Abstract
The 125I-labeled tryptic peptides of the outer membrane protein I of 33 previously characterized serological reference strains of Neisseria gonorrhoeae were investigated by peptide maps in relation to their coagglutination W serogroup. Serogroup WI strains tended to have lower-molecular-weight protein I molecules than did WII strains, and WIII strains had the highest-molecular-weight protein I molecules, although the serogroup could not be predicted from the molecular weights of the protein I molecules for a given strain. All 13 strains belonging to serogroup WI were found to have 11 peptides in common, as judged by their migration with respect to one another and to the internal marker valine in the peptide maps. Common peptides isolated from a given strain were found to comigrate with the corresponding common peptides from other strains in the same serogroup under various electrophoretic conditions. The 20 strains belonging to serogroups WII and WIII were all found to have 10 common peptides by the same criteria. When common peptides from serogroup WI were compared with the common peptides of serogroups WII and WIII, only three of these peptides appeared to be similar. Thus, two different outer membrane protein I molecules seem to exist which are mutually exclusive. Protein IA molecules contain the antigens recognized as serogroup WI, and protein IB molecules contain the antigens that characterize serogroups WII and WIII.