Résumé : A monoclonal antibody was used to characterize a serogroup 1 specific Legionella pneumophila Philadelphia strain 1 antigenic determinant. A quantitative fluorometric assay was developed to quantitate the antibody binding sites (2.7 ± 0.4 × 105) on Legionella bacteria and to determine the physico-chemical parameters of the antibody-antigen interaction (at 4°C: ΔG = -10.9Kcal × mol-1, ΔH = 1.7Kcal × mol-1, ΔS = 45cal × K-1 × mol-1). The same method was used to study the modification or the removal of the antigen by chemical and enzymatic means (trypsin, papain, lysozyme, acetone, chloroform-methanol and Tris-EDTA); only Tris-EDTA extraction resulted in a significant decrease in antibody binding sites. Inhibition studies of the fluorescein-labelled antibody binding were performed with different sugars of which only l-fucosylamine was inhibitory, and with other monoclonal antibodies to Legionella pneumophila serogroup 1 in order to compare their fine specificity and affinity. The results indicate that the epitope recognized was an immunodominant carbohydrate including an aminodideoxyhexose and carried by the lipopolysaccharide. © 1987.