Abstract
We identified lbpB, encoding the lipoprotein component of the meningococcal lactoferrin receptor. An LbpB mutant was unable to acquire Fe from lactoferrin and exhibits decreased surface binding to lactoferrin. Primer extension and reverse transcription-PCR analysis indicate that lbpB and lbpA are cotranscribed on a polycistronic Fe-repressible mRNA.
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 Proteins / biosynthesis
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Bacterial Proteins / genetics*
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Base Sequence
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Carrier Proteins / genetics
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Cloning, Molecular
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Gene Expression Regulation, Bacterial
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Genes, Bacterial
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Iron / metabolism
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Iron-Binding Proteins
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Lactoferrin / metabolism*
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Lipoproteins / biosynthesis
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Lipoproteins / genetics*
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Molecular Sequence Data
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Mutagenesis
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Neisseria meningitidis / genetics*
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RNA, Bacterial / biosynthesis
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RNA, Messenger / biosynthesis
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Receptors, Cell Surface / genetics*
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Sequence Analysis, DNA
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Transcription, Genetic
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Transferrin-Binding Proteins
Substances
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Bacterial Outer Membrane Proteins
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Bacterial Proteins
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Carrier Proteins
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Iron-Binding Proteins
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LBPA protein, Neisseria meningitidis
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Lipoproteins
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RNA, Bacterial
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RNA, Messenger
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Receptors, Cell Surface
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Transferrin-Binding Proteins
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Iron
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Lactoferrin