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. 1993 May;61(5):2200–2202. 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 1, R J Collier 1
PMCID: PMC280822  PMID: 7683003

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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Selected References

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