» Articles » PMID: 2479538

Permeabilization of the Plasma Membrane by Deletion Mutants of Diphtheria Toxin

Overview
Journal EMBO J
Date 1989 Oct 1
PMID 2479538
Citations 6
Authors
Affiliations
Soon will be listed here.
Abstract

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.

Citing Articles

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

Lanzrein M, Sand O, Olsnes S EMBO J. 1996; 15(4):725-34.

PMID: 8631294 PMC: 450271.


Protein toxins acting on intracellular targets: cellular uptake and translocation to the cytosol.

Olsnes S, van Deurs B, Sandvig K Med Microbiol Immunol. 1993; 182(2):51-61.

PMID: 8392658 DOI: 10.1007/BF00189373.


Subcloning and characterization of the binding domain of fragment B of diphtheria toxin.

Esbensen Q, Falnes P, Olsnes S, Madshus I Biochem J. 1993; 294 ( Pt 3):663-6.

PMID: 8379922 PMC: 1134513. DOI: 10.1042/bj2940663.


Diphtheria toxin endocytosis and membrane translocation are dependent on the intact membrane-anchored receptor (HB-EGF precursor): studies on the cell-associated receptor cleaved by a metalloprotease in phorbol-ester-treated cells.

Lanzrein M, Garred O, Olsnes S, Sandvig K Biochem J. 1995; 310 ( Pt 1):285-9.

PMID: 7646457 PMC: 1135885. DOI: 10.1042/bj3100285.


Membrane interactions of diphtheria toxin analyzed using in vitro synthesized mutants.

McGill S, Stenmark H, Sandvig K, Olsnes S EMBO J. 1989; 8(10):2843-8.

PMID: 2684631 PMC: 401336. DOI: 10.1002/j.1460-2075.1989.tb08431.x.


References
1.
Papini E, Schiavo G, Tomasi M, Colombatti M, Rappuoli R, Montecucco C . Lipid interaction of diphtheria toxin and mutants with altered fragment B. 2. Hydrophobic photolabelling and cell intoxication. Eur J Biochem. 1987; 169(3):637-44. DOI: 10.1111/j.1432-1033.1987.tb13655.x. View

2.
McGill S, Stenmark H, Sandvig K, Olsnes S . Membrane interactions of diphtheria toxin analyzed using in vitro synthesized mutants. EMBO J. 1989; 8(10):2843-8. PMC: 401336. DOI: 10.1002/j.1460-2075.1989.tb08431.x. View

3.
Moskaug J, Sandvig K, Olsnes S . Low pH-induced release of diphtheria toxin A-fragment in Vero cells. Biochemical evidence for transfer to the cytosol. J Biol Chem. 1988; 263(5):2518-25. View

4.
Sandvig K, Olsnes S . Diphtheria toxin-induced channels in Vero cells selective for monovalent cations. J Biol Chem. 1988; 263(25):12352-9. View

5.
Stenmark H, Olsnes S, Sandvig K . Requirement of specific receptors for efficient translocation of diphtheria toxin A fragment across the plasma membrane. J Biol Chem. 1988; 263(26):13449-55. View