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High–Level Expression of Diphtheria Toxin Peptides in Escherichia coli

Bio/Technology volume 4, pages 1006–1011 (1986)Cite this article

Abstract

Expression of two diphtheria toxin gene fragments in E. coli was studied as a means of obtaining large quantities of proteins for use in immunotoxins. Removal of the secretory leader, and replacement of the diphtheria toxin promoter and Shine–Dalgarno sequence increased the levels of expression in E. coli 36– to 216–fold. We were able to produce the DTA–like peptide at 5 to 7% of the total cell protein. The high level of expression of these proteins in E. coli will facilitate further modification for producing more efficacious effector moieties for use in immunoconjugates.

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Authors and Affiliations

  1. Department of Microbial Genetics, Cetus Corporation, 1400 Fifty-Third Street, Emeryville, CA, 94608

    Lawrence Greenfield, Harry F. Dovey, Frances C. Lawyer & David H. Gelfand

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  1. Lawrence Greenfield
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  2. Harry F. Dovey
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  3. Frances C. Lawyer
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  4. David H. Gelfand
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Greenfield, L., Dovey, H., Lawyer, F. et al. High–Level Expression of Diphtheria Toxin Peptides in Escherichia coli. Nat Biotechnol 4, 1006–1011 (1986). https://doi.org/10.1038/nbt1186-1006

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