β-Lactamases identified in clinical isolates of Pseudomonas aeruginosa

References

• al Naiemi N, Duim B, Bart A. (2006). A CTX-M extended-spectrum β-lactamase in Pseudomonas aeruginosa and Stenotrophomonas maltophilia. J Med Microbiol 55, 1607–1608 .
   PubMed Web of Science ®Google Scholar
• Alibert-Franco S, Pradines B, Mahamoud A, Davin-Regli A, Pagès JM. (2009). Efflux mechanism, an attractive target to combat multidrug resistant Plasmodium falciparum and Pseudomonas aeruginosa. Curr Med Chem 16, 301–317.
   PubMed Web of Science ®Google Scholar
• Ambler RP. (1980). The structure of β-lactamases. Philos Trans R Soc Lond B Biol Sci 289, 321–331.
   PubMed Web of Science ®Google Scholar
• Andrade SS, Jones RN, Gales AC, Sader HS. (2003). Increasing prevalence of antimicrobial resistance among Pseudomonas aeruginosa isolates in Latin American medical centres: 5 year report of the SENTRY Antimicrobial Surveillance Program (1997–2001). J Antimicrob Chemother 52, 140–141.
   PubMed Web of Science ®Google Scholar
• Aubert D, Poirel L, Ali AB, Goldstein FW, Nordmann P. (2001a). OXA-35 is an OXA-10–related β–lactamase from Pseudomonas aeruginosa. J Antimicrob Chemother 48, 717–721.
   PubMed Web of Science ®Google Scholar
• Aubert D, Poirel L, Chevalier J, Leotard S, Pages JM, Nordmann P. (2001b). Oxacillinase-mediated resistance to cefepime and susceptibility to ceftazidime in Pseudomonas aeruginosa. Antimicrob Agents Chemother 45, 1615–1620.
   PubMed Web of Science ®Google Scholar
• Bahar G, Mazzariol A, Koncan R, Mert A, Fontana R, Rossolini GM, Cornaglia G. (2004). Detection of VIM-5 metallo-β-lactamase in a Pseudomonas aeruginosa clinical isolate from Turkey. J Antimicrob Chemother 54, 282–283.
   PubMed Web of Science ®Google Scholar
• Bassetti M, Nicolini L, Esposito S, Righi E, Viscoli C. (2009). Current status of newer carbapenems. Curr Med Chem 16, 564–575.
   PubMed Web of Science ®Google Scholar
• Bauernfeind A, Stemplinger I, Jungwirth R, Mangold P, Amann S, Akalin E, Anğ O, Bal C, Casellas JM. (1996). Characterization of β-lactamase gene blaPER–2, which encodes an extended-spectrum class A β-lactamase. Antimicrob Agents Chemother 40, 616–620.
   PubMed Web of Science ®Google Scholar
• Bonomo RA, Szabo D. (2006). Mechanisms of multidrug resistance in Acinetobacter species and Pseudomonas aeruginosa. Clin Infect Dis 43, S49–56.
   PubMed Web of Science ®Google Scholar
• Bradford PA. (2001). Extended-spectrum β-lactamases in the 21st century: characterization, epidemiology, detection of this important resistance threat. Clin Microbiol Rev 14, 933–951.
   PubMed Web of Science ®Google Scholar
• Burman LG, Park JT, Lindström EB, Boman HG. (1973). Resistance of Escherichia coli to penicillins: identification of the structural gene for the chromosomal penicillinase. J Bacteriol 116, 123–130.
   PubMed Web of Science ®Google Scholar
• Bush K. (1988). β-lactamase inhibitors from laboratory to clinic. Clin Microbiol Rev 1, 109–123.
   PubMedGoogle Scholar
• Bush K, Jacoby GA, Medeiros AA. (1995). A functional classification scheme for β-lactamases and its correlation with molecular structures. Antimicrob Agents Chemother 39, 1211–1233.
   PubMed Web of Science ®Google Scholar
• Bush K, Jacoby GA. (2010). Updated functional classification of β–lactamases. Antimicrob Agents Chemother 54, 969–976.
   PubMed Web of Science ®Google Scholar
• Cagnacci S, Gualco L, Roveta S, Mannelli S, Borgianni L, Docquier JD, Dodi F, Centanaro M, Debbia E, Marchese A, Rossolini GM. (2008). Bloodstream infections caused by multidrug-resistant Klebsiella pneumoniae producing the carbapenem-hydrolysing VIM-1 metallo-β-lactamase: first Italian outbreak. J Antimicrob Chemother 61, 296–300.
   PubMed Web of Science ®Google Scholar
• Castanheira M, Bell JM, Turnidge JD, Mathai D, Jones RN. (2009). Carbapenem resistance among Pseudomonas aeruginosa strains from India: evidence for nationwide endemicity of multiple metallo-b-lactamase clones (VIM-2, -5, -6, and -11 and the newly characterized VIM–18). Antimicrob Agents Chemother 53, 1225–1227.
   PubMed Web of Science ®Google Scholar
• Castanheira M, Toleman MA, Jones RN, Schmidt FJ, Walsh TR. (2004). Molecular characterization of a β-lactamase gene, blaGIM–1, encoding a new subclass of metallo-β-lactamase. Antimicrob Agents Chemother 48, 4654–4661.
   PubMed Web of Science ®Google Scholar
• Celenza G, Pellegrini C, Caccamo M, Segatore B, Amicosante G, Perilli M. (2006). Spread of blaCTX-M-type and blaPER–2 β-lactamase genes in clinical isolates from Bolivian hospitals. J Antimicrob Chemother 57, 975–978.
   PubMed Web of Science ®Google Scholar
• Chanawong A, M’Zali FH, Heritage J, Lulitanond A, Hawkey PM. (2001). SHV-12, SHV-5, SHV-2a and VEB-1 extended-spectrum β-lactamases in gram-negative bacteria isolated in a university hospital in Thailand. J Antimicrob Chemother 48, 839–852.
   PubMed Web of Science ®Google Scholar
• Chaïbi EB, Sirot D, Paul G, Labia R. (1999). Inhibitor-resistant TEM β-lactamases: phenotypic, genetic and biochemical characteristics. J Antimicrob Chemother 43, 447–458.
   PubMed Web of Science ®Google Scholar
• Couture F, Lachapelle J, Levesque RC. (1992). Phylogeny of LCR–1 and OXA–5 with class A and class D β-lactamases. Mol Microbiol 6, 1693–1705.
   PubMed Web of Science ®Google Scholar
• Crespo MP, Woodford N, Sinclair A, Kaufmann ME, Turton J, Glover J, Velez JD, Castaneda CR, Recalde M, Livermore DM. (2004). Outbreak of carbapenem-resistant Pseudomonas aeruginosa producing VIM-8, a novel metallo-β-lactamase, in a tertiary care center in Cali, Colombia. J Clin Microbiol 42, 5094–5101.
   PubMed Web of Science ®Google Scholar
• Danel F, Hall LM, Duke B Gur D, Livermore DM. (1999). OXA-17, a further extended-spectrum variant of OXA-10 β-lactamase, isolated from Pseudomonas aeruginosa. Antimicrob Agents Chemother 43, 1362–1366.
   PubMed Web of Science ®Google Scholar
• Danel F, Hall LM, Gur D, Livermore DM. (1995). OXA–14, another extended-spectrum variant of OXA-10. (PSE-2). β-lactamase from Pseudomonas aeruginosa. Antimicrob Agents Chemother 39, 1881–1884.
   PubMed Web of Science ®Google Scholar
• Danel F, Hall LM, Gur D, Livermore DM. (1997). OXA-15, an extended-spectrum variant of OXA-2 β-lactamase, isolated from a Pseudomonas aeruginosa strain. Antimicrob Agents Chemother 41, 785–790.
   PubMed Web of Science ®Google Scholar
• Danel F, Hall LM, Gur D, Livermore DM. (1998). OXA–16, a further extended–spectrum variant of OXA-10 β-lactamase, from two Pseudomonas aeruginosa isolates. Antimicrob Agents Chemother 42, 3117–3122.
   PubMed Web of Science ®Google Scholar
• Datta N, Kontomichalou P. (1965). Penicillinase synthesis controlled by infectious R factors in Enterobacteriaceae. Nature 208, 239–241.
   PubMed Web of Science ®Google Scholar
• Drawz SM, Bonomo RA. (2010). Three decades of β–lactamase inhibitors. Clin Microbiol Rev 23, 160–201.
   PubMed Web of Science ®Google Scholar
• Dubois V, Arpin C, Noury P, Quentin C. (2002a). Clinical strain of Pseudomonas aeruginosa carrying a blaTEM–21 gene located on a chromosomal interrupted TnA type transposon. Antimicrob Agents Chemother 46, 3624–3626.
   PubMed Web of Science ®Google Scholar
• Dubois V, Poirel L, Marie C, Arpin C, Nordmann P, Quentin C. (2002b). Molecular characterization of a novel class 1 integron containing blaGES-1 and a fused product of aac3-Ib/aac6′–Ib’ gene cassettes in Pseudomonas aeruginosa Antimicrob. Agents Chemother 46, 638–645.
   PubMed Web of Science ®Google Scholar
• Duljasz W, Gniadkowski M, Sitter S, Wojna A, Jebelean C. (2009). First organisms with acquired metallo-β-lactamases. (IMP-13, IMP-22, VIM-2). reported in Austria. Antimicrob Agents Chemother 53, 2221–2222.
   PubMed Web of Science ®Google Scholar
• Empel J, Filczak K, Mrówka A, Hryniewicz W, Livermore DM, Gniadkowski M. (2007). Outbreak of Pseudomonas aeruginosa infections with PER-1 extended-spectrum β-lactamase in Warsaw, Poland: further evidence for an international clonal complex. J Clin Microbiol 45, 2829–2834.
   PubMed Web of Science ®Google Scholar
• Galani I, Souli M, Chryssouli Z, Orlandou K, Giamarellou H. (2005). Characterization of a new integron containing blaVIM-1 and aac(6′)-IIc in an Enterobacter cloacae clinical isolate from Greece. J Antimicrob Chemother 55, 634–638.
   PubMed Web of Science ®Google Scholar
• Gales AC, Menezes LC, Silbert S, Sader HS. (2003). Dissemination in distinct Brazilian regions of an epidemic carbapenem-resistant Pseudomonas aeruginosa producing SPM metallo-β-lactamase. J Antimicrob Chemother 52, 699–702.
   PubMed Web of Science ®Google Scholar
• Garza-Ramos U, Morfin-Otero R, Sader HS, Jones RN, Hernández E, Rodriguez-Noriega E, Sanchez A, Carrillo B, Esparza-Ahumada S, Silva-Sanchez J. (2008). Metallo-β-lactamase gene blaIMP-15 in a class 1 integron, In95, from Pseudomonas aeruginosa clinical isolates from a hospital in Mexico. Antimicrob Agents Chemother 52, 2943–2946.
   PubMed Web of Science ®Google Scholar
• Gibb AP, Tribuddharat C, Moore RA, Louie TJ, Krulicki W, Livermore DM, Palepou MF, Woodford N. (2002). Nosocomial outbreak of carbapenem-resistant Pseudomonas aeruginosa with a new blaIMP allele, blaIMP-7. Antimicrob Agents Chemother 46, 255–258.
   PubMed Web of Science ®Google Scholar
• Gilbert DN, Moellering RC, Eliopoulos GM, Sande MA. (2005). The Sanford Guide to Antimicrobial Therapy 2005, 35th ed. Hyde Park, VT: Antimicrobial Therapy.
   Google Scholar
• Girlich D, Naas T, Leelaporn A, Poirel L, Fennewald M, Nordmann P. (2002). Nosocomial spread of the integron-located veb-1-like cassette encoding an extended-spectrum β-lactamase in Pseudomonas aeruginosa in Thailand. Clin Infect Dis 34, 603–611.
   PubMed Web of Science ®Google Scholar
• Girlich D, Naas T, Nordmann P. (2004). Biochemical characterization of the naturally occurring oxacillinase OXA–50 of Pseudomonas aeruginosa. Antimicrob Agents Chemother 48, 2043–2048.
   PubMed Web of Science ®Google Scholar
• Giuliani F, Docquier JD, Riccio ML Pagani, L Rossolini, GM. (2005). OXA-46, a new class D β–lactamase of narrow substrate specificity encoded by a blaVIM–1-containing integron from a Pseudomonas aeruginosa clinical isolate. Antimicrob Agents Chemother 49, 1973–1980.
   PubMed Web of Science ®Google Scholar
• Giwercman B, Lambert PA, Rosdahl VT, Shand GH, Høiby N. (1990). Rapid emergence of resistance in Pseudomonas aeruginosa in cystic fibrosis patients due to in–vivo selection of stable partially derepressed β-lactamase producing strains. J Antimicrob Chemother 26, 247–259.
   PubMed Web of Science ®Google Scholar
• Hall LM, Livermore DM, Gur D, Akova M, Akalin HE. (1993). OXA–11, an extended-spectrum variant of OXA–10. (PSE–2). β-lactamase from Pseudomonas aeruginosa. Antimicrob Agents Chemother 37, 1637–1644.
   PubMed Web of Science ®Google Scholar
• Hanson ND, Hossain A, Buck L, Moland ES, Thomson KS. (2006). First occurrence of a Pseudomonas aeruginosa isolate in the United States producing an IMP metallo-β-lactamase, IMP–18. Antimicrob Agents Chemother 50, 2272–2273.
   PubMed Web of Science ®Google Scholar
• Herbert S, Halvorsen DS, Leong T, Franklin C, Harrington G, Spelman D. (2007). Large outbreak of infection and colonization with gram-negative pathogens carrying the metallo-β-lactamase gene blaIMP-4 at a 320-bed tertiary hospital in Australia. Infect Control Hosp Epidemiol 28, 98–101.
   PubMed Web of Science ®Google Scholar
• Hu Z, Zhao WH. (2009). Identification of plasmid- and integron-borne blaIMP-1 and blaIMP-10 in clinical isolates of Serratia marcescens. J Med Microbiol 58, 217–221.
   PubMed Web of Science ®Google Scholar
• Iyobe S, Kusadokoro H, Takahashi A, Yomoda S, Okubo T, Nakamura A, O’Hara K. (2002). Detection of a variant metallo-β-lactamase, IMP-10, from two unrelated strains of Pseudomonas aeruginosa and an Alcaligenes xylosoxidans strain. Antimicrob Agents Chemother 46, 2014–2016.
   PubMed Web of Science ®Google Scholar
• Jacoby GA. (2009). AmpC β-lactamases. Clin Microbiol Rev 22, 161–182.
   PubMed Web of Science ®Google Scholar
• Jacoby GA, Matthew M. (1979). The distribution of β-lactamase genes on plasmids found in Pseudomonas. Plasmid 2, 41–47.
   PubMed Web of Science ®Google Scholar
• Juan C, Beceiro A, Gutiérrez O, Albertí S, Garau M, Pérez JL, Bou G, Oliver A. (2008). 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 52, 3589–3596.
   PubMed Web of Science ®Google Scholar
• Juan C, Mulet X, Zamorano L, Albertí S, Pérez JL, Oliver A. (2009). Detection of the novel extended-spectrum β-lactamase OXA–161 from a plasmid-located integron in Pseudomonas aeruginosa clinical isolates from Spain. Antimicrob Agents Chemother 53, 5288–5290.
   PubMed Web of Science ®Google Scholar
• Kliebe C, Nies BA, Meyer JF, Tolxdorff-Neutzling RM, Wiedemann B. (1985). Evolution of plasmid-coded resistance to broad-spectrum cephalosporins. Antimicrob Agents Chemother 28, 302–307.
   PubMed Web of Science ®Google Scholar
• Kong KF, Jayawardena SR, Del Puerto A, Wiehlmann L, Laabs U, Tümmler B, Mathee K. (2005). Characterization of poxB, a chromosomal-encoded Pseudomonas aeruginosa oxacillinase. Gene 358, 82–92.
   PubMed Web of Science ®Google Scholar
• Lachapelle J, Dufresne J, Levesque RC. (1991). Characterization of the blaCARB–3 gene encoding the carbenicillinase-3 β-lactamase of Pseudomonas aeruginosa. Gene 102, 7–12.
   PubMed Web of Science ®Google Scholar
• Lauretti L, Riccio ML, Mazzariol A, Cornaglia G, Amicosante G, Fontana R, Rossolini GM. (1999). Cloning and characterization of blaVIM, a new integron-borne metallo-β-lactamase gene from a Pseudomonas aeruginosa clinical isolate. Antimicrob Agents Chemother 43, 1584–1590.
   PubMed Web of Science ®Google Scholar
• Lister PD. (2000). β-Lactamase inhibitor combinations with extended-spectrum penicillins: factors influencing antibacterial activity against enterobacteriaceae and Pseudomonas aeruginosa. Pharmacotherapy 20, 213S–218S.
   PubMed Web of Science ®Google Scholar
• Lister PD. (2002). Chromosomally-encoded resistance mechanisms of Pseudomonas aeruginosa: therapeutic implications. Am J Pharmacogenomics 2, 235–243.
   PubMedGoogle Scholar
• Lister PD. (2007). Carbapenems in the USA: focus on doripenem. Expert Rev Anti Infect Ther 5, 793–809.
   PubMed Web of Science ®Google Scholar
• Livermore DM. (1995). β-Lactamases in laboratory and clinical resistance. Clin Microbiol Rev 8, 557–584.
   PubMed Web of Science ®Google Scholar
• Lodge JM, Minchin SD, Piddock LJ, Busby SJ. (1990). Cloning, sequencing and analysis of the structural gene and regulatory region of the Pseudomonas aeruginosa chromosomal ampC β-lactamase. Biochem J 272, 627–631.
   PubMed Web of Science ®Google Scholar
• Lombardi G, Luzzaro F, Docquier JD, Riccio ML, Perilli M, Colì A, Amicosante G, Rossolini GM, Toniolo A. (2002). Nosocomial infections caused by multidrug-resistant isolates of Pseudomonas putida producing VIM–1 metallo-β-lactamase. J Clin Microbiol 40, 4051–4055.
   PubMed Web of Science ®Google Scholar
• Marchandin H, Jean-Pierre H, De Champs C, Sirot D, Darbas H, Perigault PF, Carriere C. (2000). Production of a TEM-24 plasmid-mediated extended-spectrum β-lactamase by a clinical isolate of Pseudomonas aeruginosa. Antimicrob Agents Chemother 44, 213–216.
   PubMed Web of Science ®Google Scholar
• Matthew M, Hedges RW, Smith JT. (1979). Types of β-lactamase determined by plasmids in gram-negative bacteria. J Bacteriol 138, 657–662.
   PubMed Web of Science ®Google Scholar
• Mavroidi A, Tzelepi E, Tsakris A, Miriagou V, Sofianou D, Tzouvelekis LS. (2001). An integron-associated β-lactamase (IBC-2) from Pseudomonas aeruginosa is a variant of the extended-spectrum β-lactamase IBC-1. J Antimicrob Chemother 48, 627–630.
   PubMed Web of Science ®Google Scholar
• Mazel D. (2006). Integrons: agents of bacterial evolution. Nat Rev Microbiol 4, 608–620.
   PubMed Web of Science ®Google Scholar
• Mendes RE, Toleman MA, Ribeiro J, Sader HS, Jones RN, Walsh TR. (2004). Integron carrying a novel metallo-β-lactamase gene, blaIMP-16, a fused form of aminoglycoside-resistant gene aac(6′)-30/aac(6′)-Ib’: report from the SENTRY Antimicrobial Surveillance Program. Antimicrob Agents Chemother 48, 4693–4702.
   PubMed Web of Science ®Google Scholar
• Mitsuhashi S, Inoue M. (1981). Mechanisms of resistance to β-lactam antibiotics, In S Mitsuhashi. (ed), Beta-lactam antibiotics. Springer-Verlag, New York, pp. 41–56.
   Google Scholar
• Mugnier P, Casin I, Bouthors AT, Collatz E. (1998a). Novel OXA-10-derived extended-spectrum β-lactamases selected in vivo or in vitro. Antimicrob Agents Chemother 42, 3113–3116.
   PubMed Web of Science ®Google Scholar
• Mugnier P, Dubrous P, Casin I, Arlet G, Collatz E. (1996). A TEM-derived extended-spectrum β-lactamase in Pseudomonas aeruginosa. Antimicrob Agents Chemother 40, 2488–2493.
   PubMed Web of Science ®Google Scholar
• Mugnier P, Podglajen I, Goldstein FW, Collatz E. (1998b). Carbapenems as inhibitors of OXA-13, a novel, integron-encoded β-lactamase in Pseudomonas aeruginosa. Microbiology 144, 1021–1031.
   PubMed Web of Science ®Google Scholar
• Naas T, Philippon L, Poirel L, Ronco E, Nordmann P. (1999a). An SHV-derived extended-spectrum β-lactamase in Pseudomonas aeruginosa. Antimicrob Agents Chemother 43, 1281–1284.
   PubMed Web of Science ®Google Scholar
• Naas T, Poirel L, Karim A, Nordmann P. (1999b). Molecular characterization of In50, a class 1 integron encoding the gene for the extended-spectrum β-lactamase VEB-1 in Pseudomonas aeruginosa. FEMS Microbiol Lett 176, 411–419.
   PubMed Web of Science ®Google Scholar
• Naas T, Sougakoff W, Casetta A, Nordmann P. (1998). Molecular characterization of OXA-20, a novel class D β-lactamase, its integron from Pseudomonas aeruginosa. Antimicrob Agents Chemother 42, 2074–2083.
   PubMed Web of Science ®Google Scholar
• Naas T, Nordmann P. (1999). OXA-type β-lactamases. Curr Pharm Des 5, 865–879.
   PubMed Web of Science ®Google Scholar
• Naiemi NA, Duim B, Savelkoul PH, Spanjaard L, de Jonge E, Bart A, Vandenbroucke-Grauls CM, de Jong MD. (2005). Widespread transfer of resistance genes between bacterial species in an intensive care unit: implications for hospital epidemiology. J Clin Microbiol 43, 4862–4864.
   PubMed Web of Science ®Google Scholar
• Nordmann P, Cuzon G, Naas T. (2009). The real threat of Klebsiella pneumoniae carbapenemase-producing bacteria. Lancet Infect Dis 9, 228–236.
   PubMed Web of Science ®Google Scholar
• Nordmann P, Ronco E, Naas T, Duport C, Michel-Briand Y, Labia R. (1993). Characterization of a novel extended-spectrum β-lactamase from Pseudomonas aeruginosa. Antimicrob Agents Chemother 37, 962–969.
   PubMed Web of Science ®Google Scholar
• Nordmann P, Guibert M. (1998). Extended-spectrum β-lactamases in Pseudomonas aeruginosa. J Antimicrob Chemother 42, 128–132.
   PubMed Web of Science ®Google Scholar
• Obritsch MD, Fish DN, MacLaren R, Jung R. (2005). Nosocomial infections due to multidrug-resistant Pseudomonas aeruginosa: epidemiology and treatment options. Pharmacotherapy 25, 1353–1364.
   PubMed Web of Science ®Google Scholar
• Osano E, Arakawa Y, Wacharotayankun R, Ohta M, Horii T, Ito H, Yoshimura F, Kato N. (1994). Molecular characterization of an enterobacterial metallo β-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance. Antimicrob Agents Chemother 38, 71–78.
   PubMed Web of Science ®Google Scholar
• Pasteran F, Faccone D, Petroni A, Rapoport M, Galas M, Vázquez M, Procopio A. (2005). Novel variant blaVIM–11 of the metallo-β-lactamase blaVIM family in a GES-1 extended-spectrum-β-lactamase-producing Pseudomonas aeruginosa clinical isolate in Argentina. Antimicrob Agents Chemother 49, 474–475.
   PubMed Web of Science ®Google Scholar
• Paterson DL, Bonomo RA. (2005). Extended-spectrum β-lactamases: a clinical update. Clin Microbiol Rev 18, 657–686.
   PubMed Web of Science ®Google Scholar
• Petroni A, Melano RG, Saka HA, Garutti A, Mange L, Pasterán F, Rapoport M, Miranda M, Faccone D, Rossi A, Hoffman PS, Galas MF. (2004). CARB-9, a carbenicillinase encoded in the VCR region of Vibrio cholerae non-O1, non-O139 belongs to a family of cassette-encoded β-lactamases. Antimicrob Agents Chemother 48, 4042–4046.
   PubMed Web of Science ®Google Scholar
• Philippon AM, Paul GC, Jacoby GA. (1983). Properties of PSE-2 β-lactamase and genetic basis for its production in Pseudomonas aeruginosa. Antimicrob Agents Chemother 24, 362–369.
   PubMed Web of Science ®Google Scholar
• Philippon AM, Paul GC, Jacoby GA. (1986). New plasmid-mediated oxacillin-hydrolyzing β–lactamase in Pseudomonas aeruginosa. J Antimicrob Chemother 17, 415–422.
   PubMed Web of Science ®Google Scholar
• Philippon LN, Naas T, Bouthors AT, Barakett V, Nordmann P. (1997). OXA–18, a class D clavulanic acid-inhibited extended-spectrum β-lactamase from Pseudomonas aeruginosa. Antimicrob Agents Chemother 41, 2188–2195.
   PubMed Web of Science ®Google Scholar
• Picão RC, Poirel L, Gales AC, Nordmann P. (2009). Further identification of CTX–M–2 extended-spectrum β-lactamase in Pseudomonas aeruginosa. Antimicrob Agents Chemother 53, 2225–2226.
   PubMed Web of Science ®Google Scholar
• Poirel L, Brinas L, Fortineau N, Nordmann P. (2005a). Integron-encoded GES-type extended-spectrum β-lactamase with increased activity toward aztreonam in Pseudomonas aeruginosa. Antimicrob Agents Chemother 49, 3593–3597.
   PubMed Web of Science ®Google Scholar
• Poirel L, Brinas L, Verlinde A, Ide L, Nordmann P. (2005b). BEL-1, a novel clavulanic acid-inhibited extended-spectrum β-lactamase, the class 1 integron In120 in Pseudomonas aeruginosa. Antimicrob Agents Chemother 49, 3743–3748.
   PubMed Web of Science ®Google Scholar
• Poirel L, Gerome P, De Champs C, Stephanazzi J, Naas T, Nordmann P. (2002a). Integron-located oxa–32 gene cassette encoding an extended-spectrum variant of OXA-2 β-lactamase from Pseudomonas aeruginosa. Antimicrob Agents Chemother 46, 566–569.
   PubMed Web of Science ®Google Scholar
• Poirel L, Girlich D, Naas T, Nordmann P. (2001a). OXA-28, an extended-spectrum variant of OXA–10 β–lactamase from Pseudomonas aeruginosa and its plasmid- and integron-located gene. Antimicrob Agents Chemother 45, 447–453.
   PubMed Web of Science ®Google Scholar
• Poirel L, Le Thomas I, Naas T, Karim A, Nordmann P. (2000a). Biochemical sequence analyses of GES–1, a novel class A extended-spectrum β-lactamase, the class 1 integron In52 from Klebsiella pneumonia. Antimicrob Agents Chemother 44, 622–632.
   PubMed Web of Science ®Google Scholar
• Poirel L, Lebessi E, Castro M, Fèvre C, Foustoukou M, Nordmann P. (2004a). Nosocomial outbreak of extended-spectrum β-lactamase SHV-5-producing isolates of Pseudomonas aeruginosa in Athens, Greece. Antimicrob Agents Chemother 48, 2277–2279.
   PubMed Web of Science ®Google Scholar
• Poirel L, Magalhaes M, Lopes M, Nordmann P. (2004b). Molecular analysis of metallo-β-lactamase gene blaSPM-1-surrounding sequences from disseminated Pseudomonas aeruginosa isolates in Recife, Brazil. Antimicrob Agents Chemother 48, 1406–1409.
   PubMed Web of Science ®Google Scholar
• Poirel L, Naas T, Guibert M, Chaibi EB, Labia R, Nordmann P. (1999a). Molecular and biochemical characterization of VEB-1, a novel class A extended-spectrum β-lactamase encoded by an Escherichia coli integron gene. Antimicrob Agents Chemother 43, 573–581.
   PubMed Web of Science ®Google Scholar
• Poirel L, Naas T, Nicolas D, Collet L, Bellais S, Cavallo JD, Nordmann P. (2000b). Characterization of VIM-2, a carbapenem-hydrolyzing metallo-β-lactamase and its plasmid- and integron-borne gene from a Pseudomonas aeruginosa clinical isolate in France. Antimicrob Agents Chemother 44, 891–897.
   PubMed Web of Science ®Google Scholar
• Poirel, L, Naas, T, Nordmann, P. (2010). Diversity, epidemiology, genetics of class D beta-lactamases. Antimicrob Agents Chemother 54, 24–38.
   PubMed Web of Science ®Google Scholar
• Poirel L, Ronco E, Naas T, Nordmann P. (1999b). Extended-spectrum β-lactamase TEM-4 in Pseudomonas aeruginosa. Clin Microbiol Infect 5, 651–652.
   PubMedGoogle Scholar
• Poirel L, Rotimi VO, Mokaddas EM, Karim A, Nordmann P. (2001b). VEB-1-like extended-spectrum β-lactamases in Pseudomonas aeruginosa, Kuwait. Emerg Infect Dis 7, 468–470.
   PubMed Web of Science ®Google Scholar
• Poirel L, Weldhagen GF, De Champs C, Nordmann P. (2002b). A nosocomial outbreak of Pseudomonas aeruginosa isolates expressing the extended-spectrum β-lactamase GES-2 in South Africa. J Antimicrob Chemother 49, 561–565.
   PubMed Web of Science ®Google Scholar
• Poirel L, Weldhagen GF, Naas T, De Champs C, Dove MG, Nordmann P. (2001c). GES-2, a class A β-lactamase from Pseudomonas aeruginosa with increased hydrolysis of imipenem. Antimicrob Agents Chemother 45, 2598–2603.
   PubMed Web of Science ®Google Scholar
• Pournaras S, Tsakris A, Maniati M, Tzouvelekis LS, Maniatis AN. (2002). Novel variant blaVIM-4 of the metallo-β-lactamase gene blaVIM-1 in a clinical strain of Pseudomonas aeruginosa. Antimicrob Agents Chemother 46, 4026–4028.
   PubMed Web of Science ®Google Scholar
• Queenan AM, Bush K. (2007). Carbapenemases, the versatile β–lactamases. Clin Microbiol Rev 20, 440–458.
   PubMed Web of Science ®Google Scholar
• Rasmussen BA, Bush K. (1997). Carbapenem-hydrolyzing β-lactamases. Antimicrob Agents Chemother 41, 223–232 .
   PubMed Web of Science ®Google Scholar
• Riccio ML, Pallecchi L, Fontana R, Rossolini GM. (2001). In70 of plasmid pAX22, a blaVIM-1-containing integron carrying a new aminoglycoside phosphotransferase gene cassette. Antimicrob Agents Chemother 45, 1249–1253.
   PubMed Web of Science ®Google Scholar
• Rodríguez-Martínez JM, Poirel L, Nordmann P. (2009). Extended-spectrum cephalosporinases in Pseudomonas aeruginosa. Antimicrob Agents Chemother 53, 1766–1771.
   PubMed Web of Science ®Google Scholar
• Rossolini GM, Luzzaro F, Migliavacca R, Mugnaioli C, Pini B, De Luca F, Perilli M, Pollini S, Spalla M, Amicosante G, Toniolo A, Pagani L. (2008). First countrywide survey of acquired metallo-β-lactamases in gram-negative pathogens in Italy. Antimicrob Agents Chemother 52, 4023–4029.
   PubMed Web of Science ®Google Scholar
• Ryoo NH, Lee K, Lim JB, Lee YH, Bae IK, Jeong SH. (2009). Outbreak by meropenem-resistant Pseudomonas aeruginosa producing IMP-6 metallo-β-lactamase in a Korean hospital. Diagn Microbiol Infect Dis 63, 115–117.
   PubMed Web of Science ®Google Scholar
• Sader HS, Reis AO, Silbert S, Gales AC. (2005). IMPs, VIMs and SPMs, the diversity of metallo-β-lactamases produced by carbapenem-resistant Pseudomonas aeruginosa in a Brazilian hospital. Clin Microbiol Infect 11, 73–76.
   PubMed Web of Science ®Google Scholar
• Sanschagrin F, Bejaoui N, Levesque RC. (1998). Structure of CARB–4 and AER–1 carbenicillin-hydrolyzing β-lactamases. Antimicrob Agents Chemother 42, 1966–1972.
   PubMed Web of Science ®Google Scholar
• Schneider I, Keuleyan E, Rasshofer R, Markovska R, Queenan AM, Bauernfeind A. (2008). VIM–15 and VIM–16, two new VIM-2-like metallo-β-lactamases in Pseudomonas aeruginosa isolates from Bulgaria and Germany. Antimicrob Agents Chemother 52, 2977–2979.
   PubMed Web of Science ®Google Scholar
• Scoulica EV, Neonakis IK, Gikas AI, Tselentis YJ. (2004). Spread of blaVIM–1–producing E coli in a university hospital in Greece Genetic analysis of the integron carrying the blaVIM–1 metallo-β-lactamase gene. Diagn Microbiol Infect Dis 48, 167–172.
   PubMed Web of Science ®Google Scholar
• Shahid M, Sobia F, Singh A, Malik A, Khan HM, Jonas D, Hawkey PM. (2009). β-lactams and β-lactamase-inhibitors in current- or potential-clinical practice, a comprehensive update. Crit Rev Microbiol 35, 81–108 .
   PubMed Web of Science ®Google Scholar
• Shibata N, Doi Y, Yamane K, Yagi T, Kurokawa H, Shibayama K, Kato H, Kai K, Arakawa Y. (2003). PCR typing of genetic determinants for metallo-β-lactamases and integrases carried by gram–negative bacteria isolated in Japan, with focus on the class 3 integron. J Clin Microbiol 41, 5407–5413.
   PubMed Web of Science ®Google Scholar
• Siarkou VI, Vitti D, Protonotariou E, Ikonomidis A, Sofianou D. (2009). Molecular epidemiology of outbreak-related Pseudomonas aeruginosa strains carrying the novel variant blaVIM–17 metallo-β-lactamase gene. Antimicrob Agents Chemother 53, 1325–1330.
   PubMed Web of Science ®Google Scholar
• Stokes HW, Hall RM.(1989). A novel family of potentially mobile DNA elements encoding site-specific gene-integration functions, integrons. Mol Microbiol 3, 1669–1683.
   PubMed Web of Science ®Google Scholar
• Tam VH, Schilling AN, LaRocco MT, Gentry LO, Lolans K, Quinn JP, Garey KW. (2007). Prevalence of AmpC over-expression in bloodstream isolates of Pseudomonas aeruginosa. Clin Microbiol Infect 13, 413–418.
   PubMed Web of Science ®Google Scholar
• Tassios PT, Gennimata V, Spaliara-Kalogeropoulou L, Kairis D, Koutsia C, Vatopoulos AC, Legakis NJ. (1997). Multiresistant Pseudomonas aeruginosa serogroup O,11 outbreak in an intensive care unit. Clin Microbiol Infect 3, 621–628.
   PubMedGoogle Scholar
• Toleman MA, Biedenbach D, Bennett D, Jones RN, Walsh TR. (2003a). Genetic characterization of a novel metallo-β-lactamase gene, blaIMP–13, harboured by a novel Tn5051-type transposon disseminating carbapenemase genes in Europe, report from the SENTRY worldwide antimicrobial surveillance programme. J Antimicrob Chemother 52, 583–590.
   PubMed Web of Science ®Google Scholar
• Toleman MA, Rolston K, Jones RN, Walsh TR. (2003b). Molecular and biochemical characterization of OXA-45, an extended-spectrum class 2d’ β-lactamase in Pseudomonas aeruginosa. Antimicrob Agents Chemother 47, 2859–2863.
   PubMed Web of Science ®Google Scholar
• Toleman MA, Rolston K, Jones RN, Walsh TR. (2004). blaVIM–7, an evolutionarily distinct metallo-β-lactamase gene in a Pseudomonas aeruginosa isolate from the United States. Antimicrob Agents Chemother 48, 329–332.
   PubMed Web of Science ®Google Scholar
• Toleman MA, Simm AM, Murphy TA, Gales AC, Biedenbach DJ, Jones RN, Walsh TR. (2002). Molecular characterization of SPM-1, a novel metallo-β-lactamase isolated in Latin America, report from the SENTRY antimicrobial surveillance programme. J Antimicrob Chemother 50, 673–679.
   PubMed Web of Science ®Google Scholar
• Tsakris A, Ikonomidis A, Pournaras S, Tzouvelekis LS, Sofianou D, Legakis NJ, Maniatis AN. (2006). VIM-1 metallo-β-lactamase in Acinetobacter baumannii. Emerg Infect Dis 12, 981–983.
   PubMed Web of Science ®Google Scholar
• Tzouvelekis LS, Bonomo RA. (1999). SHV-type β-lactamases. Curr Pharm Des 5, 847–864.
   PubMed Web of Science ®Google Scholar
• Vahaboglu H, Oztürk R, Aygün G, Coşkunkan F, Yaman A, Kaygusuz A, Leblebicioglu H, Balik I, Aydin K, Otkun M. (1997). Widespread detection of PER-1-type extended-spectrum β–lactamases among nosocomial Acinetobacter and Pseudomonas aeruginosa isolates in Turkey, a nationwide multicenter study. Antimicrob Agents Chemother 41, 2265–2269.
   PubMed Web of Science ®Google Scholar
• Villegas MV, Lolans K, Correa A, Kattan JN, Lopez JA, Quinn JP, Colombian Nosocomial Resistance Study Group. (2007). First identification of Pseudomonas aeruginosa isolates producing a KPC-type carbapenem-hydrolyzing β-lactamase. Antimicrob Agents Chemother 51, 1553–1555 .
   PubMed Web of Science ®Google Scholar
• Vourli S, Tsorlini H, Katsifa H, Polemis M, Tzouvelekis LS, Kontodimou A, Vatopoulos AC. (2006). Emergence of Proteus mirabilis carrying the bla metallo-β-lactamase gene. Clin Microbiol Infect 12, 691–694.
   PubMed Web of Science ®Google Scholar
• Waley SG. (1992). β–Lactamase, mechanism of action, p 198–228 In M I Page. (ed), The chemistry of β-lactams. Chapman and Hall, London.
   Google Scholar
• Walsh TR, Toleman MA, Poirel L, Nordmann P. (2005). Metallo-β-lactamases, the quiet before the storm? Clin Microbiol Rev 18, 306–325.
   PubMed Web of Science ®Google Scholar
• Walther-Rasmussen J, Høiby N. (2007). Class A carbapenemases. J Antimicrob Chemother 60, 470–482.
   PubMed Web of Science ®Google Scholar
• Wang C, Cai P, Chang D, Mi Z. (2006). A Pseudomonas aeruginosa isolate producing the GES-5 extended-spectrum β-lactamase. J Antimicrob Chemother 57, 1261–1262.
   PubMed Web of Science ®Google Scholar
• Watanabe M, Iyobe S, Inoue M, Mitsuhashi S. (1991). Transferable imipenem resistance in Pseudomonas aeruginosa. Antimicrob Agents Chemother 35, 147–151 .
   PubMed Web of Science ®Google Scholar
• Weile J, Rahmig H, Gfröer S, Schroeppel K, Knabbe C, Susa M. (2007). First detection of a VIM-1 metallo-β-lactamase in a carbapenem-resistant Citrobacter freundii clinical isolate in an acute hospital in Germany. Scand J Infect Dis 39, 264–266.
   PubMed Web of Science ®Google Scholar
• Weldhagen GF, Poirel L, Nordmann P. (2003). Ambler class A extended-spectrum β-lactamases in Pseudomonas aeruginosa, novel developments and clinical impact. Antimicrob Agents Chemother 47, 2385–2392.
   PubMed Web of Science ®Google Scholar
• Wisplinghoff H, Bischoff T, Tallent SM, Seifert H, Wenzel RP, Edmond MB. (2004). Nosocomial bloodstream infections in US hospitals, analysis of 24,179 cases from a prospective nationwide surveillance study. Clin Infect Dis 39, 309–317.
   PubMed Web of Science ®Google Scholar
• Wolter DJ, Kurpiel PM, Woodford N, Palepou MF, Goering RV, Hanson ND. (2009). Phenotypic and enzymatic comparative analysis of the novel KPC variant KPC-5 and its evolutionary variants, KPC-2 and KPC-4. Antimicrob Agents Chemother 53, 557–562.
   PubMed Web of Science ®Google Scholar
• Woodford N, Zhang J, Kaufmann ME, Yarde S, Tomas Mdel M, Faris C, Vardhan MS, Dawson S, Cotterill SL, Livermore DM. (2008). Detection of Pseudomonas aeruginosa isolates producing VEB-type extended-spectrum β-lactamases in the United Kingdom. J Antimicrob Chemother 62, 1265–1268.
   PubMed Web of Science ®Google Scholar
• Xiong J, Hynes MF, Ye H, Chen H, Yang Y, M’zali F, Hawkey PM, Guangzhou Antibiotic Resistance Study Group. (2006). blaIMP-9 and its association with large plasmids carried by Pseudomonas aeruginosa isolates from the People’s Republic of China. Antimicrob Agents Chemother 50, 355–358.
   PubMed Web of Science ®Google Scholar
• Yan JJ, Hsueh PR, Ko WC, Luh KT, Tsai SH, Wu HM, Wu JJ. (2001). Metallo-β-lactamases in clinical Pseudomonas isolates in Taiwan and identification of VIM–3, a novel variant of the VIM-2 enzyme. Antimicrob Agents Chemother 45, 2224–2228.
   PubMed Web of Science ®Google Scholar
• Yan JJ, Hsueh PR, Lu JJ, Chang FY, Ko WC, Wu JJ. (2006). Characterization of acquired β-lactamases and their genetic support in multidrug–resistant Pseudomonas aeruginosa isolates in Taiwan, the prevalence of unusual integrons. J Antimicrob Chemother 58, 530–536.
   PubMed Web of Science ®Google Scholar
• Yigit H, Queenan AM, Anderson GJ, Domenech-Sanchez A, Biddle JW, Steward CD, Alberti S, Bush K, Tenover FC. (2001). Novel carbapenem-hydrolyzing β-lactamase, KPC-1, from a carbapenem-resistant strain of Klebsiella pneumonia. Antimicrob Agents Chemother 45, 1151–1161.
   PubMed Web of Science ®Google Scholar
• Yoshimura F, Nikaido H. (1982). Permeability of Pseudomonas aeruginosa outer membrane to hydrophilic solutes. J Bacteriol 152, 636–642.
   PubMed Web of Science ®Google Scholar
• Zhao WH, Chen G, Ito R, Hu ZQ. (2009). Relevance of resistance levels to carbapenems and integron-borne blaIMP-1, blaIMP-7, blaIMP-10 and blaVIM-2 in clinical isolates of Pseudomonas aeruginosa. J Med Microbiol 58, 1080–1085.
   PubMed Web of Science ®Google Scholar