Literature DB >> 1384590

Ion channel and membrane translocation of diphtheria toxin.

C Montecucco1, E Papini, G Schiavo, E Padovan, O Rossetto.   

Abstract

Diphtheria toxin is the best studied member of a family of bacterial protein toxins which act inside cells. To reach their cytoplasmic targets, these toxins, which include tetanus and botulinum neurotoxins and anthrax toxin, have to cross the hydrophobic membrane barrier. All of them have been shown to form ion channels across planar lipid bilayer and, in the case of diphtheria toxin, also in the plasma membrane of cells. A relation between the ion channel and the process of membrane translocation has been suggested and two different models have been put forward to account for these phenomena. The two models are discussed on the basis of the available experimental evidence and in terms of the focal points of difference, amenable to further experimental investigations.

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Year:  1992        PMID: 1384590     DOI: 10.1111/j.1574-6968.1992.tb05892.x

Source DB:  PubMed          Journal:  FEMS Microbiol Immunol        ISSN: 0920-8534


  5 in total

1.  Oligomerization of membrane-bound diphtheria toxin (CRM197) facilitates a transition to the open form and deep insertion.

Authors:  M S Kent; H Yim; J K Murton; S Satija; J Majewski; I Kuzmenko
Journal:  Biophys J       Date:  2007-11-30       Impact factor: 4.033

2.  Assembly mechanism of the oligomeric streptolysin O pore: the early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization.

Authors:  M Palmer; R Harris; C Freytag; M Kehoe; J Tranum-Jensen; S Bhakdi
Journal:  EMBO J       Date:  1998-03-16       Impact factor: 11.598

3.  Structure-function comparisons of the proapoptotic protein Bax in yeast and mammalian cells.

Authors:  H Zha; H A Fisk; M P Yaffe; N Mahajan; B Herman; J C Reed
Journal:  Mol Cell Biol       Date:  1996-11       Impact factor: 4.272

4.  GPI-anchored diphtheria toxin receptor allows membrane translocation of the toxin without detectable ion channel activity.

Authors:  M Lanzrein; O Sand; S Olsnes
Journal:  EMBO J       Date:  1996-02-15       Impact factor: 11.598

5.  Helicobacter pylori vacuolating toxin forms anion-selective channels in planar lipid bilayers: possible implications for the mechanism of cellular vacuolation.

Authors:  F Tombola; C Carlesso; I Szabò; M de Bernard; J M Reyrat; J L Telford; R Rappuoli; C Montecucco; E Papini; M Zoratti
Journal:  Biophys J       Date:  1999-03       Impact factor: 4.033

  5 in total

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