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The sequence diversity of 45 Opa outer membrane proteins fromNeisseria meningitidis ,Neisseria gonorrhoeae ,Neisseria sicca , andNeisseria flava indicates that horizontal genetic exchange ofopa alleles has been rare between these species. A two-dimensional structural model containing four surface-exposed loops was constructed based on rules derived from porin crystal structure and on conservation of sequence homology within transmembrane β-strands. The minimal continuous epitopes recognized by 23 monoclonal antibodies were mapped to loops 2 and 3. Some of these epitopes are localized on the bacterial cell surface, in support of the model.

Sequence Diversity, Predicted Two-Dimensional Protein Structure, and Epitope Mapping of Neisserial Opa Proteins