CMY-42, a novel plasmid-mediated CMY-2 variant AmpC beta-lactamase.

Standard

CMY-42, a novel plasmid-mediated CMY-2 variant AmpC beta-lactamase. / Hentschke, Moritz; Kotsakis, Stathis D; Wolters, Manuel; Heisig, Peter; Miriagou, Vivi; Aepfelbacher, Martin.

In: MICROB DRUG RESIST, Vol. 17, No. 2, 2, 2011, p. 165-169.

Research output: SCORING: Contribution to journalSCORING: Journal articleResearchpeer-review

Harvard

APA

Vancouver

Bibtex

@article{00b39e4677fb48bc9ac465b4b05fbdc7,
title = "CMY-42, a novel plasmid-mediated CMY-2 variant AmpC beta-lactamase.",
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.",
keywords = "Humans, Molecular Sequence Data, Serine/genetics/metabolism, Anti-Bacterial Agents/*pharmacology, Cephalosporins/*pharmacology, Drug Resistance, Bacterial/drug effects/*genetics, *Escherichia coli/genetics/growth & development/isolation & purification, Escherichia coli Infections/drug therapy/genetics/*microbiology, Escherichia coli Proteins/*genetics/metabolism, Plasmids/*genetics/metabolism, Surgical Wound Infection/drug therapy/genetics/*microbiology, Valine/genetics/metabolism, beta-Lactamases/*genetics/metabolism, Humans, Molecular Sequence Data, Serine/genetics/metabolism, Anti-Bacterial Agents/*pharmacology, Cephalosporins/*pharmacology, Drug Resistance, Bacterial/drug effects/*genetics, *Escherichia coli/genetics/growth & development/isolation & purification, Escherichia coli Infections/drug therapy/genetics/*microbiology, Escherichia coli Proteins/*genetics/metabolism, Plasmids/*genetics/metabolism, Surgical Wound Infection/drug therapy/genetics/*microbiology, Valine/genetics/metabolism, beta-Lactamases/*genetics/metabolism",
author = "Moritz Hentschke and Kotsakis, {Stathis D} and Manuel Wolters and Peter Heisig and Vivi Miriagou and Martin Aepfelbacher",
year = "2011",
language = "English",
volume = "17",
pages = "165--169",
journal = "MICROB DRUG RESIST",
issn = "1076-6294",
publisher = "Mary Ann Liebert Inc.",
number = "2",

}

RIS

TY - JOUR

T1 - CMY-42, a novel plasmid-mediated CMY-2 variant AmpC beta-lactamase.

AU - Hentschke, Moritz

AU - Kotsakis, Stathis D

AU - Wolters, Manuel

AU - Heisig, Peter

AU - Miriagou, Vivi

AU - Aepfelbacher, Martin

PY - 2011

Y1 - 2011

N2 - 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.

AB - 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.

KW - Humans

KW - Molecular Sequence Data

KW - Serine/genetics/metabolism

KW - Anti-Bacterial Agents/pharmacology

KW - Cephalosporins/pharmacology

KW - Drug Resistance, Bacterial/drug effects/genetics

KW - Escherichia coli/genetics/growth & development/isolation & purification

KW - Escherichia coli Infections/drug therapy/genetics/microbiology

KW - Escherichia coli Proteins/genetics/metabolism

KW - Plasmids/genetics/metabolism

KW - Surgical Wound Infection/drug therapy/genetics/microbiology

KW - Valine/genetics/metabolism

KW - beta-Lactamases/genetics/metabolism

KW - Humans

KW - Molecular Sequence Data

KW - Serine/genetics/metabolism

KW - Anti-Bacterial Agents/pharmacology

KW - Cephalosporins/pharmacology

KW - Drug Resistance, Bacterial/drug effects/genetics

KW - Escherichia coli/genetics/growth & development/isolation & purification

KW - Escherichia coli Infections/drug therapy/genetics/microbiology

KW - Escherichia coli Proteins/genetics/metabolism

KW - Plasmids/genetics/metabolism

KW - Surgical Wound Infection/drug therapy/genetics/microbiology

KW - Valine/genetics/metabolism

KW - beta-Lactamases/genetics/metabolism

M3 - SCORING: Journal article

VL - 17

SP - 165

EP - 169

JO - MICROB DRUG RESIST

JF - MICROB DRUG RESIST

SN - 1076-6294

IS - 2

M1 - 2

ER -