Abstract
The sequence diversity of 45 Opa outer membrane proteins from Neisseria meningitidis, Neisseria gonorrhoeae, Neisseria sicca, and Neisseria flava indicates that horizontal genetic exchange of opa 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 beta-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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Antibodies, Bacterial / immunology
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Antibodies, Monoclonal / immunology
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Antigens, Bacterial / chemistry*
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Antigens, Bacterial / immunology
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Bacterial Outer Membrane Proteins / chemistry*
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Bacterial Outer Membrane Proteins / immunology
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Epitope Mapping*
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Molecular Sequence Data
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Neisseria / chemistry*
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Neisseria gonorrhoeae / chemistry
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Neisseria meningitidis / chemistry
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Protein Structure, Secondary
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Species Specificity
Substances
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Antibodies, Bacterial
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Antibodies, Monoclonal
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Antigens, Bacterial
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Bacterial Outer Membrane Proteins
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opacity proteins
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Opa protein, Neisseria
Associated data
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GENBANK/AF016285
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GENBANK/AF016286
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GENBANK/AF016287
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GENBANK/AF016288
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GENBANK/AF016289
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GENBANK/AF016290
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GENBANK/AF016291
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GENBANK/AF016292