genetics*; D005796:Genes; D006801:Humans; D009074:Melanocyte-Stimulating Hormones / Q000235:genetics*; D008545:Melanoma / Q000188:drug therapy; D008970:Molecular Weight; D010430:Pentosyltransferases / Q000032:analysis; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000235:genetics* / Q000494:pharmacology; D011994:Recombinant Proteins / Q000235:genetics*
D004167:Diphtheria Toxin; D011993:Recombinant Fusion Proteins; D011994:Recombinant Proteins; D000643:Ammonium Chloride; D009074:Melanocyte-Stimulating Hormones; D036002:ADP Ribose Transferases; D010430:Pentosyltransferases