[en] An isolate of Klebsiella oxytoca carrying a novel IMP metallo-β-lactamase was discovered in Madrid, Spain. The bla(IMP-28) gene is part of a chromosomally located class I integron. The IMP-28 k(cat)/K(m) values for ampicillin, ceftazidime, and cefepime and, to a lesser extent, imipenem and meropenem, are clearly lower than those of IMP-1. The His306Gln mutation may induce important modifications of the L3 loop and thus of substrate accessibility and hydrolysis and be the main reason for this behavior.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Pérez-Llarena, FJ
Fernández, A
Zamorano, L
Kerff, Frédéric ; Université de Liège - ULiège > Centre d'ingénierie des protéines
Beceiro, A
Aracil, B
Cercenado, E
Miro, E
Oliver, A
Oteo, J
Navarro, F
Bou, G
Language :
English
Title :
Characterization of a novel IMP-28 metallo-β-lactamase from a Spanish Klebsiella oxytoca clinical isolate
Publication date :
August 2012
Journal title :
Antimicrobial Agents and Chemotherapy
ISSN :
0066-4804
eISSN :
1098-6596
Publisher :
American Society for Microbiology (ASM), Washington, United States - District of Columbia
Borgianni L, et al. 2011. Genetic context and biochemical characterization of the IMP-18 metallo-β-lactamase identified in a Pseudomonas aeruginosa isolate from the United States. Antimicrob. Agents Chemother. 55:140-145.
Bush K. 2001. New β-lactamases in gram-negative bacteria: diversity and impact on the selection of antimicrobial therapy. Clin. Infect. Dis. 32:1085-1089. (Pubitemid 32299644)
Docquier JD, et al. 2003. IMP-12, a new plasmid-encoded metallo-β-lactamase from a Pseudomonas putida clinical isolate. Antimicrob. Agents Chemother. 47:1522-1528.
García A, et al. 2007. Acquisition and diffusion of bla CTX-M-9 gene by R478-IncHI2 derivative plasmids. FEMS Microbiol. Lett. 271:71-77. (Pubitemid 46701057)
Garza-Ramos U, et al. 2008. Metallo-β-lactamase gene bla IMP-15 in a class 1 integron, In95, from Pseudomonas aeruginosa clinical isolates from a hospital in Mexico. Antimicrob. Agents Chemother. 52:2943-2946.
Iyobe S, et al. 2000. Amino acid substitutions in a variant of IMP-1 metallo-β-lactamase. Antimicrob. Agents Chemother. 44:2023-2027. (Pubitemid 30484421)
Laraki N, et al. 1999. Structure of In31, a blaIMP-containing Pseudomonas aeruginosa integron phyletically related to In5, which carries an unusual array of gene cassettes. Antimicrob. Agents Chemother. 43:890-901.
Laraki N, et al. 1999. Biochemical characterization of the Pseudomonas aeruginosa 101/1477 metallo-β-lactamase IMP-1 produced by Escherichia coli. Antimicrob. Agents Chemother. 43:902-906. (Pubitemid 29165755)
Liu SL, Hessel A, Sanderson KE. 1993. Genomic mapping with I-Ceu I, an intron-encoded endonuclease specific for genes for ribosomal RNA, in Salmonella spp., Escherichia coli, and other bacteria. Proc. Natl. Acad. Sci. U. S. A. 90:6874-6878. (Pubitemid 23207316)
Mallo S, et al. 2010. A tripeptide deletion in the R2 loop of the class C β-lactamase enzyme FOX-4 impairs cefoxitin hydrolysis and slightly increases susceptibility to β-lactamase inhibitors. J. Antimicrob. Chemother. 65:1187-1194.
Maltezou HC. 2009. Metallo-β-lactamases in Gram-negative bacteria: introducing the era of pan-resistance? Int. J. Antimicrob. Agents 33:405.e1-7.
Mendes RE, et al. 2007. Characterization of an integron carrying bla IMP-1 and a new aminoglycoside resistance gene, aac(6′)-31, and its dissemination among genetically unrelated clinical isolates in a Brazilian hospital. Antimicrob. Agents Chemother. 51:2611-2614.
Merino M, et al. 2010. Roles of changes in the L3 loop of the active site in the evolution of enzymatic activity of VIM-type metallo-β-lactamases. J. Antimicrob. Chemother. 65:1950-1954.
Neuwirth C, Siebor E, Robin F, Bonnet R. 2007. First occurrence of an IMP metallo-β-lactamase in Aeromonas caviae: IMP-19 in an isolate from France. Antimicrob. Agents Chemother. 51:4486-4488. (Pubitemid 350209909)
Pellegrini C, et al. 2009. Identification of blaIMP-22 in Pseudomonas spp. in urban wastewater and nosocomial environments: biochemical characterization of a new IMP metallo-enzyme variant and its genetic location. J. Antimicrob. Chemother. 63:901-908.
Pérez-Llarena FJ, et al. 2008. Structure-function studies of arginine at position 276 in CTX-M β-lactamases. J. Antimicrob. Chemother. 61:792-797.
Yano H, et al. 2001. Plasmid-encoded metallo-β-lactamase (IMP-6) conferring resistance to carbapenems, especially meropenem. Antimicrob. Agents Chemother. 45:1343-1348. (Pubitemid 32374100)
Zhao WH, Chen G, Ito R, Hu ZQ. 2009. Relevance of resistance levels to carbapenems and integron-borne blaIMP-1, blaIMP-7, blaIMP10 and blaVIM-2 in clinical isolates of Pseudomonas aeruginosa. J. Med. Microbiol. 58: 1080-1085.
