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 journal › SCORING: Journal article › Research › peer-review
Harvard
APA
Vancouver
Bibtex
}
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 -