Abstract
We cloned lbpB, encoding a predicted 80-kDa lipoprotein, upstream of lbpA. A nonpolar mutant (LbpB- LbpA+) had normal lactoferrin (LF) binding and grew normally with LF as an iron source, whereas LbpB- LbpA- and LbpB+ LbpA- strains had reduced binding of LF and did not grow with LF as an iron source. LbpB bound LF directly in an affinity purification, suggesting that LbpB might play a still-uncharacterized role in the LF iron utilization.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Bacterial Outer Membrane Proteins / genetics*
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Bacterial Outer Membrane Proteins / isolation & purification
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Bacterial Outer Membrane Proteins / metabolism
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Chromatography, Affinity
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Cloning, Molecular
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Genes, Bacterial / physiology*
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Iron / metabolism
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Lactoferrin / metabolism*
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Molecular Sequence Data
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Neisseria gonorrhoeae / genetics*
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Neisseria gonorrhoeae / physiology
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Receptors, Cell Surface / genetics*
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Receptors, Cell Surface / isolation & purification
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Receptors, Cell Surface / metabolism
Substances
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Bacterial Outer Membrane Proteins
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LBPA protein, Neisseria meningitidis
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Receptors, Cell Surface
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Iron
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Lactoferrin