Dimer dissociation of the pore-forming toxin aerolysin precedes receptor binding

The pore-forming toxin aerolysin is secreted by Aeromonas hydrophila as an inactive precursor. Based on chemical cross-linking and gel filtration, we show here that proaerolysin exists as a monomer at low concentrations but is dimeric above 0.1 mg/ml. At intermediate concentrations, monomers and dimers appeared to be in rapid equilibrium. All together our data indicate that, at low concentrations, the toxin is a monomer and that this species is competent for receptor binding. In contrast, a mutant toxin that forms a covalent dimer was unable to bind to target cells.


Published in:
J Biol Chem, 274, 53, 37705-8
Year:
1999
Keywords:
Note:
Department of Biochemistry, University of Geneva, 30 quai E. Ansermet, 1211 Geneva, Switzerland.
Laboratories:




 Record created 2009-01-30, last modified 2018-03-17


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