Premium
Localization in diphtheria toxin fragment B of a region that induces pore formation in planar lipid bilayers at low pH
Author(s) -
Deleers Michel,
Beugnier Nadine,
Falmagne Paul,
Cabiaux Véronique,
Ruysschaert Jean-Marie
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80941-7
Subject(s) - diphtheria toxin , chemistry , lipid bilayer , corynebacterium diphtheriae , stereochemistry , toxin , bilayer , amphiphile , biophysics , crystallography , biochemistry , membrane , diphtheria , copolymer , biology , organic chemistry , vaccination , immunology , polymer
Like diphtheria toxin and the N‐terminal ( M r 23 000) region of fragment B, CB1 ( M r 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 ( M r 23 000 and 13 000) share a common segment ( M r 6300) containing the predicted amphipathic, α‐helical, transverse lipid‐associating domain ( M r 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.