Affinities of endotoxin-specific human monoclonal antibodies, their polyclonal counterparts and murine monoclonal antibodies.
Affinity as a measurement of the strength of binding is a crucial factor in biological significance. In general, high-affinity antibodies are most effective in mediating immunological effector mechanisms. Here, we compare the affinity distributions of corresponding polyclonal and monoclonal human antibodies specific for lipopolysaccharide determinants of the nosocomial pathogen Pseudomonas aeruginosa. The affinities of the 14 human mAb analysed ranged from 8.3 x 10(5) to 7.5 x 10(8). The average affinities of their polyclonal counterparts, assessed by analysing chromatographically separated antibody populations, ranged from 1.7 x 10(6) to 6.3 x 10(7). Furthermore, the affinities of murine mAb of the same specificity ranged from 3.7 x 10(5) to 1.4 x 10(7). These results suggest that the generated human monoclonal anti-carbohydrate antibodies exhibit affinities comparable to or higher than those of their human polyclonal counterparts and those of murine mAb of the same specificity.
Bruderer
U
U
Swiss Serum and Vaccine Institute, Berne.
Deusinger
M
M
Schürch
U
U
Lang
A B
AB
D000818:Animals; D000906:Antibodies / Q000276:immunology; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000915:Antibody Affinity / Q000276:immunology*; D004731:Endotoxins / Q000276:immunology*; D006801:Humans; D008070:Lipopolysaccharides / Q000276:immunology; D051379:Mice
D000906:Antibodies; D000911:Antibodies, Monoclonal; D004731:Endotoxins; D008070:Lipopolysaccharides