Abstract
We isolated a clinical Escherichia coli strain with an antimicrobial resistance phenotype characteristic for the expression of an AmpC beta-lactamase. Molecular methods revealed a novel, plasmid-localized variant of CMY-2 with a substitution of valine 231 for serine (V231S), which was designated CMY-42. Like the CMY-2-like AmpC beta-lactamase CMY-30, carrying the substitution V231G, CMY-42 displayed increased activity toward expanded spectrum cephalosporins. This finding supports the hypothesis that a bulky side chain at position 231 (Ambler's position 211) may pose a steric clash with certain cephalosporins hindering the access of the AmpC beta-lactamase; however, additional phenomena may account for the observed hydrolytic properties.
MeSH terms
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Anti-Bacterial Agents / pharmacology*
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Cephalosporins / pharmacology*
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Drug Resistance, Bacterial / drug effects
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Drug Resistance, Bacterial / genetics*
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Escherichia coli Infections / drug therapy
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Escherichia coli Infections / genetics
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Escherichia coli Infections / microbiology*
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Escherichia coli Proteins / genetics*
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Escherichia coli Proteins / metabolism
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Escherichia coli* / genetics
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Escherichia coli* / growth & development
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Escherichia coli* / isolation & purification
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Humans
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Molecular Sequence Data
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Plasmids / genetics*
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Plasmids / metabolism
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Serine / genetics
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Serine / metabolism
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Surgical Wound Infection / drug therapy
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Surgical Wound Infection / genetics
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Surgical Wound Infection / microbiology*
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Valine / genetics
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Valine / metabolism
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beta-Lactamases / genetics*
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beta-Lactamases / metabolism
Substances
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Anti-Bacterial Agents
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Cephalosporins
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Escherichia coli Proteins
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Serine
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beta-lactamase CMY-2
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beta-Lactamases
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beta-lactamase CMY-42, E coli
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Valine