The ACT-1 plasmid-encoded AmpC β-lactamase is inducible: Detection in a complex β-lactamase background

Mark D. Reisbig; Nancy D. Hanson

The ACT-1 plasmid-encoded AmpC β-lactamase is inducible: Detection in a complex β-lactamase background

Research output: Contribution to journal › Article › peer-review

Abstract

The purpose of this study was to identify the genetic organization and inducibility of bla_ACT-1 in a clinical isolate of Klebsiella pneumoniae possessing at least five different β-lactamases. The genetic organization of the bla_ACT-1lampR region is identical to those of inducible chromosomal ampC genes. RNA analysis using primer extension demonstrated a five-fold increase in bla_ACT-1 transcript production on exposure to cefoxitin. These findings are significant because induction was detected in a complicated β-lactamase background. In addition, this report is the first to describe an inducible plasmid-encoded AmpC β-lactamase of Enterobacter cloacae origin.

Original language	English (US)
Pages (from-to)	557-560
Number of pages	4
Journal	Journal of Antimicrobial Chemotherapy
Volume	49
Issue number	3
State	Published - 2002

All Science Journal Classification (ASJC) codes

Pharmacology
Microbiology (medical)
Infectious Diseases
Pharmacology (medical)

Fingerprint Dive into the research topics of 'The ACT-1 plasmid-encoded AmpC β-lactamase is inducible: Detection in a complex β-lactamase background'. Together they form a unique fingerprint.

Cite this

@article{6d5e5d6e095a4b81b214231bcf60f6be,

title = "The ACT-1 plasmid-encoded AmpC β-lactamase is inducible: Detection in a complex β-lactamase background",

abstract = "The purpose of this study was to identify the genetic organization and inducibility of blaACT-1 in a clinical isolate of Klebsiella pneumoniae possessing at least five different β-lactamases. The genetic organization of the blaACT-1lampR region is identical to those of inducible chromosomal ampC genes. RNA analysis using primer extension demonstrated a five-fold increase in blaACT-1 transcript production on exposure to cefoxitin. These findings are significant because induction was detected in a complicated β-lactamase background. In addition, this report is the first to describe an inducible plasmid-encoded AmpC β-lactamase of Enterobacter cloacae origin.",

author = "Reisbig, {Mark D.} and Hanson, {Nancy D.}",

year = "2002",

language = "English (US)",

volume = "49",

pages = "557--560",

journal = "Journal of Antimicrobial Chemotherapy",

issn = "0305-7453",

publisher = "Oxford University Press",

number = "3",

}

TY - JOUR

T1 - The ACT-1 plasmid-encoded AmpC β-lactamase is inducible

T2 - Detection in a complex β-lactamase background

AU - Reisbig, Mark D.

AU - Hanson, Nancy D.

PY - 2002

Y1 - 2002

N2 - The purpose of this study was to identify the genetic organization and inducibility of blaACT-1 in a clinical isolate of Klebsiella pneumoniae possessing at least five different β-lactamases. The genetic organization of the blaACT-1lampR region is identical to those of inducible chromosomal ampC genes. RNA analysis using primer extension demonstrated a five-fold increase in blaACT-1 transcript production on exposure to cefoxitin. These findings are significant because induction was detected in a complicated β-lactamase background. In addition, this report is the first to describe an inducible plasmid-encoded AmpC β-lactamase of Enterobacter cloacae origin.

AB - The purpose of this study was to identify the genetic organization and inducibility of blaACT-1 in a clinical isolate of Klebsiella pneumoniae possessing at least five different β-lactamases. The genetic organization of the blaACT-1lampR region is identical to those of inducible chromosomal ampC genes. RNA analysis using primer extension demonstrated a five-fold increase in blaACT-1 transcript production on exposure to cefoxitin. These findings are significant because induction was detected in a complicated β-lactamase background. In addition, this report is the first to describe an inducible plasmid-encoded AmpC β-lactamase of Enterobacter cloacae origin.

UR - http://www.scopus.com/inward/record.url?scp=0036118955&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036118955&partnerID=8YFLogxK

M3 - Article

C2 - 11864960

AN - SCOPUS:0036118955

VL - 49

SP - 557

EP - 560

JO - Journal of Antimicrobial Chemotherapy

JF - Journal of Antimicrobial Chemotherapy

SN - 0305-7453

IS - 3

ER -