Localization in diphtheria toxin fragment B of a region that induces pore formation in planar lipid bilayers at low pH |
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Authors: | Michel Deleers, Nadine Beugnier, Paul Falmagne, V ronique Cabiaux,Jean-Marie Ruysschaert |
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Affiliation: | Michel Deleers, Nadine Beugnier, Paul Falmagne, Véronique Cabiaux,Jean-Marie Ruysschaert, |
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Abstract: | Like diphtheria toxin and the N-terminal (Mr 23 000) region of fragment B, CB1 (Mr 13 000), the cyanogen bromide peptide located in the middle region of fragment B is able to induce pore formation in lipid bilayer membrane at low pH. These two peptides (Mr 23 000 and 13 000) share a common segment (Mr 6300) containing the predicted amphipathic, -helical, transverse lipid-associating domain (Mr 2750) of fragment B[J. Cell Biol. (1980) 87, 837–840]. Therefore, we postulated this domain to be responsible for the pore formation ability of diphtheria toxin [Proc. Natl. Acad. Sci. USA (1981) 78, 172–176]. A relationship between the pH dependency of pore formation and the presence of a cluster of prolines in the C-terminal region of CB1 is proposed. |
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Keywords: | Diphtheria toxin Fragment B amphipathic region Lipid-associating domain Voltage-dependent conductance Proline isomerization |
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