Cloning, nucleotide sequence, and expression of the Bacillus cereus 5/B/6 beta-lactamase II structural gene

Lim, Heon M.; Pène, Jacques J.; Shaw, Robert W.

doi:10.1128/jb.170.6.2873-2878.1988

Cited by 86 publications

(61 citation statements)

References 31 publications

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“…Interestingly, not all of the MBLs readily hydrolyze nitrocefin. The first MBL detected were chromosomally encoded and was detected in Bacillus cereus ( Lim et al, 1988). Since then there has been a dramatic increase in detection and spread of acquired or transferable families of these MBLs.…”

Section: Carbapenemasesmentioning

confidence: 99%

Pseudomonas Aeruginosa and Newer β-Lactamases: An Emerging Resistance Threat

Basak¹,

Attal²,

Rajurkar³

2012

Infection Control - Updates

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Section: Carbapenemasesmentioning

confidence: 99%

Pseudomonas Aeruginosa and Newer β-Lactamases: An Emerging Resistance Threat

Basak¹,

Attal²,

Rajurkar³

2012

Infection Control - Updates

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“…The mechanism of hydrolysis is dependent on interaction of the ␤-lactams with zinc ions in the active site of the enzyme, resulting in the distinctive trait of their inhibition by EDTA, a chelator of Zn 2ϩ and other divalent cations. The first metallo-␤-lactamases detected and studied were chromosomal enzymes present in environmental and opportunistic pathogenic bacteria such as Bacillus cereus (98,109), Aeromonas spp. (78), and Stenotrophomonas maltophilia (188).…”

Section: Class B Metallo-␤-lactamasesmentioning

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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“…The early studies on chromosomally mediated MBLs mainly centered around Bacillus cereus (BC II) (83), and Stenotrophomonas maltophilia (L1) (178). However, primarily due to genomic sequencing, increasingly more chromosomally mediated genes are being discovered but are often found in obscure nonclinical bacteria (89,103,146,149,161).…”

Section: Introductionmentioning

confidence: 99%

Metallo-β-Lactamases: the Quiet before the Storm?

et al. 2005

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SUMMARY The ascendancy of metallo-β-lactamases within the clinical sector, while not ubiquitous, has nonetheless been dramatic; some reports indicate that nearly 30% of imipenem-resistant Pseudomonas aeruginosa strains possess a metallo-β-lactamase. Acquisition of a metallo-β-lactamase gene will invariably mediate broad-spectrum β-lactam resistance in P. aeruginosa, but the level of in vitro resistance in Acinetobacter spp. and Enterobacteriaceae is less dependable. Their clinical significance is further embellished by their ability to hydrolyze all β-lactams and by the fact that there is currently no clinical inhibitor, nor is there likely to be for the foreseeable future. The genes encoding metallo-β-lactamases are often procured by class 1 (sometimes class 3) integrons, which, in turn, are embedded in transposons, resulting in a highly transmissible genetic apparatus. Moreover, other gene cassettes within the integrons often confer resistance to aminoglycosides, precluding their use as an alternative treatment. Thus far, the metallo-β-lactamases encoded on transferable genes include IMP, VIM, SPM, and GIM and have been reported from 28 countries. Their rapid dissemination is worrisome and necessitates the implementation of not just surveillance studies but also metallo-β-lactamase inhibitor studies securing the longevity of important anti-infectives.

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Cloning, nucleotide sequence, and expression of the Bacillus cereus 5/B/6 beta-lactamase II structural gene

Cited by 86 publications

References 31 publications

Pseudomonas Aeruginosa and Newer β-Lactamases: An Emerging Resistance Threat

Pseudomonas Aeruginosa and Newer β-Lactamases: An Emerging Resistance Threat

Carbapenemases: the Versatile β-Lactamases

Metallo-β-Lactamases: the Quiet before the Storm?

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