Beta-lactamase

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Beta-lactamase database (BLDB) – structure and function

Beta-lactamase database (BLDB) – structure and function

ABSTRACT Beta-Lactamase Database (BLDB) is a comprehensive, manually curated public resource providing up-to- date structural and functional information focused on this superfamily of enzymes with a great impact on antibiotic resistance. All the enzymes reported and characterised in the literature are presented according to the class (A, B, C and D), family and subfamily to which they belong. All three-dimensional structures of b-lactamases present in the Protein Data Bank are also shown. The characterisation of representative mutants and hydrolytic profiles (kinetics) completes the picture and altogether these four elements consti- tute the essential foundation for a better understanding of the structure-function relationship within this enzymes family. BLDB can be queried using different protein- and nucleotide-based BLAST searches, which represents a key feature of particular importance in the context of the surveillance of the evolution of the antibiotic resistance. BLDB is available online at http://bldb.eu without any registration and supports all modern browsers.
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Extended-spectrum beta-lactamase − producing enterobacteriaceae in the intensive care unit: acquisition does not mean cross-transmission

Extended-spectrum beta-lactamase − producing enterobacteriaceae in the intensive care unit: acquisition does not mean cross-transmission

Additional file Additional file 1: Characterization of ESBL-E. (DOCX 92 kb) Abbreviations CA-SFM: comite de l ’antibiogramme – societe française de microbiologie; DNA: deoxyribonucleic acid; ESBL-E: extended-spectrum beta-lactamase − producing Enterobacteriaceae; ESBL: extended-spectrum beta-lactamase; ICU: intensive care unit; IGSII: index gravity score; IRB: institutional review board; GRE: glycopeptide-resistant Enterococcus; MALDI-TOF: matrix- assisted laser desorption/ionisation, time-of-flight mass spectrometry; MRSA: methicillin resistant Staphylococcus aureus; PCR: polymerase chain reaction; Rep-PCR: repetitive-element PCR; UPGMA: unweighted pair group method with arithmetic mean.
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Prevalence of extended-spectrum beta-lactamase producing Escherichia coli in community-onset urinary tract infections in France in 2013

Prevalence of extended-spectrum beta-lactamase producing Escherichia coli in community-onset urinary tract infections in France in 2013

PT ED The production of extended-spectrum beta-lactamase in Enterobacteriaceae has been associated with increased treatment failure and higher management costs. The prevalence of extended-spectrum beta-lactamase producing Escherichia coli in urinary samples from outpatients has increased significantly in France to reach 3.3%.

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Émergence de souches de Salmonella Virchow multirésistantes et productrices d'une beta-lactamase à spectre étendu en Belgique en 2003

Émergence de souches de Salmonella Virchow multirésistantes et productrices d'une beta-lactamase à spectre étendu en Belgique en 2003

EMERGENCE DE SOUCHES DE SALMONELLA VIRCHOW MULTIRESITANTES ET PRODUCTRICES D’UNE BETA-LACTAMASE A SPECTRE ETENDU EN BELGIQUE EN 2003 Introduction: L’émergence des souches de salmonelles multirésitantes représente un problème important tant en médecine humaine que pour la médecine vétérinaire (1). Bien qu’une antibiothérapie ne soit pas recommandée pour traiter les salmonelloses non-typhoïdes chez l’humain, un traitement devient essentiel en cas d’infection invasive extra-intestinale chez les patients à risque ou chez les patients présentant des symptômes sévères ou prolongés (2).
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First Detection of VIM-2 Metallo-beta-Lactamase-Producing Pseudomonas putida in Blattella germanica Cockroaches in an Algerian Hospital

First Detection of VIM-2 Metallo-beta-Lactamase-Producing Pseudomonas putida in Blattella germanica Cockroaches in an Algerian Hospital

5. Loucif L, Gacemi-Kirane D, Cherak Z, Chamlal N, Grainat N, Rolain J-M. 2016. First report of German cockroaches (Blattella germanica) as reser- voirs of CTX-M-15 extended-spectrum-beta-lactamase- and OXA-48 carbapenemase-producing Enterobacteriaceae in Batna University Hos- pital, Algeria. Antimicrob Agents Chemother 60:6377– 6380. https://doi .org/10.1128/AAC.00871-16 .

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Presenec of extended-spectrum beta-lactamase-producing Enterobacteriaceae in the fecal flora of patients from general practice

Presenec of extended-spectrum beta-lactamase-producing Enterobacteriaceae in the fecal flora of patients from general practice

Presence of extended-spectrum beta-lactamase-producing Enterobacteriaceae (ESBL-E) in the fecal flora of patients from general practice 18 th ECCMID Abstract 631 Cécile Meex 1 , Pierrette Melin 1 , Jean Denis Docquier 2 , Tukumbane Kabasele 1 , Pascale Huynen 1 , Paul M. Tulkens 3 , Patrick De Mol 1

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Quantifying carriage of extended-spectrum beta-lactamase-producing enterobacteriaceae and subsequent ICU acquired infection in French Guiana

Quantifying carriage of extended-spectrum beta-lactamase-producing enterobacteriaceae and subsequent ICU acquired infection in French Guiana

[29] Bonten MJ, Slaughter S, Ambergen AW, Hayden MK, van Voorhis J, Nathan C, et al. The role of “colonization pressure” in the spread of vancomycin-resistant enterococci: an important infection control variable. Arch Intern Med 1998;158:1127–32. [30] Harris AD, Perencevich EN, Johnson JK, Paterson DL, Morris JG, Strauss SM, et al. Patient-to-patient transmission is important in extended-spectrum beta-lactamase- producing Klebsiella pneumoniae acquisition. Clin Infect Dis 2007;45:1347–50. doi:10.1086/522657.

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2-Aminopropane-1,2,3-tricarboxylic acid: Synthesis and co-crystallization with the class A beta-lactamase BS3 of Bacillus licheniformis.

2-Aminopropane-1,2,3-tricarboxylic acid: Synthesis and co-crystallization with the class A beta-lactamase BS3 of Bacillus licheniformis.

on the synthesis and the biochemical evaluation of potential inhib- itors of b-lactamases. Numerous b-lactamase inhibitors have been reported in the literature. 2 However, most of these drugs are b-lac- tam derivatives, and when exposed to such molecules, bacteria ac- quire resistance. To disrupt this vicious circle, non b-lactam inhibitors may be an alternative. The search of novel structures considered as ‘hits’ in medicinal chemistry proceeds from different strategies, such as the mechanism-based design and the screening of various chemical libraries, but also from serendipity. Our pres- ent work is precisely based on a fortuitous observation related to protein crystallography, when using 100 mM sodium citrate buffer in the crystallization protocols.
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The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold

The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold

The structure was solved by the multiple isomorphous replacement method, with density modification and phase combination, using X-ray data collected from the native.. protein and the T97[r]

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Correction to: Infection-related ventilator-associated complications in ICU patients colonised with extended-spectrum beta-lactamase-producing Enterobacteriaceae.

Correction to: Infection-related ventilator-associated complications in ICU patients colonised with extended-spectrum beta-lactamase-producing Enterobacteriaceae.

Biostatistical and information system expertise: Jean-Francois Timsit (Medical and Infectious Diseases ICU, Bichat-Claude Bernard Hospital, Paris, France; UMR 1137 Inserm –Paris Didero[r]

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First occurrence of an IMP metallo-beta-lactamase in Aeromonas caviae: IMP-19 in an isolate from France.

First occurrence of an IMP metallo-beta-lactamase in Aeromonas caviae: IMP-19 in an isolate from France.

manual, 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Har- bor, NY. 16. Senda, K., Y. Arakawa, S. Ichiyama, K. Nakashima, H. Ito, S. Ohsuka, K. Shimokata, N. Kato, and M. Ohta. 1996. PCR detection of metallo- ␤- lactamase gene (blaIMP) in gram-negative rods resistant to broad-spectrum ␤-lactams. J. Clin. Microbiol. 34:2909–2913.

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Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by site-directed mutagenesis

Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by site-directed mutagenesis

From a B2 to a B3 Metallo-β-lactamase The Arg 121 residue is conserved in the BcII and CphA enzymes. Dal Peraro et al. (23) have shown by quantum chemistry calculations that, in the mono-zinc form of BcII, Arg 121 anchors the Asp 120 side chain by forming a strong ionic bond, ultimately orienting the Zn(II)-bound hydroxide for nucleophilic attack of the antibiotic β- lactam ring. Moreover, Rasia et al. (24) have shown that the R121H mutation in BcII leads to poor positioning of Asp 120 , and thus the k cat values of this mutant are lower than those of WT BcII. Our kinetic results are consistent with a similar role for the Arg 121 residue in CphA, because the k cat value for imipenem is strongly decreased with R121H.
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Consequences of Extended Spectrum Beta‐Lactamase–Producing Enterobacteriaceae and Methicillin‐Resistant Staphylococcus aureus Carriage in Awaiting Liver Transplant Patients

Consequences of Extended Spectrum Beta‐Lactamase–Producing Enterobacteriaceae and Methicillin‐Resistant Staphylococcus aureus Carriage in Awaiting Liver Transplant Patients

We retrospectively included 250 of 483 cirrhotic placed on waitlist for LT from December 2015 to January 2018 in our liver transplant center at Pitié-Salpêtrière hospital, tha[r]

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Crystal structures of the Bacillus licheniformis BS3 class A beta-lactamase and of the acyl-enzyme adduct formed with cefoxitin

Crystal structures of the Bacillus licheniformis BS3 class A beta-lactamase and of the acyl-enzyme adduct formed with cefoxitin

It is important to emphasize that in the BS3-cefoxitin structure, the R-methoxy group does not directly cause the conformational change but that it does so by influencing the 7β side chain orientation. In agreement with that, and as observed by NMR experiments, the 7β-formamidoyl-7R- methoxycephalosporanic acid does not induce structural modifications in the B. licheniformis 749/C β-lactamase. 2 Indeed, in this case, there is no steric incompatibility between the short 7β side chain and the Ω-loop. Nevertheless, for all compounds bearing a 7R-methoxy group, all steps of the hydrolysis pathway are severely impeded. To both accom- modate the 7R and eventually the 7β side chains into the catalytic pocket and bring the substrate in a suitable position for the nucleophilic attack, the β-lactamase must necessarily undergo some conformational changes. The catalytic mech- anism leading to formation of the acyl-enzyme complex is thus greatly impaired. Comparatively, the k cat /K m value determined for BS3 and cephalothin is more than 10 5 -fold larger than with a similar substrate bearing a 7R-methoxy group (Table 1). Similarly, the deacylation process is also impaired by the introduction of a new hydrogen bonding scheme, which directly involves essential amino acid residues such as Ser70, Lys73, and Glu166, and by the disappearance of the hydrolytic water molecule.
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Discovery of novel lipophilic inhibitors of OXA-10 enzyme (class D beta-lactamase) by screening amino analogs and homologs of citrate and isocitrate.

Discovery of novel lipophilic inhibitors of OXA-10 enzyme (class D beta-lactamase) by screening amino analogs and homologs of citrate and isocitrate.

C (P99 26 ), class D (OXA-10 27 ), and class B (BcII 28 , VIM-4 29 ). Class A enzymes are primarily penicillinases, susceptible to inhibition by the presently marketed -lactamase inhibitors, namely potassium clavulanate, sulbactam and tazobactam which are also efficient against some class D -lactamases. Class C enzymes are primarily cephalosporinases, resistant to inhibition by the previous agents. There is no clinically useful inhibitor for class B enzymes that emerge now as worldwide source of carbapenem resistance.

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X-ray analysis of the NMC-A beta-lactamase at 1.64-A resolution, a class A carbapenemase with broad substrate specificity

X-ray analysis of the NMC-A beta-lactamase at 1.64-A resolution, a class A carbapenemase with broad substrate specificity

coding a mutant of the chromosomal ␤-lactamase of Kluyvera cryocrescens, was also identified at a plasmid location in E. cloacae 7506, suggesting the ISEcp1-assisted escape of bla KLUC from the chromosome. Determi- nation of the KPC-2 structure at 1.6 Å revealed that the binding site was occupied by the C-terminal (C-ter) residues coming from a symmetric KPC-2 monomer, with the ultimate C-ter Glu interacting with Ser130, Lys234, Thr235, and Thr237 in the active site. This mode of binding can be paralleled to the inhibition of the TEM-1 ␤-lactamase by the inhibitory protein BLIP. Determination of the 1.23-Å structure of a KPC-2 mutant in which the five C-ter residues were deleted revealed that the catalytic site was filled by a citrate molecule. Structure analysis and docking simulations with cefotaxime and imipenem provided further insights into the molecular basis of the extremely broad spectrum of KPC-2, which behaves as a cefotaximase with significant activity against carbapenems. In particular, residues 104, 105, 132, and 167 draw a binding cavity capable of accommodating both the aminothiazole moiety of cefotaxime and the 6 ␣-hydroxyethyl group of imipenem, with the binding of the former drug being also favored by a significant degree of freedom at the level of the loop at positions 96 to 105 and by an enlargement of the binding site at the end of strand ␤3.
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Role of Cys221 and Asn116 in the zinc-binding sites of the Aeromonas hydrophila metallo-beta-lactamase.

Role of Cys221 and Asn116 in the zinc-binding sites of the Aeromonas hydrophila metallo-beta-lactamase.

* Measured as Ki. Measurements were done at 30 °C in 15 mM sodium cacodylate, pH 6.5. N.D., not determined. Mutation of Cys221 Cys221 was replaced by a Ser or an Ala residue. The purified proteins were analyzed by MS. For the C221S mutant, the expected mass of 25,177 Da was found. By contrast, analysis of the C221A mutant indicated the presence of three majors peaks of 24,346, 24,276 and 23,503 Da (for an expected mass of 25,156 Da), indicating that the mutant protein had lost 8, 9 and 15 residues at the C terminus. There was no degradation at the N terminus, as confirmed by N-terminal sequencing (not shown). Surprisingly, we found that cefoxitin treatment of the C221S preparation resulted in a significant decrease in the hydrolytic activity against imipenem. This was completely unexpected because cefoxitin inactivates the CphA β-lactamase via a covalent modification of the Cys221 side chain [18], and we anticipated that the C221S mutant would be insensitive to this compound. We therefore concluded that the mutant preparation was contaminated by traces of wild-type protein. Similar findings have been reported before, and were suggested to occur through a 'misreading' at the transcriptional and/or trans-lational level [19, and references therein]. In the present case, however, the wild-type enzyme could be completely inactivated by repeated treatments with cefoxitin (see Materials and methods). This resulted in a ~200-fold decrease in the hydrolytic activity of the preparation against imipenem (not shown). All the data reported here (e.g. in table 3) were obtained after wild-type-enzyme inactiva-tion.
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Crystal structure of Enterobacter cloacae 908R class C beta-lactamase bound to iodo-acetamido-phenyl boronic acid, a transition-state analogue

Crystal structure of Enterobacter cloacae 908R class C beta-lactamase bound to iodo-acetamido-phenyl boronic acid, a transition-state analogue

with aryl boronic acids were investigated. From the sta- tistical search with Relibase, apart from the structure of cocaine esterase in complex with phenyl boronic acid (PDB code 1JU3 [25]), aryl boronic acid ligands are ap- parently not found in other structures deposited at the PDB. This does not mean that the aryl boronic fragment is specific for class C b-lactamase but probably reflects

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Beta-lactamase-encoding gene identification by micro-arrays in phenotypically resistant pathogenic Escherichia coli from young calves in Wallonia, Belgium.

Beta-lactamase-encoding gene identification by micro-arrays in phenotypically resistant pathogenic Escherichia coli from young calves in Wallonia, Belgium.

Objectives Since 2012, a decrease of β-lactam resistance of pathogenic Escherichia (E.) coli from calves has been observed at ARSIA, the Regional Veterinary Diagnostics laboratory in Wallonia, Belgium. This may be a consequence of the recommendation for a prior antibiotic sensitivity test of bovine pathogenic E. coli for human critical antibiotics, like 3 rd and 4 th generation cefalosporins. The most frequent -lactam resistance mechanism is the production of a -lactamase enzyme that inactivates the antibiotic. Actual classification(s) of β-lactamases (BLA) is highly complex, but four groups can be summarily described: classical BLA (BLAC), extended cefalosporinases (BLAAmpC), extended spectrum BLA (BLAESBL) and carbapenemases (BLACPE). The aim of this study was to identify the resistance genes coding for β-lactamases in pathogenic E. coli from calves with a resistance phenotype at the disk diffusion assay.
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The two beta-lactamase genes of Streptomyces cacaoi, blaL and blaU, are under the control of the same regulatory system.

The two beta-lactamase genes of Streptomyces cacaoi, blaL and blaU, are under the control of the same regulatory system.

Bartowsky E, Normark S (1993) Interactions of wild-type and mutant AmpR of Citrobacter freundii with target DNA. Mol Microbiol 10:555±565 Bennett PM, Chopra I (1993) Molecular basis of b-lactamase in- duction in bacteria. Antimicrob Agents Chemother 37:153±158 Bikel I, Roberts TM, Bladon MT, Green R, Amann E, Livingston DM (1983) Puri®cation of biologically active simian virus 40 small tumor antigen. Proc Natl Acad Sci USA 80:906±910 Blackwell TK, Weintraub H (1990) Di€erences and similarities in

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