Neisseria gonorrhoeae IgA1 proteases share epitopes recognized by neutralizing antibodies.

The antigenic diversity among IgA1 proteases of 61 Neisseria gonorrhoeae strains isolated during a period of 23 years and on four continents was examined in enzyme neutralization assays employing rabbit antisera raised against selected IgA1 proteases. The antigenic analyses were compared with results of iga gene-region RFLP patterns and enzyme cleavage specificity for substrate IgA1. Type 1 IgA1 proteases were antigenically uniform while six different antigenic types were detected among type 2 enzymes. Extensive cross-reactions of antibodies against the different antigenic types suggested only minor differences in relevant epitopes. Epitopes previously found to be common to all Neisseria meningitidis IgA1 proteases were also shared by all N. gonorrhoeae IgA1 proteases in the collection. Human sera from patients with gonorrhoea showed broadly cross-reactive neutralizing activity at titers comparable to those of sera from immunized rabbits. In conclusion, N. gonorrhoeae IgA1 proteases show a remarkable lack of diversity of epitopes recognized by enzyme-neutralizing antibodies. If future studies confirm that cleavage of IgA1 is an important step in gonococcal infections, Neisseria IgA1 proteases may be attractive vaccine candidates.