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American Society for Microbiology, Infection and Immunity, 5(61), p. 2200-2202, 1993

DOI: 10.1128/iai.61.5.2200-2202.1993

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Membrane translocation and channel-forming activities of diphtheria toxin are blocked by replacing isoleucine 364 with lysine.

Journal article published in 1993 by V. Cabiaux, J. Mindell ORCID, R. J. Collier
This paper is available in a repository.
This paper is available in a repository.

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Abstract

A mutant of diphtheria toxin in which Ile-364 was replaced by Lys was at least 500-fold less toxic to Vero cells than the parental toxin. Its ability to undergo low-pH-triggered translocation across the plasma membrane was greatly diminished, as was its ability to form ion-conductive channels. In addition, the mutant toxin was inactive in the pH-dependent killing of Escherichia coli.