Quantitative analysis of the binding and oligomerization of staphylococcal alpha-toxin in target erythrocyte membranes.

摘要: The binding of staphylococcal alpha-toxin to rabbit and human erythrocytes was quantitated over a wide range toxin concentrations (3 x 10(-11) 3 10(-6) M) with the use an enzyme-linked immunosorbent assay that permitted simultaneous quantitation monomeric oligomeric forms. Three basic observations were made. First, in no did display characteristics receptor-ligand interaction. Net cells nil at sublytic (10(-10) M or ng/ml). onset occurred around 10 ng/ml remained fairly constant ineffective (5 8% offered) concentration (up micrograms/ml). Second, hemolysis 37 degrees C always accompanied by formation oligomers membrane. Third, overall 0 degree followed pattern similar C. However, oligomer cell lysis retarded (but not totally inhibited) When incubated low levels (0.5 microgram/ml) for 30 min, became bound exclusively monomer form, occurred. thus treated washed suspended C, rapidly ensued, native replaced toxin. collective results directly support pore concept action also indicate form lateral aggregation monomers bilayer. They speak against existence specific sites on erythrocytes.