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

par Cabiaux, Véronique ;Mindell, J;Collier, R J
Référence Infection and immunity, 61, 5, page (2200-2202)
Publication Publié, 1993-05

Article révisé par les pairs

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Résumé :

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.