Genetic construction, expression, and melanoma-selective cytotoxicity of a diphtheria toxin-related α-melanocyte-stimulating hormone fusion protein

J. R. Murphy, W. Bishai, M. Borowski, A. Miyanohara, J. Boyd, S. Nagle

Research output: Contribution to journalArticlepeer-review

106 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)8258-8262
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume83
Issue number21
DOIs
StatePublished - 1986
Externally publishedYes

ASJC Scopus subject areas

  • General

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