β-Lactamases with high activity against imipenem and Sch 34343 from <i>Aeromonas hydrophila</i>

Shannon, Kevin; King, Anna; Phillips, Ian

doi:10.1093/jac/17.1.45

Cited by 55 publications

(33 citation statements)

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“…The "hidden" carbapenemases of Aeromonas spp. hydrolyzed nitrocefin and other cephalosporins imperceptibly and could be detected only by using a carbapenem bioassay or hydrolysis test (64,65,196,223,241). Recently, the VIM-2 enzyme was shown to share this property and was detected on IEF gels by an imipenem hydrolysis detection method (171).…”

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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Section: Class B Metallo-␤-lactamasesmentioning

confidence: 99%

Carbapenemases: the Versatile β-Lactamases

2007

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“…A strong sequence similarity exists between these two enzymes (28), suggesting that the CfiA enzyme also belongs to molecular class B. More information on molecular sequence data of other CH metallo-3-lactamases is needed for a better understanding of this group of enzymes, including their biochemical properties and evolutionary relationships.Production of CH metallo-,B-lactamases has been reported among members of the genus Aeromonas (2,26). In this * Corresponding author.…”

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confidence: 98%

“…Production of CH metallo-,B-lactamases has been reported among members of the genus Aeromonas (2,26). In this * Corresponding author.…”

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confidence: 98%

“…The prototype for this group of enzymes is the 1-lactamase II of Bacillus cereus, which has long been studied as a model of metallo-13-lactamases and for which molecular sequence data, along with enzymologic and crystallographic data, are available (3,12,17,27). In the molecular classification of 1-lactamases, a class B was devised for this enzyme (1).Interest in this group of enzymes has grown recently since an increasing number of metallo-1-lactamases have been described in several gram-negative species which share the important characteristic of being able to hydrolyze carbapenem compounds (2,7,9,22,25,26,31). Carbapenems are new P-lactam antibiotics of great therapeutic potential, since they are not hydrolyzed by most bacterial 3-lactamases and show a broad spectrum of activity.…”

mentioning

confidence: 99%

“…Interest in this group of enzymes has grown recently since an increasing number of metallo-1-lactamases have been described in several gram-negative species which share the important characteristic of being able to hydrolyze carbapenem compounds (2,7,9,22,25,26,31). Carbapenems are new P-lactam antibiotics of great therapeutic potential, since they are not hydrolyzed by most bacterial 3-lactamases and show a broad spectrum of activity.…”

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The Aeromonas hydrophila cphA gene: molecular heterogeneity among class B metallo-beta-lactamases

1991

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An Aeromonas hydrophila gene, named cphA, coding for a carbapenem-hydrolyzing metallo-,I-lactamase, was cloned in Escherichia coli by screening an Aeromonas genomic library for clones able to grow on imipenem-containing medium. From sequencing data, the cloned cphA gene appeared able to code for a polypeptide of 254 amino acids whose sequence includes a potential N-terminal leader sequence for targeting the protein to the periplasmic space. These data were in agreement with the molecular mass of the original Aeromonas enzyme and of the recombinant enzyme produced in E. coli, evaluated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of crude P-lactamase preparations followed by renaturation treatment for proteins separated in the gel and localization of protein bands showing carbapenem-hydrolyzing I-lactamase activity by a modified iodometric technique. The deduced amino acid sequence of the CphA enzyme showed regions of partial homology with both the I-lactamase II of Bacillus cereus and the CfiA I-lactamase of Bacteroides fragilis. Sequence homologies were more pronounced in the regions encompassing the amino acid residues known in the enzyme of B. cereus to function as ligand-binding residues for the metal cofactor. The CphA enzyme, however, appeared to share a lower degree of similarity with the two other enzymes, which, in turn, seemed more closely related to each other. These results, therefore, suggest the existence of at least two molecular subclasses within molecular class B metallo-,I-lactamases.In recent classification schemes for ,B-lactamases, a distinct grouping has been reserved for those enzymes requiring a metal cofactor for activity (metallo-1-lactamases) (1, 4, 5). The prototype for this group of enzymes is the 1-lactamase II of Bacillus cereus, which has long been studied as a model of metallo-13-lactamases and for which molecular sequence data, along with enzymologic and crystallographic data, are available (3,12,17,27). In the molecular classification of 1-lactamases, a class B was devised for this enzyme (1).Interest in this group of enzymes has grown recently since an increasing number of metallo-1-lactamases have been described in several gram-negative species which share the important characteristic of being able to hydrolyze carbapenem compounds (2,7,9,22,25,26,31). Carbapenems are new P-lactam antibiotics of great therapeutic potential, since they are not hydrolyzed by most bacterial 3-lactamases and show a broad spectrum of activity.Information currently available on carbapenem-hydrolyzing (CH) metallo-1-lactamases is limited, in most cases, to a few biochemical features and suggests the existence of different molecular species within this group of enzymes (5). Molecular sequence data are presently available only for the CfiA P-lactamase of Bacteroides fragilis TAL2480 (28) and for the ,B-lactamase II of B. cereus 569/H (12) and 5/B/6 (17). A strong sequence similarity exists between these two enzymes (28), suggesting that the CfiA enzyme also belongs to molecular class B...

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Resistance to β-Lactams, a Self-Regenerating Problem

Aszodi

Bryskier

2001

Novel Frontiers in the Production of Compounds for Biomedical Use

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β-Lactamases with high activity against imipenem and Sch 34343 from Aeromonas hydrophila

Cited by 55 publications

References 0 publications

Carbapenemases: the Versatile β-Lactamases

Carbapenemases: the Versatile β-Lactamases

The Aeromonas hydrophila cphA gene: molecular heterogeneity among class B metallo-beta-lactamases

Resistance to β-Lactams, a Self-Regenerating Problem

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