000133492 001__ 133492 000133492 005__ 20190527135626.0 000133492 0247_ $$2doi$$a10.1074/jbc.274.53.37705 000133492 037__ $$aARTICLE 000133492 245__ $$aDimer dissociation of the pore-forming toxin aerolysin precedes receptor binding 000133492 269__ $$a1999 000133492 260__ $$c1999 000133492 336__ $$aJournal Articles 000133492 500__ $$aDepartment of Biochemistry, University of Geneva, 30 quai E. Ansermet, 1211 Geneva, Switzerland. 000133492 520__ $$aThe pore-forming toxin aerolysin is secreted by Aeromonas hydrophila as an inactive precursor. Based on chemical cross-linking and gel filtration, we show here that proaerolysin exists as a monomer at low concentrations but is dimeric above 0.1 mg/ml. At intermediate concentrations, monomers and dimers appeared to be in rapid equilibrium. All together our data indicate that, at low concentrations, the toxin is a monomer and that this species is competent for receptor binding. In contrast, a mutant toxin that forms a covalent dimer was unable to bind to target cells. 000133492 6531_ $$aAnimals 000133492 6531_ $$aBacterial Toxins/*chemistry/genetics/*metabolism 000133492 6531_ $$aCell Line 000133492 6531_ $$aChromatography 000133492 6531_ $$aGel 000133492 6531_ $$aCricetinae 000133492 6531_ $$aCross-Linking Reagents 000133492 6531_ $$aDimerization 000133492 6531_ $$aMutation 000133492 6531_ $$aPore Forming Cytotoxic Proteins 000133492 6531_ $$aReceptors 000133492 6531_ $$aCell Surface/*metabolism 000133492 700__ $$aFivaz, M. 000133492 700__ $$aVelluz, M. C. 000133492 700__ $$0240085$$g171549$$avan der Goot, F. G. 000133492 773__ $$j274$$tJournal of Biological Chemistry$$k53$$q37705-8 000133492 909C0 $$xU11271$$0252037$$pVDG 000133492 909CO $$pSV$$particle$$ooai:infoscience.tind.io:133492 000133492 937__ $$aVDG-ARTICLE-1999-007 000133492 973__ $$rREVIEWED$$sPUBLISHED$$aOTHER 000133492 980__ $$aARTICLE