This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Nakano, R.
Right arrow Articles by Inoue, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nakano, R.
Right arrow Articles by Inoue, M.

 Previous Article  |  Next Article 

Antimicrobial Agents and Chemotherapy, April 2004, p. 1151-1158, Vol. 48, No. 4
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.4.1151-1158.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

CFE-1, a Novel Plasmid-Encoded AmpC ß-Lactamase with an ampR Gene Originating from Citrobacter freundii

Ryuichi Nakano,1 Ryoichi Okamoto,1 Yumiko Nakano,1 Kenichi Kaneko,1 Naohiro Okitsu,1,2 Yoshio Hosaka,1 and Matsuhisa Inoue1*

Department of Microbiology, School of Medicine and Environmental Infectious Disease, Graduate School of Medical Sciences, Kitasato University, Sagamihara, Kanagawa,1 Department of Otolaryngology, Tohoku University School of Medicine, Sendai, Japan2

Received 13 May 2003/ Returned for modification 1 September 2003/ Accepted 30 December 2003

A clinical isolate of Escherichia coli from a patient in Japan, isolate KU6400, was found to produce a plasmid-encoded ß-lactamase that conferred resistance to extended-spectrum cephalosporins and cephamycins. Resistance arising from production of a ß-lactamase could be transferred by either conjugation or transformation with plasmid pKU601 into E. coli ML4947. The substrate and inhibition profiles of this enzyme resembled those of the AmpC ß-lactamase. The resistance gene of pKU601, which was cloned and expressed in E. coli, proved to contain an open reading frame showing 99.8% DNA sequence identity with the ampC gene of Citrobacter freundii GC3. DNA sequence analysis also identified a gene upstream of ampC whose sequence was 99.0% identical to the ampR gene from C. freundii GC3. In addition, a fumarate operon (frdABCD) and an outer membrane lipoprotein (blc) surrounding the ampR-ampC genes in C. freundii were identified, and insertion sequence (IS26) elements were observed on both sides of the sequences identified (forming an IS26 composite transposon); these results confirm the evidence of the translocation of a ß-lactamase-associated gene region from the chromosome to a plasmid. Finally, we describe a novel plasmid-encoded AmpC ß-lactamase, CFE-1, with an ampR gene derived from C. freundii.

* Corresponding author. Mailing address: Department of Microbiology, School of Medicine and Environmental Infectious Disease, Graduate School of Medical Sciences, Kitasato University, Sagamihara 1-15-1, Kanagawa 228-8555, Japan. Phone: 81-42-778-9349. Fax: 81-42-778-9350. E-mail: matsu{at}kitasato-u.ac.jp.

Antimicrobial Agents and Chemotherapy, April 2004, p. 1151-1158, Vol. 48, No. 4
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.4.1151-1158.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Jacoby, G. A. (2009). AmpC {beta}-Lactamases. Clin. Microbiol. Rev. 22: 161-182 [Abstract] [Full Text]  
  • Stubbs, K. A., Balcewich, M., Mark, B. L., Vocadlo, D. J. (2007). Small Molecule Inhibitors of a Glycoside Hydrolase Attenuate Inducible AmpC-mediated beta-Lactam Resistance. J. Biol. Chem. 282: 21382-21391 [Abstract] [Full Text]  
  • Zienkiewicz, M., Kern-Zdanowicz, I., Golebiewski, M., Zylinska, J., Mieczkowski, P., Gniadkowski, M., Bardowski, J., Ceglowski, P. (2007). Mosaic Structure of p1658/97, a 125-Kilobase Plasmid Harboring an Active Amplicon with the Extended-Spectrum {beta}-Lactamase Gene blaSHV-5. Antimicrob. Agents Chemother. 51: 1164-1171 [Abstract] [Full Text]  
  • Schmidtke, A. J., Hanson, N. D. (2006). Model System To Evaluate the Effect of ampD Mutations on AmpC-Mediated {beta}-Lactam Resistance.. Antimicrob. Agents Chemother. 50: 2030-2037 [Abstract] [Full Text]  
  • Jacoby, G. A. (2006). {beta}-Lactamase Nomenclature.. Antimicrob. Agents Chemother. 50: 1123-1129 [Full Text]  
  • Wachino, J.-i., Kurokawa, H., Suzuki, S., Yamane, K., Shibata, N., Kimura, K., Ike, Y., Arakawa, Y. (2006). Horizontal Transfer of blaCMY-Bearing Plasmids among Clinical Escherichia coli and Klebsiella pneumoniae Isolates and Emergence of Cefepime-Hydrolyzing CMY-19. Antimicrob. Agents Chemother. 50: 534-541 [Abstract] [Full Text]  
  • Verdet, C., Benzerara, Y., Gautier, V., Adam, O., Ould-Hocine, Z., Arlet, G. (2006). Emergence of DHA-1-Producing Klebsiella spp. in the Parisian Region: Genetic Organization of the ampC and ampR Genes Originating from Morganella morganii. Antimicrob. Agents Chemother. 50: 607-617 [Abstract] [Full Text]  
  • D'Andrea, M. M., Nucleo, E., Luzzaro, F., Giani, T., Migliavacca, R., Vailati, F., Kroumova, V., Pagani, L., Rossolini, G. M. (2006). CMY-16, a Novel Acquired AmpC-Type {beta}-Lactamase of the CMY/LAT Lineage in Multifocal Monophyletic Isolates of Proteus mirabilis from Northern Italy. Antimicrob. Agents Chemother. 50: 618-624 [Abstract] [Full Text]  
  • Wei, Z.-Q., Chen, Y.-G., Yu, Y.-S., Lu, W.-X., Li, L.-J. (2005). Nosocomial spread of multi-resistant Klebsiella pneumoniae containing a plasmid encoding multiple {beta}-lactamases. J Med Microbiol 54: 885-888 [Abstract] [Full Text]  
  • Kaneko, K., Okamoto, R., Nakano, R., Kawakami, S., Inoue, M. (2005). Gene Mutations Responsible for Overexpression of AmpC {beta}-Lactamase in Some Clinical Isolates of Enterobacter cloacae. J. Clin. Microbiol. 43: 2955-2958 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»