Nosocomial Spread of Ceftazidime-Resistant
            <i>Klebsiella pneumoniae</i>
            Strains Producing a Novel Class A β-Lactamase, GES-3, in a Neonatal Intensive Care Unit in Japan

Wachino, Jun-ichi; Doi, Yohei; Yamane, Kunikazu; Shibata, Naohiro; Yagi, Tetsuya; Kubota, Takako; Ito, Hideo; Arakawa, Yoshichika

doi:10.1128/aac.48.6.1960-1967.2004

Cited by 64 publications

(53 citation statements)

References 40 publications

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“…The bacterial strains used in this study and the ␤-lactamases that they produce are shown in Table 1. The types of ␤-lactamase genes were previously confirmed by PCR analyses, cloning and sequencing experiments, as well as isoelectric focusing, as described elsewhere (6,10,15,25,36,40,42,43,44). APB, 3-nitrophenylboronic acid (NPB), and 2-thiopheneboronic acid (TPB) were purchased from Tokyo Kasei Kogyo Co., Ltd. (Tokyo, Japan).…”

Section: Methodsmentioning

confidence: 99%

Practical Methods Using Boronic Acid Compounds for Identification of Class C β-Lactamase-ProducingKlebsiella pneumoniaeandEscherichia coli

et al. 2005

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Detection of the resistance mediated by class C ␤-lactamases remains a challenging issue, considering that transferable plasmid-mediated class C ␤-lactamases are of worldwide concern. Methods for the identification of strains that produce extended-spectrum ␤-lactamases (ESBLs) or metallo-␤-lactamases (MBLs) have been developed and applied for routine use in clinical microbiology laboratories, but no practical methods for identification of plasmid-mediated class C producers have been established to date. We therefore developed three simple methods for clinical microbiology laboratories that allow identification of plasmid-mediated class C ␤-lactamase-producing bacteria using a boronic acid derivative, 3-aminophenylboronic acid (APB), one of the specific inhibitors of class C ␤-lactamases. Detection by the disk potentiation test was based on the enlargement of the growth-inhibitory zone diameter (by greater than or equal to 5 mm) around a Kirby-Bauer disk containing a ceftazidime (CAZ) or a cefotaxime (CTX) disk in combination with APB. In a double-disk synergy test, the discernible expansion of the growth-inhibitory zone around the CAZ or the CTX disk toward a disk containing APB was indicative of class C ␤-lactamase production. A greater than or equal to eightfold decrease in the MIC of CAZ or CTX in the presence of APB was the criterion for detection in the microdilution test. By using these methods, Escherichia coli and Klebsiella pneumoniae isolates producing plasmid-mediated class C ␤-lactamases, ACT-1, CMY-2, CMY-9, FOX-5, LAT-1, and MOX-1, were successfully distinguished from those producing other classes of ␤-lactamases, such as ESBLs and MBLs. These methods will provide useful information needed for targeted antimicrobial therapy and better infection control.

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Section: Methodsmentioning

confidence: 99%

Practical Methods Using Boronic Acid Compounds for Identification of Class C β-Lactamase-ProducingKlebsiella pneumoniaeandEscherichia coli

et al. 2005

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“…GES (76,118,320,327,410,413,416,418), BES (45), TLA (8,369), SFO (240), and IBC (133,138,191,208,241,(410)(411)(412) are other examples of non-TEM, non-SHV ESBLs and have been found in a wide range of geographic locations.…”

Section: Veb-1 Bes-1 and Other Esblsmentioning

confidence: 99%

Extended-Spectrum β-Lactamases: a Clinical Update

2005

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SUMMARY Extended-spectrum β-lactamases (ESBLs) are a rapidly evolving group of β-lactamases which share the ability to hydrolyze third-generation cephalosporins and aztreonam yet are inhibited by clavulanic acid. Typically, they derive from genes for TEM-1, TEM-2, or SHV-1 by mutations that alter the amino acid configuration around the active site of these β-lactamases. This extends the spectrum of β-lactam antibiotics susceptible to hydrolysis by these enzymes. An increasing number of ESBLs not of TEM or SHV lineage have recently been described. The presence of ESBLs carries tremendous clinical significance. The ESBLs are frequently plasmid encoded. Plasmids responsible for ESBL production frequently carry genes encoding resistance to other drug classes (for example, aminoglycosides). Therefore, antibiotic options in the treatment of ESBL-producing organisms are extremely limited. Carbapenems are the treatment of choice for serious infections due to ESBL-producing organisms, yet carbapenem-resistant isolates have recently been reported. ESBL-producing organisms may appear susceptible to some extended-spectrum cephalosporins. However, treatment with such antibiotics has been associated with high failure rates. There is substantial debate as to the optimal method to prevent this occurrence. It has been proposed that cephalosporin breakpoints for the Enterobacteriaceae should be altered so that the need for ESBL detection would be obviated. At present, however, organizations such as the Clinical and Laboratory Standards Institute (formerly the National Committee for Clinical Laboratory Standards) provide guidelines for the detection of ESBLs in klebsiellae and Escherichia coli. In common to all ESBL detection methods is the general principle that the activity of extended-spectrum cephalosporins against ESBL-producing organisms will be enhanced by the presence of clavulanic acid. ESBLs represent an impressive example of the ability of gram-negative bacteria to develop new antibiotic resistance mechanisms in the face of the introduction of new antimicrobial agents.

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“…Although rare, GES enzymes have been identified worldwide, with reports from Greece, France, Portugal, South Africa, French Guiana, Brazil, Argentina, Korea, and Japan (25,33,42,86,90,155,164,168,173,186,(218)(219)(220). These enzymes have been most frequently associated with single occurrences.…”

Section: Plasmid-encoded Enzymes: Kpc and Gesmentioning

confidence: 99%

Carbapenemases: the Versatile β-Lactamases

2007

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SUMMARY Carbapenemases are β-lactamases with versatile hydrolytic capacities. They have the ability to hydrolyze penicillins, cephalosporins, monobactams, and carbapenems. Bacteria producing these β-lactamases may cause serious infections in which the carbapenemase activity renders many β-lactams ineffective. Carbapenemases are members of the molecular class A, B, and D β-lactamases. Class A and D enzymes have a serine-based hydrolytic mechanism, while class B enzymes are metallo-β-lactamases that contain zinc in the active site. The class A carbapenemase group includes members of the SME, IMI, NMC, GES, and KPC families. Of these, the KPC carbapenemases are the most prevalent, found mostly on plasmids in Klebsiella pneumoniae. The class D carbapenemases consist of OXA-type β-lactamases frequently detected in Acinetobacter baumannii. The metallo-β-lactamases belong to the IMP, VIM, SPM, GIM, and SIM families and have been detected primarily in Pseudomonas aeruginosa; however, there are increasing numbers of reports worldwide of this group of β-lactamases in the Enterobacteriaceae. This review updates the characteristics, epidemiology, and detection of the carbapenemases found in pathogenic bacteria.

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Nosocomial Spread of Ceftazidime-Resistant Klebsiella pneumoniae Strains Producing a Novel Class A β-Lactamase, GES-3, in a Neonatal Intensive Care Unit in Japan

Cited by 64 publications

References 40 publications

Practical Methods Using Boronic Acid Compounds for Identification of Class C β-Lactamase-ProducingKlebsiella pneumoniaeandEscherichia coli

Practical Methods Using Boronic Acid Compounds for Identification of Class C β-Lactamase-ProducingKlebsiella pneumoniaeandEscherichia coli

Extended-Spectrum β-Lactamases: a Clinical Update

Carbapenemases: the Versatile β-Lactamases

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