Role of changes in the L3 loop of the active site in the evolution of enzymatic activity of VIM-type metallo-β-lactamases

Journal of Antimicrobial Chemotherapy

Volumn 65, Issue 9, 2010, Pages 1950-1954

  Merino, María ^a   Pérez Llarena, Francisco J ^a   Kerff, Frederic ^c   Poza, Margarita ^a   Mallo, Susana ^a   Rumbo Feal, Soraya ^a   Beceiro, Alejandro ^a   Juan, Carlos ^b   Oliver, Antonio ^b   Bou, Germán ^a  

^a UNIVERSITY OF A CORUÑA   (Spain)

^b HOSPITAL UNIVERSITARIO SON ESPASES   (Spain)

^c UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

Antibiotic resistance; Pseudomonas aeruginosa; Site directed mutagenesis

Indexed keywords

AMPICILLIN; CEFEPIME; CEFTAZIDIME; METALLO BETA LACTAMASE; METALLO BETA LACTAMASE VIM 1; METALLO BETA LACTAMASE VIM 13; UNCLASSIFIED DRUG;

AFFINITY CHROMATOGRAPHY; ANTIBIOTIC RESISTANCE; ARTICLE; ENZYME ACTIVITY; KINETICS; MINIMUM INHIBITORY CONCENTRATION; MUTAGENESIS; MUTANT; NONHUMAN;

EID: 77955618651     PISSN: 03057453     EISSN: 14602091     Source Type: Journal    
DOI: 10.1093/jac/dkq259     Document Type: Article

References (24)

1. Ambler RP. The structure of β-lactamases. Philos Trans R Soc Lond B Biol Sci 1980; 289: 321-31.
2. Bush K, Jacoby GA. Updated functional classification of β-lactamases. Antimicrob Agents Chemother 2010; 54: 969-76.
3. Docquier JD, Lamotte-Brasseur J, Galleni M et al. On functional and structural heterogeneity of VIM-type metallo-β-lactamases. J Antimicrob Chemother 2003; 51: 257-66.
4. Crowder MW, Spencer J, Vila AJ. Metallo-β-lactamases: novel weaponry for antibiotic resistance in bacteria. Acc Chem Res 2006; 39: 721-8.
5. Walsh TR, Toleman MA, Poirel L et al. Metallo-β-lactamases: the quiet before the storm? Clin Microbiol Rev 2005; 18: 306-25.
6. Perez-Llarena FJ, Bou G. β-Lactamase inhibitors: the story so far. Curr Med Chem 2009; 16: 3740-65.
7. Poirel L, Pitout JD, Nordmann P. Carbapenemases: molecular diversity and clinical consequences. Future Microbiol 2007; 2: 501-12.
8. SIM-1, in a class 1 integron from Acinetobacter baumannii clinical isolates from Korea. Antimicrob Agents Chemother 2005; 49: 4485-91.
9. Sekiguchi J, Morita K, Kitao T et al. KHM-1, a novel plasmid-mediated metallo-β-lactamase from a Citrobacter freundii clinical isolate. Antimicrob Agents Chemother 2008; 52: 4194-7.
10. Yong D, Walsh TR, Bell J et al. Novel ISCR element ISCR15 is responsible for the movement of the B3 subgroup mobile metallo-β-lactamase (MBL) gene blaAim-1. In: Abstracts of the Forty-eighth Interscience Conference on Antimicrobial Agents and Chemotherapy, Washington, DC, 2008. Abstract C1-110, p. 88. American Society for Microbiology, Washington, DC, USA.
11. Yong D, Toleman MA, Giske CG et al. Characterization of a new metallo-β-lactamase gene, blaNDM-1, and a novel erythromycin esterase gene carried on a unique genetic structure in Klebsiella pneumoniae sequence type 14 from India. Antimicrob Agents Chemother 2009; 53: 5046-54.
12. Poirel L, Rodriguez-Martinez JM, Al Naiemi N et al. Characterization of DIM-1, an integron-encoded metallo-β-lactamase from a Pseudomonas stutzeri clinical isolate in the Netherlands. Antimicrob Agents Chemother 2010; 54: 2420-4.
13. Rodriguez-Martinez JM, Nordmann P, Fortineau N et al. VIM-19, a metallo-β-lactamase with increased carbapenemase activity from Escherichia coli and Klebsiella pneumoniae. Antimicrob Agents Chemother 2009; 54: 471-6.
14. Samuelsen O, Castanheira M, Walsh TR et al. Kinetic characterization of VIM-7, a divergent member of the VIM metallo-β-lactamase family. Antimicrob Agents Chemother 2008; 52: 2905-8.
15. Juan C, Beceiro A, Gutierrez O et al. Characterization of the new metallo-β-lactamase VIM-13 and its integron-borne gene from a Pseudomonas aeruginosa clinical isolate in Spain. Antimicrob Agents Chemother 2008; 52: 3589-96.
16. Galleni M, Lamotte-Brasseur J, Rossolini GM et al. Standard numbering scheme for class B β-lactamases. Antimicrob Agents Chemother 2001; 45: 660-3.
17. Marchiaro P, Tomatis PE, Mussi MA et al. Biochemical characterization of metallo-β-lactamase VIM-11 from a Pseudomonas aeruginosa clinical strain. Antimicrob Agents Chemother 2008; 52: 2250-2.
18. Ho SN, Hunt HD, Horton RM et al. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 1989; 77: 51-9.
19. Gacar GG, Midilli K, Kolayli F et al. Genetic and enzymatic properties of metallo-β-lactamase VIM-5 from a clinical isolate of Enterobacter cloacae. Antimicrob Agents Chemother 2005; 49: 4400-3.
20. Pournaras S, Ikonomidis A, Tzouvelekis LS et al. VIM-12, a novel plasmid-mediated metallo-β-lactamase from Klebsiella pneumoniae that resembles a VIM-1/VIM-2 hybrid. Antimicrob Agents Chemother 2005; 49: 5153-6.
21. Franceschini N, Caravelli B, Docquier JD et al. Purification and biochemical characterization of the VIM-1 metallo-β-lactamase. Antimicrob Agents Chemother 2000; 44: 3003-7.
22. Yamaguchi Y, Jin W, Matsunaga K et al. Crystallographic investigation of the inhibition mode of a VIM-2 metallo-β-lactamase from Pseudomonas aeruginosa by a mercaptocarboxylate inhibitor. J Med Chem 2007; 50: 6647-53.
23. Garcia-Saez I, Docquier JD, Rossolini GM et al. The three-dimensional structure of VIM-2, a Zn-β-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form. J Mol Biol 2008; 375: 604-11.
24. Concha NO, Janson CA, Rowling P et al. Crystal structure of the IMP-1 metallo β-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor. Biochemistry 2000; 39: 4288-98.