Abstract
The swine pathogen Actinobacillus pleuropneumoniae possesses a 75-kDa outer membrane protein (OMP), FhuA, the receptor for ferrichrome, a hydroxamate-type siderophore. Polyclonal serum to FhuA reacted with OMP preparations from 12 serotypes of A. pleuropneumoniae under conditions of iron repletion and restriction. Reverse transcription-PCR confirmed that A. pleuropneumoniae fhuA expression is not upregulated in response to low iron levels. An A. pleuropneumoniae fhuA deletion mutant was generated and showed abolishment of ferrichrome uptake.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actinobacillus pleuropneumoniae / chemistry
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Actinobacillus pleuropneumoniae / genetics*
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Animals
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Bacterial Outer Membrane Proteins / analysis
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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 / physiology
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / genetics*
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Escherichia coli Proteins / physiology
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Ferrichrome / metabolism*
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Gene Expression Regulation, Bacterial
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Iron / pharmacology*
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Male
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Molecular Weight
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Rabbits
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Receptors, Virus / chemistry
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Receptors, Virus / genetics*
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Receptors, Virus / physiology
Substances
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Bacterial Outer Membrane Proteins
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Escherichia coli Proteins
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FhuA protein, E coli
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Receptors, Virus
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Ferrichrome
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Iron