Abstract
The FrpB protein from pathogenic neisseriae is a 77 kDa iron-regulated outer-membrane protein that belongs to the family of TonB-dependent receptors and may have potential as a vaccine component. Comparison between the frpB gene from three different meningococcal strains and a published gonococcal one revealed that the region from residues 350 to 390 displays pronounced sequence variability. In a model for the topology of FrpB in the outer membrane, this region corresponds to loop 7, the longest of the predicted 13 surface-exposed loops. Binding of four out of a total of eight bactericidal monoclonal antibodies to synthetic peptides corresponding to loop 7 showed that their epitopes are located here. The frpB genes from five additional meningococcal strains were cloned and sequenced in this region. Pairwise comparisons showed different degrees of similarity.
MeSH terms
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Amino Acid Sequence
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Antibodies, Monoclonal
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Bacterial Outer Membrane Proteins / chemistry
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Bacterial Outer Membrane Proteins / genetics*
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Bacterial Outer Membrane Proteins / immunology
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Epitopes / chemistry
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Epitopes / genetics
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Genetic Variation
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Humans
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Molecular Sequence Data
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Neisseria / chemistry
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Neisseria / genetics*
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Neisseria / pathogenicity
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Neisseria gonorrhoeae / chemistry
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Neisseria gonorrhoeae / genetics
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Neisseria gonorrhoeae / pathogenicity
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Neisseria meningitidis / chemistry
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Neisseria meningitidis / genetics
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Neisseria meningitidis / pathogenicity
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Protein Structure, Secondary
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Sequence Homology, Amino Acid
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Species Specificity
Substances
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Antibodies, Monoclonal
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Bacterial Outer Membrane Proteins
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Epitopes
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FrpB protein, bacteria
Associated data
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GENBANK/U55377
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GENBANK/U55378
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GENBANK/U67310
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GENBANK/U67311
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GENBANK/U67312
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GENBANK/U67313
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GENBANK/U67314