Abstract
Phosphoethanolamine (PEA) decoration of lipid A produced by Neisseria gonorrhoeae has been linked to bacterial resistance to cationic antimicrobial peptides/proteins (CAMPs) and in vivo fitness during experimental infection. We now report that the lptA gene, which encodes the PEA transferase responsible for this decoration, is in an operon and that high-frequency mutation in a polynucleotide repeat within lptA can influence gonococcal resistance to CAMPs.
Copyright © 2014, American Society for Microbiology. All Rights Reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Anti-Bacterial Agents / pharmacology
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Antimicrobial Cationic Peptides / pharmacology*
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Base Sequence
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Drug Resistance, Bacterial / genetics
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Ethanolaminephosphotransferase / biosynthesis
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Ethanolaminephosphotransferase / genetics*
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Ethanolamines / chemistry*
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Lipid A / chemistry*
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Microbial Sensitivity Tests
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Neisseria gonorrhoeae / drug effects*
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Neisseria gonorrhoeae / genetics
Substances
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Anti-Bacterial Agents
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Antimicrobial Cationic Peptides
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Ethanolamines
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Lipid A
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phosphorylethanolamine
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Ethanolaminephosphotransferase