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See detailMetallo-beta-lactamases as emerging resistance determinants in Gram-negative pathogens: open issues
Cornaglia, G.; Akova, M.; Amicosante, G. et al

in International Journal of Antimicrobial Agents (2007), 29(4), 380-388

The rapid spread of acquired metallo-beta-lactamases (MBLs) among major Gram-negative pathogens is a matter of particular concern worldwide and primarily in Europe, one of first continents where the ... [more ▼]

The rapid spread of acquired metallo-beta-lactamases (MBLs) among major Gram-negative pathogens is a matter of particular concern worldwide and primarily in Europe, one of first continents where the emergence of acquired MBLs has been reported and possibly the geographical area where the increasing diversity of these enzymes and the number of bacterial species affected are most impressive. This spread has not been paralleled by accuracy/standardisation of detection methods, completeness of epidemiological knowledge or a clear understanding of what MBL production entails in terms of clinical impact, hospital infection control and antimicrobial chemotherapy. A number of European experts in the field met to review the current knowledge on this phenomenon, to point out open issues and to reinforce and relate to one another the existing activities set forth by research institutes, scientific societies and European Union-driven networks. (c) 2006 Elsevier B.V. and the International Society of Chemotherapy. All rights reserved. [less ▲]

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See detailCharacterisation of KLUA-9, a beta-lactamase from extended-spectrum cephalosporin-susceptible Kluyvera ascorbata, and genetic organisation of bla(KLUA-9)
Rodriguez, M. M.; Power, Pablo ULg; Bauvois, C. et al

in International Journal of Antimicrobial Agents (2007), 29(3), 332-337

This study characterised the genetic environment of the chromosomally encoded blaKLUA-9 gene from a clinical Kluyvera ascorbata isolate and performed a kinetic characterisation of KLUA-9. Purified KLUA-9 ... [more ▼]

This study characterised the genetic environment of the chromosomally encoded blaKLUA-9 gene from a clinical Kluyvera ascorbata isolate and performed a kinetic characterisation of KLUA-9. Purified KLUA-9 showed the highest catalytic efficacies towards benzylpenicillin, ampicillin, piperacillin, first-generation cephalosporins, cefuroxime and cefoperazone; like other 'cefotaximases', it showed a much higher rate of hydrolysis of cefotaxime than ceftazidime, whilst dicloxacillin, cefoxitin and imipenem behaved as poor substrates. A 9 kb insert from K. ascorbata was cloned (Escherichia coli KK68C1) and sequenced. blaKLUA-9 and its 266 bp upstream flanking region (almost identical to the integron-associated bla(CTX-M-2)) are preceded by an aspat variant, a ypdABC-like operon and two open reading frames with unknown functions. Unlike IS CRI -associated bla(CTX-M-2) genes, we failed to detect the putative orf513 recombination sites. Instead, we were able to localise the 5 bp target sites for insertion of ISEcp1B, suggesting that this element could be responsible for future (or still undetected) mobilisation of blaKLUA-9 to more efficiently transferred elements. (c) 2006 Elsevier B.V and the International Society of Chemotherapy. All rights reserved. [less ▲]

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See detailBiochemical characterisation of the CTX-M-14 beta-lactamase
Ishii, Y.; Galleni, Moreno ULg; Ma, L. et al

in International Journal of Antimicrobial Agents (2007), 29(2), 159-164

Cefotaxime-resistant Escherichia coli TUM 1121 was isolated from an abscess of an 83-year-old patient. The CTX-M-14 gene was located on a 70 kb plasmid. The enzyme was purified and its activity was ... [more ▼]

Cefotaxime-resistant Escherichia coli TUM 1121 was isolated from an abscess of an 83-year-old patient. The CTX-M-14 gene was located on a 70 kb plasmid. The enzyme was purified and its activity was analysed. CTX-M-14 was poorly active against ceftazidime and aztreonam. Aztreonam behaved as a competitive inhibitor. Among the tested suicide substrates for class A beta-lactamases, sulbactam was a rather good substrate. Tazobactam and clavulanic acid behaved as inactivators. The interactions between clavulanic acid and CTX-M-14 were characterised by progressive inactivation of the P-lactamase. Carbapenems such as imipenem, meropenem or doripenem did not behave as inactivators of CTX-M-14, however very small k(cat) values were observed. This result shows that CTX-M-14 is able to hydrolyse carbapenems. (c) 2006 Elsevier B.V. and the International Society of Chemotherapy. All rights reserved. [less ▲]

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See detailPenicillin-binding proteins. Wall peptidoglycan assembly and resistance to penicillin: facts, doubts and hopes
Ghuysen, Jean-Marie ULg; Charlier, Paulette ULg; Coyette, Jacques ULg et al

in International Journal of Antimicrobial Agents (1997), 8(1), 45-60

As the protein sequence and structure databases expand, the relationships between proteins, the notion of protein superfamily, and the driving forces of evolution are better understood. Key steps of the ... [more ▼]

As the protein sequence and structure databases expand, the relationships between proteins, the notion of protein superfamily, and the driving forces of evolution are better understood. Key steps of the synthesis of the bacterial cell wall peptidoglycan are revisited in light of these advances. The reactions through which the D-alanyl-D-alanine depeptide is formed, utilized, and hydrolyzed and the sites of action of the glycopeptide and β-lactam antibiotics illustrate the concept according to which new enzyme functions evolve as a result of tinkering of existing proteins. This occurs by the acquisition of local structural changes, the fusion into mul-timodular polypeptides, and the association into multiprotein complexes. [less ▲]

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