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. 1993 May;61(5):2200-2.
doi: 10.1128/iai.61.5.2200-2202.1993.

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

V Cabiaux  1 , J Mindell, R J Collier
Affiliations

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

V Cabiaux et al. Infect Immun. 1993 May.

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.

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