Dissemination of Transferable AmpC-type β-Lactamase (CMY-10) in a Korean Hospital

Lee, Jung Hun; Jung, Ho Sang; Jung, Jee‐Hoon; Park, Jin Seo; Ahn, Jun Bae; Jeong, Seok Hoon; Jeong, Byeong Chul; Lee, Sangeun

doi:10.1089/mdr.2004.10.224

Cited by 17 publications

(3 citation statements)

References 16 publications

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“…They are mainly chromosomal class C β-lactamases in several potential pathogens, such as Acinetobacter spp., Aeromonas spp., Chromobacterium violaceum , Citrobacter spp., Enterobacter spp., Escherichia coli , Morganella spp., Proteus rettgeri , P. aeruginosa , Serratia spp., and Yersinia enterocolitica [64,65]. In addition, the plasmid-encoded class C β-lactamases have been reported in K. pneumoniae (CMY-1, CMY-2, CMY-8, CMY-12, MOX-1, MOX-2, FOX-1, FOX-5, LAT-1, LAT-2, LAT-2b, ACT-1, MIR-1, ACC-1, ACT-3, DHA-2, and DHA-3), Klebsiella oxytoca (CMY-5 and FOX-3), E. coli (CMY-4, CMY-6, CMY-7, CMY-9, CMY-11, CMY-13, FOX-2, FOX-4, B1L-1, LAT-3, LAT-4, ACC-4, and DHA-6), Salmonella enteritidis (DHA-1), Proteus mirabilis (CMY-3, CMY-12, CMY-14, and CMY-15), Salmonella senftenberg (CMY-2b), Enterobacter aerogenes K9911729 (CMY-10), Pantoea agglomerans (ACT-9), S. marcescens (ACT-10), and E. cloacae (DHA-7) [8,9,10,11,64,66,67,68,69,70,71,72,73,74,75,76,77,78]. Compared with chromosomal enzymes, plasmid-encoded class C β-lactamases are more problematic because they are transmissible to other bacterial species and are often expressed in large amounts [79].…”

Section: Non-metallo-carbapenemases: Zinc-independent Classes a Cmentioning

confidence: 99%

“…Compared with chromosomal enzymes, plasmid-encoded class C β-lactamases are more problematic because they are transmissible to other bacterial species and are often expressed in large amounts [79]. Recently, five class C carbapenemases (namely ACT-1, DHA-1, CMY-2, CMY-10, and ADC-68) have been reported [9,11,12,66]. ACT-1, DHA-1, CMY-2, and CMY-10 are plasmid-encoded class C β-lactamases that exhibit catalytic activity for imipenem [8,80].…”

Section: Non-metallo-carbapenemases: Zinc-independent Classes a Cmentioning

confidence: 99%

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Structural Basis for Carbapenem-Hydrolyzing Mechanisms of Carbapenemases Conferring Antibiotic Resistance

Jeon

Lee

et al. 2015

IJMS

159

121

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Carbapenems (imipenem, meropenem, biapenem, ertapenem, and doripenem) are β-lactam antimicrobial agents. Because carbapenems have the broadest spectra among all β-lactams and are primarily used to treat infections by multi-resistant Gram-negative bacteria, the emergence and spread of carbapenemases became a major public health concern. Carbapenemases are the most versatile family of β-lactamases that are able to hydrolyze carbapenems and many other β-lactams. According to the dependency of divalent cations for enzyme activation, carbapenemases can be divided into metallo-carbapenemases (zinc-dependent class B) and non-metallo-carbapenemases (zinc-independent classes A, C, and D). Many studies have provided various carbapenemase structures. Here we present a comprehensive and systematic review of three-dimensional structures of carbapenemase-carbapenem complexes as well as those of carbapenemases. We update recent studies in understanding the enzymatic mechanism of each class of carbapenemase, and summarize structural insights about regions and residues that are important in acquiring the carbapenemase activity.

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Section: Non-metallo-carbapenemases: Zinc-independent Classes a Cmentioning

confidence: 99%

Section: Non-metallo-carbapenemases: Zinc-independent Classes a Cmentioning

confidence: 99%

Structural Basis for Carbapenem-Hydrolyzing Mechanisms of Carbapenemases Conferring Antibiotic Resistance

Jeon

Lee

et al. 2015

IJMS

159

121

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“…Subsequently, several variants of that enzyme, such as MOX-1 (16), CMY-8 (33), CMY-9 (12), , and CMY-11 (21), have been identified, mainly in East Asian countries, including Taiwan and Japan. The dissemination of CMY- 10-and CMY-11-producing isolates of the family Enterobacteriaceae was also reported in Korea (18,19). In the present study, CMY-type ␤-lactamase-producing K. pneumoniae and E. coli clinical isolates from a Japanese general hospital were investigated.…”

Section: Discussionmentioning

confidence: 69%

Horizontal Transfer of bla _CMY -Bearing Plasmids among Clinical Escherichia coli and Klebsiella pneumoniae Isolates and Emergence of Cefepime-Hydrolyzing CMY-19

Wachino

Kurokawa

Suzuki

et al. 2006

Antimicrob Agents Chemother

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Nine Escherichia coli and 5 Klebsiella pneumoniae clinical isolates resistant to various cephalosporins and cephamycins were identified in a Japanese general hospital between 1995 and 1997. All nine E. coli isolates and one K. pneumoniae isolate carried bla CMY-9 , while the other four K. pneumoniae isolates harbored a variant of bla CMY-9 , namely, bla CMY-19 . The pulsed-field gel electrophoresis patterns of the nine CMY-9-producing E. coli isolates were almost identical, suggesting their clonal relatedness, while those of the five K. pneumoniae isolates were divergent. Plasmid profiles, Southern hybridization, and conjugation assays revealed that the genes for the CMY-9 and the CMY-19 ␤-lactamases were located on very similar conjugative plasmids in E. coli and K. pneumoniae. The genetic environment of bla CMY-19 was identical to that of bla CMY-9 . A single amino acid substitution, I292S, adjacent to the H-10 helix region was observed between CMY-9 and CMY-19. This substitution was suggested to be responsible for the expansion of the hydrolyzing activity against several broad-spectrum cephalosporins, and this finding was consistent with the kinetic parameters determined with purified enzymes. These findings suggest that the bla CMY-19 genes found in the four K. pneumoniae isolates might have originated from bla CMY-9 gene following a point mutation and dispersed among genetically different K. pneumoniae isolates via a large transferable plasmid.Resistance to ␤-lactam antibiotics in gram-negative bacilli is mainly mediated by the production of ␤-lactamases, which are divided into four major molecular classes, classes A, B, C, and D (1, 10). Genes for AmpC (class C) ␤-lactamases are generally encoded on the chromosomes in many gram-negative microbes, including Enterobacter spp., Citrobacter freundii, Serratia marcescens, Morganella morganii, and Pseudomonas aeruginosa (27). Chromosomal AmpC enzymes are usually inducible and are often responsible for resistance to cephalosporins (27) as well as to penicillins. Plasmid-mediated class C ␤-lactamases have mainly been described in Klebsiella spp., Escherichia coli, and Salmonella spp. throughout the world (25). A cephamycin-resistant Klebsiella pneumoniae strain producing a plasmid-mediated class C ␤-lactamase, CMY-1, was first reported in 1989 in Korea (7,8). Plasmid-mediated class C enzymes are currently divided into at least five clusters (25) on the basis of amino acid sequence similarities, together with their putative progenitor chromosomal AmpC enzymes. In Japan, MOX-1 (16), CMY-8 (unpublished data), CMY-9 (12), CMY-2 (unpublished data), CFE-1 (23), and DHA-1 (unpublished data) have so far been found as plasmid-mediated AmpC ␤-lactamases, mainly in nosocomial isolates of the family Enterobacteriaceae.Between 1995 and 1997, eight additional E. coli isolates and five K. pneumoniae isolates resistant to both oximino-cephalosporins and cephamycins were isolated in the same hospital where the first CMY-9-producing E. coli strain (strain HKYM68) was isolated in 19...

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Long-term dissemination of acquired AmpC β-lactamases among Klebsiella spp. and Escherichia coli in Portuguese clinical settings

Freitas

Machado

Ribeiro

et al. 2013

Eur J Clin Microbiol Infect Dis

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We investigated the occurrence, diversity and molecular epidemiology of genes coding for acquired AmpC β-lactamases (qAmpC) among clinical isolates of Enterobacteriaceae lacking inducible chromosomal AmpCs in Portugal. A total of 675 isolates non-susceptible to broadspectrum cephalosporins obtained from four hospitals and three community laboratories during a 7-year period (2002)(2003)(2004)(2005)(2006)(2007)(2008) were analysed. The presence of genes coding for qAmpC was investigated by phenotypic criteria, polymerase chain reaction (PCR) and sequencing. Bacterial identification, antibiotic susceptibility testing, conjugation assays and clonal analysis were performed by standard procedures. The presence of bla qAmpC genes was detected in 50 % (50/100; 41 Klebsiella pneumoniae, 5 Escherichia coli, 4 Klebsiella oxytoca) of the presumptive qAmpC producers. DHA-1, detected in those species, was the most prevalent qAmpC (94 %, 47/50), being identified since 2003 and throughout the studied period in different institutions. Despite the high clonal diversity observed, three DHA-1-producing Klebsiella spp. clones were more frequently identified. CMY-2 (6 %, 3/50) was observed in B1-E. coli clones. Conjugative transfer was only observed in one (2 %) CMY-2-producing isolate. Most qAmpC producers (94 %, 47/50) co-expressed SHV-type and/or OXA-1 or CTX-M-32 extended-spectrum β-lactamases (ESBLs). To the authors' knowledge, this is the first description of the molecular epidemiology and the long-term dissemination of qAmpCproducing Enterobacteriaceae in Portuguese clinical settings, highlighting an evolution towards a more complex epidemiological situation regarding cephalosporin resistance in Portugal.

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Dissemination of Transferable AmpC-type β-Lactamase (CMY-10) in a Korean Hospital

Cited by 17 publications

References 16 publications

Structural Basis for Carbapenem-Hydrolyzing Mechanisms of Carbapenemases Conferring Antibiotic Resistance

Structural Basis for Carbapenem-Hydrolyzing Mechanisms of Carbapenemases Conferring Antibiotic Resistance

Horizontal Transfer of bla _CMY -Bearing Plasmids among Clinical Escherichia coli and Klebsiella pneumoniae Isolates and Emergence of Cefepime-Hydrolyzing CMY-19

Long-term dissemination of acquired AmpC β-lactamases among Klebsiella spp. and Escherichia coli in Portuguese clinical settings

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Dissemination of Transferable AmpC-type β-Lactamase (CMY-10) in a Korean Hospital

Cited by 17 publications

References 16 publications

Structural Basis for Carbapenem-Hydrolyzing Mechanisms of Carbapenemases Conferring Antibiotic Resistance

Structural Basis for Carbapenem-Hydrolyzing Mechanisms of Carbapenemases Conferring Antibiotic Resistance

Horizontal Transfer of bla CMY -Bearing Plasmids among Clinical Escherichia coli and Klebsiella pneumoniae Isolates and Emergence of Cefepime-Hydrolyzing CMY-19

Long-term dissemination of acquired AmpC β-lactamases among Klebsiella spp. and Escherichia coli in Portuguese clinical settings

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Product

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Horizontal Transfer of bla _CMY -Bearing Plasmids among Clinical Escherichia coli and Klebsiella pneumoniae Isolates and Emergence of Cefepime-Hydrolyzing CMY-19