000133492 001__ 133492
000133492 005__ 20181203021432.0
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$$avan der Goot, F. G.$$g171549
000133492 773__ $$j274$$k53$$q37705-8$$tJ Biol Chem
000133492 909C0 $$0252037$$pVDG$$xU11271
000133492 909CO $$ooai:infoscience.tind.io:133492$$pSV$$particle
000133492 937__ $$aVDG-ARTICLE-1999-007
000133492 973__ $$aOTHER$$rREVIEWED$$sPUBLISHED
000133492 980__ $$aARTICLE