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Permeabilization of the plasma membrane by deletion mutants of diphtheria toxin.
Author(s) -
Stenmark H.,
McGill S.,
Olsnes S.,
Sandvig K.
Publication year - 1989
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1989.tb08432.x
Subject(s) - norwegian , radium , diphtheria toxin , cancer , library science , biology , medicine , microbiology and biotechnology , toxin , philosophy , physics , linguistics , computer science , nuclear physics
Diphtheria toxin B‐fragment binds to cell‐surface receptors and facilitates translocation of the enzymatically active A‐fragment to the cytosol. In this process the B‐fragment inserts into the plasma membrane and induces formation of cation‐selective channels. We examined the ability of a number of diphtheria toxin‐derived molecules translated in vitro to permeabilize cells. Two proteins consisting of the whole B‐fragment and small parts of the A‐fragment, and one protein comprising most of the B‐fragment alone, were more efficient than full‐length toxin in permeabilizing the plasma membrane to monovalent cations. Two shorter B‐fragment‐derived proteins, with 3 and 10 kd N‐terminal deletions, permeabilized the cells to sulfate and sucrose in addition to monovalent cations. The relationship between channel formation and toxin translocation is discussed.