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 α-melanocyte-stimulating hormone (α-MSH). The resulting fusion gene directs the expression of a diphtheria toxin-related α-MSH hybrid protein in which the diphtheria toxin receptor-binding domain has been replaced with α-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 α-MSH receptor-positive human malignant melanoma NEL-M1 cells in vitro.
|Number of pages
|Proceedings of the National Academy of Sciences of the United States of America
|Published - 1986
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