Abstract
The major outer membrane protein (MOMP), or protein 1, of Neisseria gonorrhoeae is one of the immunodominant proteins of the gonococcal cell surface. It is at least partially responsible for imparting serotyping specificity. This study attempted to compare the primary structure of MOMP molecules isolated from several gonococcal strains by preparative polyacrylamide gel electrophoresis. These isolated proteins were then subjected to enzymatic digestion with staphylococcal V8 protease and alpha-chymotrypsin. The generated peptides were separated by polyacrylamide gradient gel electrophoresis in the presence of sodium dodecyl sulfate. Of the eight strains analyzed, six exhibited distinct peptide maps after either staphylococcal V8 protease or alpha-chymotrypsin digestion. These six strains have also been shown to be immunologically distinct. The data suggest that the gene pool coding for the MOMP is diverse and reflect the complexity of the evolution of N. gonorrhoeae.