A structure-based classification of class A β-Lactamases, a broadly diverse family of enzymes

Clinical Microbiology Reviews

Volumn 29, Issue 1, 2016, Pages 29-57

  Philippon, Alain ^a   Slama, Patrick ^b   Dény, Paul ^c   Labia, Roger ^d  

^a Laboratoire de Bacteriologie Groupe   (France)

^b Independent Research   (France)

^c UNIVERSITÉ SORBONNE NOUVELLE PARIS 3   (France)

^d UNIVERSITÉ DE BREST   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AZTREONAM; BETA LACTAMASE; CEFTAZIDIME; PENICILLIN DERIVATIVE;

AMINO ACID SEQUENCE; ANTIBIOTIC RESISTANCE; BACTEROIDALES; BETAPROTEOBACTERIA; DEINOCOCCUS RADIODURANS; ENTEROBACTERIACEAE; ENZYME ACTIVITY; FLAVOBACTERIALES; FUSOBACTERIUM NUCLEATUM; GAMMAPROTEOBACTERIA; GENE CLUSTER; GENE SEQUENCE; MICROBIAL DIVERSITY; MOLECULAR GENETICS; MORITELLA; MYCOBACTERIUM ABSCESSUS; MYCOBACTERIUM TUBERCULOSIS; PHYLOGENY; POINT MUTATION; PROTEIN ENGINEERING; PSEUDOMONAS AERUGINOSA; REVIEW; SEQUENCE ANALYSIS; SERRATIA MARCESCENS; SPHINGOBACTERIALES; THERMOSYNECHOCOCCUS ELONGATUS; X RAY CRYSTALLOGRAPHY; YERSINIA ENTEROCOLITICA; BACTERIUM; CHEMISTRY; CLASSIFICATION; ENZYMOLOGY; GENETIC VARIATION; GENETICS; GENOTYPE; METABOLISM; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION;

BACTERIA; BETA-LACTAMASES; CRYSTALLOGRAPHY, X-RAY; GENETIC VARIATION; GENOTYPE; PHYLOGENY; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84945977754     PISSN: 08938512     EISSN: 10986618     Source Type: Journal    
DOI: 10.1128/CMR.00019-15     Document Type: Review

References (197)

1. Sawai T, Mitsuhashi S, Yamagishi S. 1968. Drug resistance of enteric bacteria. XIV. Comparison of β-lactamases in gram-negative rod bacteria resistant to a-aminobenzylpenicillin. Jpn J Microbiol 12:423-434.
2. Richmond MH, Sykes RB. 1973. The β-lactamases of gram-negative bacteria and their possible physiological role, p 31-88. In Rose AH, TempestDW(ed), Advances in microbial physiology, vol 9. Academic Press, New York, NY.
3. Medeiros AA. 1997. Evolution and dissemination of β-lactamases accelerated by generations of β-lactam antibiotics. Clin Infect Dis 24(Suppl 1):S19 -S45.
4. Bush K, Jacoby GA, Medeiros AA. 1995. A functional classification scheme for β-lactamases and its correlation with molecular structure. Antimicrob Agents Chemother 39:1211-1133. http://dx.doi.org/10.1128/AAC.39.6.1211.
5. Bush K, Jacoby GA. 2010. Updated functional classification of β-lactamases. Antimicrob Agents Chemother 54:969-976. http://dx.doi.org/10.1128/AAC.01009-09.
6. Ambler RP. 1980. The structure of β-lactamases. Philos Trans R Soc Lond B Biol Sci 289:321-331. http://dx.doi.org/10.1098/rstb.1980.0049.
7. Galleni M, Lamotte-Brasseur J, Rossolini GM, Spencer J, Dideberg O, Frère JM. 2001. Standard numbering scheme for class B β-lactamases. Antimicrob Agents Chemother 45:660-663. http://dx.doi.org/10.1128/AAC.45.3.660-663.2001.
8. Bush K, Fisher JF. 2011. Epidemiological expansion, structural studies, and clinical challenges of new β-lactamases from gram-negative bacteria. Annu Rev Microbiol 65:455-478. http://dx.doi.org/10.1146/annurev -micro-090110-102911.
9. Buchan BW, Ledeboer NA. 2014. Emerging technologies for the clinical microbiology laboratory. Clin Microbiol Rev 27:783-822. http://dx.doi.org/10.1128/CMR.00003-14.
10. Hall BG, Barlow M. 2004. Evolution of the serine β-lactamases: past, present and future. Drug Resist Updat 7:111-123. http://dx.doi.org/10.1016/j.drup.2004.02.003.
11. Urbach C, Fastrez J, Soumillion P. 2008. A new family of cyanobacterial penicillin-binding proteins. A missing link in the evolution of class A β-lactamases. J Biol Chem 283:32516-32526. http://dx.doi.org/10.1074/jbc.M805375200.
12. Matagne A, Lamotte-Brasseur J, Frère JM. 1998. Catalytic properties of class A β-lactamases: efficiency and diversity. Biochem J 330:581-598. http://dx.doi.org/10.1042/bj3300581.
13. Bush K. 2013. The ABCD's of β-lactamase nomenclature. J Infect Chemother 19:549-559. http://dx.doi.org/10.1007/s10156-013-0640-7.
14. Galán JC, Reig M, Navas A, Baquero F, Blazquez J. 2000. ACI-1 from Acidaminococcus fermentans: characterization of the first β-lactamase in anaerobic cocci. Antimicrob Agents Chemother 44:3144-3149. http://dx.doi.org/10.1128/AAC.44.11.3144-3149.2000.
15. Weng SF, Chao YF, Lin JW. 2004. Identification and characteristic analysis of the ampC gene encoding β-lactamase from Vibrio fischeri. Biochem Biophys ResCommun314:838-843. http://dx.doi.org/10.1016/j.bbrc.2003.12.171.
16. Poirel L, Laurent F, Naas T, Labia R, Boiron P, Nordmann P. 2001. Molecular and biochemical analysis of AST-1, a class Aβ-lactamase from Nocardia asteroides sensu stricto. Antimicrob Agents Chemother 45: 878-882. http://dx.doi.org/10.1128/AAC.45.3.878-882.2001.
17. Girlich D, Leclercq R, Naas T, Nordmann P. 2007. Molecular and biochemical characterization of the chromosome-encoded class A β-lactamase BCL-1 from Bacillus clausii. Antimicrob Agents Chemother 51: 4009-4014. http://dx.doi.org/10.1128/AAC.00537-07.
18. Poirel L, Brinas L, Verlinde A, Ide L, Nordmann P. 2005. BEL-1, a novel clavulanic acid-inhibited extended-spectrum β-lactamase, and the class 1 integron In120 in Pseudomonas aeruginosa. Antimicrob Agents Chemother 49:3743-3748. http://dx.doi.org/10.1128/AAC.49.9.3743-3748.2005.
19. Glupczynski Y, Bogaerts P, Deplano A, Berhin C, Huang TD, Van Eldere J, Rodriguez-Villalobos HJ. 2010. Detection and characterization of class A extended-spectrum-β-lactamase-producing Pseudomonas aeruginosa isolates in Belgian hospitals. Antimicrob Agents Chemother 65:866-871. http://dx.doi.org/10.1093/jac/dkq048.
20. Bonnet R, Sampaio JLM, Chanal C, Sirot D, de Champs C, Viallard JL, Labia R, Sirot J. 2000. A novel class A extended-spectrum β-lactamase (BES-1) in Serratia marcescens isolated in Brazil. Antimicrob Agents Chemother 44:3061-3068. http://dx.doi.org/10.1128/AAC.44.11.3061-3068.2000.
21. Girlich D, Poirel L, Nordmann P. 2010. Novel ambler class A carbapenem- hydrolyzing β-lactamase from a Pseudomonas fluorescens isolate from the Seine River, Paris, France. Antimicrob Agents Chemother 54: 328-332. http://dx.doi.org/10.1128/AAC.00961-09.
22. Hackbarth CJ, Unsal I, Chambers HF. 1997. Cloning and sequence analysis of a class A β-lactamase from Mycobacterium tuberculosis H37Ra. Antimicrob Agents Chemother 41:1182-1185.
23. Wang F, Cassidy C, Sacchettini JC. 2006. Crystal structure and activity studies of the Mycobacterium tuberculosis β-lactamase reveal its critical role in resistance to β-lactam antibiotics. Antimicrob Agents Chemother 50:2762-2771. http://dx.doi.org/10.1128/AAC.00320-06.
24. Lartigue MF, Poirel L, Fortineau N, Nordmann P. 2005. Chromosome- borne class A BOR-1 β-lactamase of Bordetella bronchiseptica and Bordetella parapertussis. Antimicrob Agents Chemother 49:2565-2567. http://dx.doi.org/10.1128/AAC.49.6.2565-2567.2005.
25. Cheung TK, Ho PL, Woo PC, Yuen KY, Chau PY. 2002. Cloning and expression of class A β-lactamase gene blaA(BPS) in Burkholderia pseudomallei. Antimicrob Agents Chemother 46:1132-1135. http://dx.doi.org/10.1128/AAC.46.4.1132-1135.2002.
26. Yi H, Cho KH, Cho YS, Kim K, Nierman WC, Kim HS. 2012. Twelve positions in a β-lactamase that can expand its substrate spectrum with a single amino acid substitution. PLoS One 7:e37585. http://dx.doi.org/10.1371/journal.pone.0037585.
27. Yi H, Kim K, Cho KH, Jung O, Kim HS. 2012. Substrate spectrum extension of PenA in Burkholderia thailandensis with a single amino acid deletion, Glu168del. Antimicrob Agents Chemother 56:4005-4008. http://dx.doi.org/10.1128/AAC.00598-12.
28. Meziane-Cherif D, Decré D, Høiby EA, Courvalin P, Périchon B. 2008. Genetic and biochemical characterization of CAD-1, a chromosomally encoded new class A penicillinase from Carnobacterium divergens. Antimicrob Agents Chemother 52:551-556. http://dx.doi.org/10.1128/AAC.01145-07.
29. Bellais S, Naas T, Nordmann P. 2002. Molecular and biochemical characterization of Ambler class A extended-spectrum β-lactamase CGA-1 from Chryseobacterium gleum. Antimicrob Agents Chemother 46:966-970. http://dx.doi.org/10.1128/AAC.46.4.966-970.2002.
30. Matsumoto T, Nagata M, Ishimine N, Kawasaki K, Yamauchi K, Hidaka E, Kasuga E, Horiuchi K, Oana K, Kawakami Y, Honda T. 2012. Characterization of CIA-1, an Ambler class A extended-spectrum β-lactamase from Chryseobacterium indologenes. Antimicrob Agents Chemother 56:588-590. http://dx.doi.org/10.1128/AAC.05165-11.
31. Petrella S, Renard M, Ziental-Gelus N, Clermont D, Jarlier V, Sougakoff W. 2006. Characterization of the chromosomal class A β-lactamase CKO from Citrobacter koseri. FEMS Microbiol Lett 254:285-292. http://dx.doi.org/10.1111/j.1574-6968.2005.00028.x.
32. Rossolini GM, Franceschini N, Caravelli B, Riccio ML, Galleni M, Frère JM, Amicosante G. 1999. Cloning of a Chryseobacterium (Flavobacterium) meningosepticum chromosomal gene (blaACME) encoding an extended-spectrum class A β-lactamase related to the Bacteroides cephalosporinases and the VEB-1 and PER β-lactamases. Antimicrob Agents Chemother 43:2193-2199.
33. Guillon H, Eb F, Mammeri H. 2010. Characterization of CSP-1, a novel extended-spectrum β-lactamase produced by a clinical isolate of Capnocytophaga sputigena. Antimicrob Agents Chemother 54:2231-2234. http://dx.doi.org/10.1128/AAC.00791-09.
34. Bauernfeind A, Stemplinger I, Jungwirth R, Casellas JM. 1996. Sequences of β-lactamase genes encoding CTX-M-1 (MEN-1) and CTXM- 2 and relationship of their amino acid sequences with those of other β-lactamases. Antimicrob Agents Chemother 40:509-513.
35. Bonnet R, Sampaio JLM, Labia R, de Champs C, Sirot D, Chanal C, Sirot J. 2000. A novel CTX-M β-lactamase (CTX-M-8) in cefotaximeresistant Enterobacteriaceae isolated in Brazil. Antimicrob Agents Chemother 44:1936-1942. http://dx.doi.org/10.1128/AAC.44.7.1936-1942.2000.
36. Morin AS, Poirel L, Mory F, Labia R, Nordmann P. 2002. Biochemicalgenetic analysis and distribution of DES-1, an Ambler class A extendedspectrum β-lactamase from Desulfovibrio desulfuricans. Antimicrob Agents Chemother 46:3215-3222. http://dx.doi.org/10.1128/AAC.46.10.3215-3222.2002.
37. Vimont S, Poirel L, Naas T, Nordmann P. 2002. Identification of a chromosome-borne expanded-spectrum class A β-lactamase from Erwinia persicina. Antimicrob Agents Chemother 46:3401-3405. http://dx.doi.org/10.1128/AAC.46.11.3401-3405.2002.
38. Laurent F, Poirel L, Naas T, Chaibi EB, Labia R, Boiron P, Nordmann P. 1999. Biochemical-genetic analysis and distribution of FAR-1, a class A β-lactamase from Nocardia farcinica. Antimicrob Agents Chemother 43:1644-1650.
39. Péduzzi J, Farzaneh S, Reynaud A, Barthélémy M, Labia R. 1997. Characterization and amino acid sequence analysis of a new oxyimino cephalosporin-hydrolyzing class A β-lactamase from Serratia fonticola CUV. Biochim Biophys Acta 1341:58-70. http://dx.doi.org/10.1016/S0167-4838(97)00020-4.
40. Toth M, Vakulenko V, Antunes NT, Frase H, Vakulenko SB. 2012. Class A carbapenemase FPH-1 from Francisella philomiragia. Antimicrob Agents Chemother 56:2852-2857. http://dx.doi.org/10.1128/AAC.00223-12.
41. Antunes NT, Frase H, Toth M, Vakulenko SB. 2012. The class A β-lactamase FTU-1 is native to Francisella tularensis. Antimicrob Agents Chemother 56:666-671. http://dx.doi.org/10.1128/AAC.05305-11.
42. Poirel L, Le Thomas I, Naas T, Karim A, Nordmann P. 2000. Biochemical sequence analyses of GES-1, a novel class A extended-spectrum β-lactamase, and the class 1 integron In52 from Klebsiella pneumoniae. Antimicrob Agents Chemother 44:622-632. http://dx.doi.org/10.1128/AAC.44.3.622-632.2000.
43. Naas T, Aubert D, Ozcan A, Nordmann P. 2007. Chromosomeencoded narrow-spectrum Ambler class A β-lactamase GIL-1 from Citrobacter gillenii. Antimicrob Agents Chemother 51:1365-1372. http://dx.doi.org/10.1128/AAC.01152-06.
44. Beauchef-Havard A, Arlet G, Gautier V, Labia R, Grimont P, Philippon A. 2003. Molecular and biochemical characterization of a novel class A β-lactamase (HER-1) from Escherichia hermannii. Antimicrob Agents Chemother 47:2669 -2673. http://dx.doi.org/10.1128/AAC.47.8.2669 -2673.2003.
45. Liassine N, Madec S, Ninet B, Metral C, Fouchereau-Péron M, Labia R, Auckenthaler R. 2002. Postneurosurgical meningitis due to Proteus penneri with selection of a ceftriaxone-resistant isolate: analysis of chromosomal class A β-lactamase HugA and its LysR-type regulatory protein HugR. Antimicrob Agents Chemother 46:216-219. http://dx.doi.org/10.1128/AAC.46.1.216-219.2002.
46. Giakkoupi P, Tzouvelekis LS, Tsakris A, Loukova V, Sofianou D, Tzelepi E. 2000. IBC-1, a novel integron-associated class A β-lactamase with extended-spectrum properties produced by an Enterobacter cloacae clinical strain. Antimicrob Agents Chemother 44:2247-2253. http://dx.doi.org/10.1128/AAC.44.9.2247-2253.2000.
47. Rasmussen BA, Bush K, Keeney D, Yang Y, Hare R, O'Gara C, Medeiros AA. 1996. Characterization of IMI-1 β-lactamase, a class A carbapenem-hydrolyzing enzyme from Enterobacter cloacae. Antimicrob Agents Chemother 40:2080-2086.
48. Humeniuk C, Arlet G, Gautier V, Grimont P, Labia R, Philippon A. 2002. β-lactamases of Kluyvera ascorbata, probable progenitors of some plasmid-encoded CTX-M types. Antimicrob Agents Chemother 46: 3045-3049. http://dx.doi.org/10.1128/AAC.46.9.3045-3049.2002.
49. Decousser JW, Poirel L, Nordmann P. 2001. Characterization of a chromosomally encoded extended-spectrum class A β-lactamase from Kluyvera cryocrescens. Antimicrob Agents Chemother 45:3595-3598. http://dx.doi.org/10.1128/AAC.45.12.3595-3598.2001.
50. Poirel L, Kämpfer P, Nordmann P. 2002. Chromosome-encoded Ambler class A β-lactamase of Kluyvera georgiana, a probable progenitor of a subgroup of CTX-M extended-spectrum β-lactamases. Antimicrob Agents Chemother 46:4038-4040. http://dx.doi.org/10.1128/AAC.46.12.4038-4040.2002.
51. Smith Moland E, Hanson ND, Herrera VL, Black JA, Lockhart TJ, Hossain A, Johnson JA, Goering RV, Thomson KS. 2003. Plasmidmediated, carbapenem-hydrolysing β-lactamase, KPC-2, in Klebsiella pneumoniae isolates. J Antimicrob Chemother 51:711-714. http://dx.doi.org/10.1093/jac/dkg124.
52. Poirel L, Cattoir V, Soares A, Soussy CJ, Nordmann P. 2007. Novel Ambler class A β-lactamase LAP-1 and its association with the plasmidmediated quinolone resistance determinant QnrS1. Antimicrob Agents Chemother 51:631-637. http://dx.doi.org/10.1128/AAC.01082-06.
53. Doublet B, Robin F, Casin I, Fabre L, Le Flèche A, Bonnet R, Weill FX. 2010. Molecular and biochemical characterization of the natural chromosome- encoded class A β-lactamase from Pseudomonas luteola. Antimicrob Agents Chemother 54:45-51. http://dx.doi.org/10.1128/AAC.00427-09.
54. Soroka D, Dubée V, Soulier-Escrihuela O, Cuinet G, Hugonnet JE, Gutmann L, Mainardi JL, Arthur M. 2014. Characterization of broadspectrum Mycobacterium abscessus class A β-lactamase. J Antimicrob Chemother 69:691-696. http://dx.doi.org/10.1093/jac/dkt410.
55. Bercot B, Nordmann P, Drancourt M, Poirel L. 2012. Chromosomeencoded extended-spectrum class A β-lactamase MIN-1 from Minibac- terium massiliensis. Antimicrob Agents Chemother 56:4009-4012. http://dx.doi.org/10.1128/AAC.06401-11.
56. Tanaka M, Okuyama H, Morita N. 2001. Characterization of the gene encoding the β-lactamase of the psychrophilic marine bacterium Moritella marina strain MP-1. Biosci Biotechnol Biochem 65:666-669. http://dx.doi.org/10.1271/bbb.65.666.
57. Mariotte-Boyer S, Nicolas-Chanoine MH, Labia R. 1996. A kinetic study of NMC-A β-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins. FEMS Microbiol Lett 143:29-33. http://dx.doi.org/10.1111/j.1574-6968.1996.tb08457.x.
58. Fèvre C, Passet V, Weill FX, Grimont PAD, Brisse S. 2005. Variants of the Klebsiella pneumoniae OKP chromosomal β-lactamase are divided into two main groups, OKP-A and OKP-B. Antimicrob Agents Chemother 49:5149-5152. http://dx.doi.org/10.1128/AAC.49.12.5149-5152.2005.
59. Walckenaer E, Poirel L, Leflon-Guibout V, Nordmann P, Nicolas- Chanoine MH. 2004. Genetic and biochemical characterization of the chromosomal class A β-lactamases of Raoultella (formerly Klebsiella) planticola and Raoultella ornithinolytica. Antimicrob Agents Chemother 48:305-312. http://dx.doi.org/10.1128/AAC.48.1.305-312.2004.
60. Fournier B, Roy PH, Lagrange PH, Philippon A. 1996. Chromosomal β-lactamase genes of Klebsiella oxytoca are divided into two main groups, blaOXY-1 and blaOXY-2. Antimicrob Agents Chemother 40:454-459.
61. Poirel L, Rodriguez-Martinez JM, Plésiat P, Nordmann P. 2009. Naturally occurring classAβ-lactamases from the Burkholderia cepacia complex. Antimicrob Agents Chemother 53:876-882. http://dx.doi.org/10.1128/AAC.00946-08.
62. Trépanier S, Prince A, Huletsky A. 1997. Characterization of the penA and penR genes of Burkholderia cepacia 249 which encode the chromosomal class A penicillinase and its LysR-type transcriptional regulator. Antimicrob Agents Chemother 41:2399-2405.
63. Papp-Wallace KM, Taracila MA, Gatta JA, Ohuchi N, Bonomo RA, Nukaga M. 2013. Insights into β-lactamases from Burkholderia species, two phylogenetically related yet distinct resistance determinants. J Biol Chem 288:19090-19102. http://dx.doi.org/10.1074/jbc.M113.458315.
64. Tian GB, Adams-Haduch JM, Bogdanovich T, Wang HN, Doi Y. 2011. PME-1, an extended-spectrum β-lactamase identified in Pseudomonas aeruginosa. Antimicrob Agents Chemother 55:2710-2713. http://dx.doi.org/10.1128/AAC.01660-10.
65. Bellais S, Rholl L, Fortineau N, Decousser JW, Nordmann P. 2001. Biochemical-genetic characterization of the chromosomally encoded extended- spectrum class A β-lactamase from Rahnella aquatilis. Antimicrob Agents Chemother 45:2965-2968. http://dx.doi.org/10.1128/AAC.45.10.2965-2968.2001.
66. Choury D, Szajnert MF, Joly-Guillou ML, Azibi K, Delpech M, Paul G. 2000. Nucleotide sequence of the bla(RTG-2)(CARB-5) gene and phylogeny of a new group of carbenicillinases. Antimicrob Agents Chemother 44:1070-1074. http://dx.doi.org/10.1128/AAC.44.4.1070-1074.2000.
67. Poirel L, Corvec S, Rapoport M, Mugnier P, Petroni A, Pasteran F, Faccone D, Galas M, Drugeon H, Cattoir V, Nordmann P. 2007. Identification of the novel narrow-spectrum β-lactamase SCO-1 in Acinetobacter spp. from Argentina. Antimicrob Agents Chemother 51:2179- 2184. http://dx.doi.org/10.1128/AAC.01600-06.
68. Papagiannitsis CC, Loli A, Tzouvelekis LS, Tzelepi E, Arlet G, Miriagou V. 2007. SCO-1, a novel plasmid-mediated class A β-lactamase with carbenicillinase characteristics from Escherichia coli. Antimicrob Agents Chemother 51:2185-2188. http://dx.doi.org/10.1128/AAC.01439-06.
69. Petrella S, Clermont D, Casin I, Jarlier V, Sougakoff W. 2001. Novel class A β-lactamase Sed-1 from Citrobacter sedlakii: genetic diversity of β-lactamases within the Citrobacter genus. Antimicrob Agents Chemother 45:2287-2298. http://dx.doi.org/10.1128/AAC.45.8.2287-2298.2001.
70. Henriques I, Moura A, Alves A, Saavedra MJ, Correia A. 2004. Molecular characterization of a carbapenem-hydrolyzing class A β-lactamase, SFC-1, from Serratia fonticola UTAD54. Antimicrob Agents Chemother 48:2321-2324. http://dx.doi.org/10.1128/AAC.48.6.2321-2324.2004.
71. Matsumoto Y, Inoue M. 1999. Characterization of SFO-1, a plasmidmediated inducible class A β-lactamase from Enterobacter cloacae. Antimicrob Agents Chemother 43:307-313.
72. Lamoureaux TL, Vakulenko V, Toth M, Frase H, Vakulenko SB. 2013. A novel extended-spectrum β-lactamase, SGM-1, from an environmental isolate of Sphingobium sp. Antimicrob Agents Chemother 57:3783- 3788. http://dx.doi.org/10.1128/AAC.00808-13.
73. Lartigue MF, Nordmann P, Edelstein MV, Cuzon G, Brisse S, Poirel L. 2013. Characterization of an extended-spectrum class A β-lactamase from a novel enterobacterial species taxonomically related to Rahnella spp/Ewingella spp. J Antimicrob Chemother 68:1733-1736. http://dx.doi.org/10.1093/jac/dkt122.
74. Queenan AM, Torres-Viera C, Gold HS, Carmeli Y, Eliopoulos GM, Moellering RC, Jr, Quinn JP, Hindler J, Medeiros AA, Bush K. 2000. SME-type carbapenem-hydrolyzing class A β-lactamases from geographically diverse Serratia marcescens strains. Antimicrob Agents Chemother 44:3035-3039. http://dx.doi.org/10.1128/AAC.44.11.3035-3039.2000.
75. Handal T, Giraud-Morin C, Caugant DA, Madinier I, Olsen I, Fosse T. 2005. Chromosome- and plasmid-encoded β-lactamases in Capnocytophaga spp. Antimicrob Agents Chemother 49:3940-3943. http://dx.doi.org/10.1128/AAC.49.9.3940-3943.2005.
76. Ehrmann E, Handal T, Tamanai-Shacoori Z, Bonnaure-Mallet M, Fosse T. 2014. High prevalence of β-lactam and macrolide resistance genes in human oral Capnocytophaga species. J Antimicrob Chemother 69:381-384. http://dx.doi.org/10.1093/jac/dkt350.
77. Ogawara H, Horikawa S, Shimada-Miyoshi S, Yasuzawa K. 1978. Production and property of β-lactamases in Streptomyces: comparison of the strains isolated newly and thirty years ago. Antimicrob Agents Chemother 13:865-870. http://dx.doi.org/10.1128/AAC.13.5.865.
78. Sendouda A, Urabe H, Ogawara H. 1993. Cloning, nucleotide sequence and expression of a β-lactamase gene from Streptomyces lavendulae. FEMS Microbiol Lett 112:343-348. http://dx.doi.org/10.1111/j.1574 -6968.1993.tb06473.x.
79. Walckenaer E, Delmas J, Leflon-Guibout V, Bonnet R, Nicolas- Chanoine MH. 16 June 2015. Genetic, biochemical characterization and mutagenesis of the chromosomal class A β-lactamase of Raoultella (formerly Klebsiella) terrigena. Pathol Biol (Paris) http://dx.doi.org/10.1016/j.patbio.2015.05.002.
80. Silva J, Aguilar C, Ayala G, Estrada MA, Garza-Ramos U, Lara-Lemus R, Ledezma L. 2000. TLA-1: a new plasmid mediated extendedspectrum β-lactamase from Escherichia coli. Antimicrob Agents Chemother 44:997-1003. http://dx.doi.org/10.1128/AAC.44.4.997-1003.2000.
81. Girlich D, Poirel L, Schluter A, Nordmann P. 2005. TLA-2, a novel Ambler class A expanded-spectrum β-lactamase. Antimicrob Agents Chemother 49:4767-4770. http://dx.doi.org/10.1128/AAC.49.11.4767 -4770.2005.
82. Ishii Y, Ohno A, Taguchi H, Imajo S, Ishiguro M, Matsuzaw H. 1995. Cloning and sequence of the gene encoding a cefotaxime-hydrolyzing class A β-lactamase isolated from Escherichia coli. Antimicrob Agents Chemother 39:2269-2275. http://dx.doi.org/10.1128/AAC.39.10.2269.
83. Jun LJ, Kim JH, Jin JW, Jeong HD. 2012. Characterization of a new β-lactamase gene from isolates of Vibrio spp. in Korea. J Microbiol Biotechnol 22:555-562. http://dx.doi.org/10.4014/jmb.1110.10014.
84. Poirel L, Naas T, Guibert M, Chaibi EB, Labia R, Nordmann P. 1999. 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.
85. Teo JW, Suwanto A, Poh CL. 2000. Novel β-lactamase genes from two environmental isolates of Vibrio harveyi. Antimicrob Agents Chemother 44:1309-1314. http://dx.doi.org/10.1128/AAC.44.5.1309-1314.2000.
86. Weng SF, Chen CY, Lee YS, Lin JW, Tseng YH. 1999. Identification of a novel β-lactamase produced by Xanthomonas campestris, a phytopathogenic bacterium. Antimicrob Agents Chemother 43:1792-1797.
87. Sharma S, Mittal S, Mallik S, Virdi JS. 2006. Molecular characterization of β-lactamase genes blaA and blaB of Yersinia enterocolitica biovar 1A. FEMS Microbiol Lett 257:319-327. http://dx.doi.org/10.1111/j.1574 -6968.2006.00191.x.
88. Dortet L, Poirel L, Abbas S, Oueslati S, Nordmann P. 21 September 2015. Genetic and biochemical characterization of FRI-1, a carbapenemhydrolyzing class A β-lactamase from Enterobacter cloacae. Antimicrob Agents Chemother. http://dx.doi.org/10.1128/AAC.01636-15.
89. Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. 1997. The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25:4876-4882. http://dx.doi.org/10.1093/nar/25.24.4876.
90. Saitou N, Nei M. 1987. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4:406-425.
91. Maddison DR, Swofford DJ, Maddison WP. 1997. NEXUS: an extensible file format for systematic information. Syst Biol 46:590-621. http://dx.doi.org/10.1093/sysbio/46.4.590.
92. Walther-Rasmussen J, Høiby N. 2007. Class A carbapenemases. J Antimicrob Chemother 60:470-482. http://dx.doi.org/10.1093/jac/dkm226.
93. Galán JC. 2002. Trans-gram gene transfer: the case of β-lactamases. Rev Esp Quimioter 15:215-223. (In Spanish.)
94. Brown JR, Douady CJ, Italia MJ, Marshall WE, Stanhope MJ. 2001. Universal trees based on large combined protein sequence data sets. Nat Genet 28:281-285. http://dx.doi.org/10.1038/90129.
95. Naas T, Poirel L, Nordmann P. 2008. Minor extended-spectrum β-lactamases. Clin Microbiol Infect 14(Suppl 1):42-52. http://dx.doi.org/10.1111/j.1469-0691.2007.01861.x.
96. Ambler RP, Coulson AF, Frère JM, Ghuysen JM, Joris B, Forsman M, Levesque RC, Tiraby G, Waley SG. 1991. A standard numbering scheme for the class A β-lactamases. Biochem J 276:269-270. http://dx.doi.org/10.1042/bj2760269.
97. Risso VA, Gavira JA, Mejia-Carmona DF, Gaucher EA, Sanchez-Ruiz JM. 2013. Hyperstability and substrate promiscuity in laboratory resurrections of Precambrian β-lactamases. J Am Chem Soc 135:2899-2902. http://dx.doi.org/10.1021/ja311630a.
98. Tranier S, Bouthors AT, Maveyraud L, Guillet V, Sougakoff W, Samama JP. 2000. The high resolution crystal structure for class A β-lactamase PER-1 reveals the bases for its increase in breadth of activity. J Biol Chem 275:28075-28082.
99. Ruggiero M, Kerff F, Herman R, Sapunaric F, Galleni M, Gutkind G, Charlier P, Sauvage E, Power P. 2014. Crystal structure of the extendedspectrum β-lactamase PER-2 and insights into the role of specific residues in the interaction with β-lactams and β-lactamase inhibitors. Antimicrob Agents Chemother 58:5994-6002. http://dx.doi.org/10.1128/AAC.00089-14.
100. Brown-Elliott BA, Brown JM, Conville PS, Wallace RJ, Jr. 2006. Clinical and laboratory features of the Nocardia spp. based on current molecular taxonomy. Clin Microbiol Rev 19:259-282. http://dx.doi.org/10.1128/CMR.19.2.259-282.2006.
101. Chen Y, Tenover FC, Koehler TM. 2004. β-lactamase gene expression in a penicillin-resistant Bacillus anthracis strain. Antimicrob Agents Chemother 48:4873-4877. http://dx.doi.org/10.1128/AAC.48.12.4873-4877.2004.
102. David MZ, Daum RS. 2010. Community-associated methicillinresistant Staphylococcus aureus: epidemiology and clinical consequences of an emerging epidemic. Clin Microbiol Rev 23:616-687. http://dx.doi.org/10.1128/CMR.00081-09.
103. Kapadia M, Rolston KV, Han XY. 2007. Invasive Streptomyces infections: six cases and literature review. Am J Clin Pathol 127:619-624. http://dx.doi.org/10.1309/QJEBXP0BCGR54L15.
104. Kurai S, Urabe H, Ogawara H. 1995. Cloning, sequencing, and sitedirected mutagenesis of β-lactamase gene from Streptomyces fradiae Y59. Antimicrob Agents Chemother 39:260-263. http://dx.doi.org/10.1128/AAC.39.1.260.
105. Loncaric I, Hübber-Heiss A, Posautz A, Stalder GL, Hoffmann D, Rosengarten R, Walzer C. 2013. Characterization of methicillinresistant Staphylococcus spp. carrying the mecC gene, isolated from wildlife. J Antimicrob Chemother 68:2222-2225. http://dx.doi.org/10.1093/jac/dkt186.
106. Materon IC, Queenan AM, Koehler TM, Bush K, Palzkill T. 2003. Biochemical characterization of β-lactamases Bla1 and Bla2 from Bacillus anthracis. Antimicrob Agents Chemother 47:2040-2042. http://dx.doi.org/10.1128/AAC.47.6.2040-2042.2003.
107. Pérez-Llarena F, Martin JF, Galleni M, Coque JJ, Fuente JL, Frère JM, Liras P. 1997. The bla gene of the cephamycin cluster of Streptomyces clavuligerus encodes a class A β-lactamase of low enzymatic activity. J Bacteriol 179:6035-6040.
108. Seipke RF, Kaltenpoth M, Hutchings MI. 2012. Streptomyces as symbionts: an emerging and widespread theme? FEMS Microbiol Rev 36:862-876. http://dx.doi.org/10.1111/j.1574-6976.2011.00313.x.
109. Chambers HF, Moreau D, Yajko D, Miick C, Wagner C, Hackbarth C, Kocagoz S, Rosenberg E, Hadley WK, Nikaido H. 1995. Can penicillins and other β-lactam antibiotics be used to treat tuberculosis? Antimicrob Agents Chemother 39:2620-2624. http://dx.doi.org/10.1128/AAC.39.12.2620.
110. Kurz SG, Bonomo RA. 2012. Reappraising the use of β-lactams to treat tuberculosis. Expert Rev Anti Infect Ther 10:999-1006. http://dx.doi.org/10.1586/eri.12.96.
111. Quinting B, Reyrat JM, Monnaie D, Amicosante G, Pelicic V, Gicquel B, Frère JM, Galleni M. 1997. Contribution of β-lactamase production to the resistance of mycobacteria to β-lactam antibiotics. FEBS Lett 406: 275-278. http://dx.doi.org/10.1016/S0014-5793(97)00286-X.
112. Utrup LJ, Moore TD, Actor P, Poupard JA. 1995. Susceptibilities of nontuberculosis mycobacterial species to amoxicillin-clavulanic acid alone and in combination with antimycobacterial agents. Antimicrob Agents Chemother 39:1454-1457. http://dx.doi.org/10.1128/AAC.39.7.1454.
113. Sauvage E, Fonzé E, Quinting B, Galleni M, Frère JM, Charlier P. 2006. Crystal structure of the Mycobacterium fortuitum class A β-lactamase: structural basis for broad substrate specificity. Antimicrob Agents Chemother 50:2516-2521. http://dx.doi.org/10.1128/AAC.01226-05.
114. Gniadkowski M. 2008. Evolution of extended-spectrum β-lactamases by mutation. Clin Microbiol Infect 14(Suppl 1):11-32. http://dx.doi.org/10.1111/j.1469-0691.2007.01854.x.
115. Page MG. 2008. Extended-spectrum β-lactamases: structure and kinetic mechanism. Clin Microbiol Infect 14(Suppl 1):63-74. http://dx.doi.org/10.1111/j.1469-0691.2007.01863.x.
116. Philippon A, Arlet G. 2012. Entérobactéries et bêta-lactamines: phénotypes de résistance naturelle. Pathol Biol (Paris) 60:112-126. http://dx.doi.org/10.1016/j.patbio.2011.12.002.
117. Mulvey MR, Boyd DA, Olson AB, Doublet B, Cloeckaert A. 2006. The genetics of Salmonella genomic island 1. Microbes Infect 8:1915-1922. http://dx.doi.org/10.1016/j.micinf.2005.12.028.
118. Vanhove M, Guillaume G, Ledent P, Richards JH, Pain RH, Frère JM. 1997. Kinetic and thermodynamic consequences of the removal of the Cys-77-Cys-123 disulphide bond for the folding of TEM-1 β-lactamase. Biochem J 321:413-417. http://dx.doi.org/10.1042/bj3210413.
119. Lim D, Sanschagrin F, Passmore L, De Castro L, Levesque RC, Strynadka NC. 2001. Insights into the molecular basis for the carbenicillinase activity of PSE-4 β-lactamase from crystallographic and kinetic studies. Biochemistry 40:395-402. http://dx.doi.org/10.1021/bi001653v.
120. Lenfant F, Petit A, Labia R, Maveyraud L, Samama JP, Masson JM. 1993. Site-directed mutagenesis of β-lactamase TEM-1. Investigating the potential role of specific residues on the activity of Pseudomonas-specific enzymes. Eur J Biochem 217:939-946.
121. Degnan PH, Yu Y, Sisneros N, Wing RA, Moran NA. 2009. Hamiltonella defensa, genome evolution of protective bacterial endosymbiont from pathogenic ancestors. Proc Natl Acad Sci U S A 106:9063-9068. http://dx.doi.org/10.1073/pnas.0900194106.
122. Rao Q, Wang S, Su YL, Bing XL, Liu SS, Wang XW. 2012. Draft genome sequence of "Candidatus Hamiltonella defensa," an endosymbiont of the whitefly Bemisia tabaci. J Bacteriol 194:3558. http://dx.doi.org/10.1128/JB.00069-12.
123. Potron A, Poirel L, Croizé J, Chanteperdrix V, Nordmann P. 2009. Genetic and biochemical characterization of the first extended-spectrum CARB-type β-lactamase, RTG-4, from Acinetobacter baumannii. Antimicrob Agents Chemother 53:3010 -3016. http://dx.doi.org/10.1128/AAC.01164-08.
124. Bonnet R. 2004. Growing group of extended-spectrum β-lactamases: the CTX-M enzymes. Antimicrob Agents Chemother 48:1-14. http://dx.doi.org/10.1128/AAC.48.1.1-14.2004.
125. Zhao WH, Hu ZQ. 2013. Epidemiology and genetics of CTX-M extended- spectrum β-lactamases in Gram-negative bacteria. Crit Rev Microbiol 39:79-101. http://dx.doi.org/10.3109/1040841X.2012.691460.
126. Fernández A, Pereira MJ, Suárez JM, Poza M, Treviño M, Villalón P, Sáez-Nieto JA, Regueiro BJ, Villanueva R, Bou G. 2011. Emergence in Spain of a multidrug-resistant Enterobacter cloacae clinical isolate producing SFO-1 extended-spectrum β-lactamase. J Clin Microbiol 49:822-828. http://dx.doi.org/10.1128/JCM.01872-10.
127. González-López JJ, Coelho A, Larrosa MN, Lavilla S, Bartolomé R, Prats G. 2009. First detection of plasmid-encoded blaOXY β-lactamase. Antimicrob Agents Chemother 53:3143-3146. http://dx.doi.org/10.1128/AAC.01473-08.
128. Fournier B, Arlet G, Lagrange PH, Philippon A. 1994. Klebsiella oxytoca: resistance to aztreonam by overproduction of the chromosomally encoded β-lactamase. FEMS Microbiol Lett 116:31-36. http://dx.doi.org/10.1111/j.1574-6968.1994.tb06671.x.
129. Fournier B, Lagrange PH, Philippon A. 1996. In-vitro susceptibility of Klebsiella oxytoca strains to 13 β-lactams in the presence and absence of β-lactamase inhibitors. J Antimicrob Chemother 37:931-942. http://dx.doi.org/10.1093/jac/37.5.931.
130. Péduzzi J, Reynaud A, Baron P, Barthélémy M, Labia R. 1994. Chromosomally encoded cephalosporin-hydrolyzing β-lactamase of Proteus vulgaris RO104 belongs to Ambler's class A. Biochim Biophys Acta 1207: 31-39. http://dx.doi.org/10.1016/0167-4838(94)90048-5.
131. Ruimy R, Meziane-Cherif D, Momcilovic S, Arlet G, Andremont A, Courvalin P. 2010. RAHN-2, a chromosomal extended-spectrum class A β-lactamase from Rahnella aquatilis. J Antimicrob Chemother 65:1619- 1623. http://dx.doi.org/10.1093/jac/dkq178.
132. Delmas J, Chen Y, Prati F, Robin F, Shoichet BK, Bonnet R. 2008. Structure and dynamics ofCTX-Menzymes reveal insights into substrate accommodation by extended-spectrum β-lactamases. J Mol Biol 375: 192-201. http://dx.doi.org/10.1016/j.jmb.2007.10.026.
133. Delmas J, Robin F, Carvalho F, Mongaret C, Bonnet R. 2006. Prediction of the evolution of ceftazidime resistance in extended-spectrum β-lactamase CTX-M-9. Antimicrob Agents Chemother 50:731-738. http://dx.doi.org/10.1128/AAC.50.2.731-738.2006.
134. Shimizu-Ibuka A, Oishi M, Yamada S, Ishii Y, Mura K, Sakai H, Matsuzawa H. 2011. Roles of residues Cys69, Asn104, Phe160, Gly232, Ser237, and Asp240 in extended-spectrum β-lactamase Toho-1. Antimicrob Agents Chemother 55:284 -290. http://dx.doi.org/10.1128/AAC.00098-10.
135. Decré D, Burghoffer B, Gautier V, Petit JC, Arlet G. 2004. Outbreak of multi-resistant Klebsiella oxytoca involving strains with extendedspectrum β-lactamases and strains with extended-spectrum activity of the chromosomal β-lactamase. J Antimicrob Chemother 54:881-888. http://dx.doi.org/10.1093/jac/dkh440.
136. Cantón R, Morosini MI, de la Maza OM, de la Pedrosa EG. 2008. IRT and CMT β-lactamases and inhibitor resistance. Clin Microbiol Infect 14(Suppl 1):53-62. http://dx.doi.org/10.1111/j.1469-0691.2007.01849.x.
137. Celenza G, Luzi C, Aschi M, Segatore B, Setacci D, Pellegrini C, Forcella C, Amicosante G, Perilli M. 2008. Natural D240G Toho-1 mutant conferring resistance to ceftazidime: biochemical characterization of CTX-M-43. J Antimicrob Chemother 62:991-997. http://dx.doi.org/10.1093/jac/dkn339.
138. Mammeri H, Poirel L, Nordmann P. 2003. In vivo selection of a chromosomally encoded β-lactamase variant conferring ceftazidime resistance in Klebsiella oxytoca. Antimicrob Agents Chemother 47:3739- 3742. http://dx.doi.org/10.1128/AAC.47.12.3739-3742.2003.
139. Younes A, Hamouda A, Amyes SG. 2011. First report of a novel extended- spectrum β-lactamase KOXY-2 producing Klebsiella oxytoca that hydrolyses cefotaxime and ceftazidime. J Chemother 23:127-130. http://dx.doi.org/10.1179/joc.2011.23.3.127.
140. Ripoll A, Baquero F, Novais A, Rodríguez-Domínguez MJ, Turrientes MC, Cantón R, Galán JC. 2011. In vitro selection of variants resistant to β-lactams plus β-lactamase inhibitors in CTX-M β-lactamases: predicting the in vivo scenario? Antimicrob Agents Chemother 55:4530-4536. http://dx.doi.org/10.1128/AAC.00178-11.
141. Sirot D, Labia R, Pouedras P, Chanal-Claris C, Cerceau C, Sirot J. 1998. Inhibitor-resistant OXY-2-derived β-lactamase produced by Klebsiella oxytoca. Antimicrob Agents Chemother 42:2184-2187.
142. Hornstein MJ, Jupeau AM, Scavizzi MR, Philippon AM, Grimont PAD. 1985. In vitro susceptibilities of 126 clinical isolates of Yersinia enterocolitica to 21 β-lactam antibiotics. Antimicrob Agents Chemother 27:806-811.
143. Pham JN, Bell SM, Martin L, Carniel E. 2000. The β-lactamases and β-lactam antibiotic susceptibility of Yersinia enterocolitica. J Antimicrob Chemother 46:951-957. http://dx.doi.org/10.1093/jac/46.6.951.
144. Stock I, Wiedemann B. 1999. An in-vitro study of the antimicrobial susceptibilities of Yersinia enterocolitica and the definition of a database. J Antimicrob Chemother 43:37- 45. http://dx.doi.org/10.1093/jac/43.1.37.
145. Poirel L, Pitout JD, Nordmann P. 2007. Carbapenemases: molecular diversity and clinical consequences. Future Microbiol 2:501-512. http://dx.doi.org/10.2217/17460913.2.5.501.
146. Queenan AM, Bush K. 2007. Carbapenemases: the versatile β-lactamases. Clin Microbiol Rev 20:440-458. http://dx.doi.org/10.1128/CMR.00001-07.
147. Papp-Wallace KM, Endimiani A, Taracila MA, Bonomo RA. 2011. Carbapenems: past, present, and future. Antimicrob Agents Chemother 55:4943-4960. http://dx.doi.org/10.1128/AAC.00296-11.
148. Papp-Wallace KM, Bethel CR, Distler AM, Kasuboski C, Taracila M, Bonomo RA. 2010. Inhibitor resistance in the KPC-2 β-lactamase, a preeminent property of this class A β-lactamase. Antimicrob Agents Chemother 54:890-897. http://dx.doi.org/10.1128/AAC.00693-09.
149. Ke W, Bethel CR, Papp-Wallace KM, Pagadala SR, Nottingham M, Fernandez D, Buynak JD, Bonomo RA, van den Akker F. 2012. Crystal structures of KPC-2 β-lactamase in complex with 3-nitrophenyl boronic acid and the penam sulfone PSR-3-226. Antimicrob Agents Chemother 56:2713-2718. http://dx.doi.org/10.1128/AAC.06099-11.
150. Sougakoff W, L'Hermite G, Pernot L, Naas T, Guillet V, Nordmann P, Jarlier V, Delettré J. 2002. Structure of the imipenem-hydrolyzing class A β-lactamase SME-1 from Serratia marcescens. Acta Crystallogr D Biol Crystallogr 58:267-274. http://dx.doi.org/10.1107/S0907444901019606.
151. Fonseca F, Chudyk EI, van der Kamp MW, Correia A, Mulholland AJ, Spencer J. 2012. The basis for carbapenem hydrolysis by class A β-lactamases: a combined investigation using crystallography and simulations. J Am Chem Soc 134:18275-18285. http://dx.doi.org/10.1021/ja304460j.
152. Papp-Wallace KM, Taracila MA, Smith KM, Xu Y, Bonomo RA. 2012. Understanding the molecular determinants of substrate and inhibitor specificities in the carbapenemase KPC-2: exploring the roles of Arg220 and Glu276. Antimicrob Agents Chemother 56:4428-4438. http://dx.doi.org/10.1128/AAC.05769-11.
153. Poirel L, Brinas L, Fortineau N, Nordmann P. 2005. Integron-encoded GES-type extended-spectrum β-lactamase with increased activity toward aztreonam in Pseudomonas aeruginosa. Antimicrob Agents Chemother 49:3593-3597. http://dx.doi.org/10.1128/AAC.49.8.3593-3597.2005.
154. Delbrück H, Bogaerts P, Kupper MB, Rezende de Castro R, Bennink S, Glupczynski Y, Galleni M, Hoffmann KM, Bebrone C. 2012. Kinetic and crystallographic studies of extended-spectrum GES-11, GES-12, and GES-14 β-lactamases. Antimicrob Agents Chemother 56:5618-5625. http://dx.doi.org/10.1128/AAC.01272-12.
155. Bontron S, Poirel L, Nordmann P. 2015. In vitro prediction of the evolution of GES-1 β-lactamase hydrolytic activity. Antimicrob Agents Chemother 59:1664-1670. http://dx.doi.org/10.1128/AAC.04450-14.
156. Regan KH, Bhatt J. 2014. Eradication therapy for Burkholderia cepacia complex in people with cystic fibrosis. Cochrane Database Syst Rev 10: CD009876. http://dx.doi.org/10.1002/14651858.CD009876.pub2.
157. Dando SJ, Mackay-Sim A, Norton R, Currie BJ, St John JA, Ekberg JA, Batzloff M, Ulett GC, Beacham IR. 2014. Pathogens penetrating the central nervous system: infection pathways and the cellular and molecular mechanisms of invasion. Clin Microbiol Rev 27:691-726. http://dx.doi.org/10.1128/CMR.00118-13.
158. Khan I, Wieler LH, Melzer F, Elschner MC, Muhammad G, Ali S, Sprague LD, Neubauer H, Saqib M. 2013. Glanders in animals: a review on epidemiology, clinical presentation, diagnosis and countermeasures. Transbound Emerg Dis 60:204-221. http://dx.doi.org/10.1111/j.1865 -1682.2012.01342.x.
159. Dance D. 2014. Treatment and prophylaxis of melioidosis. Int J Antimicrob Agents 43:310 -318. http://dx.doi.org/10.1016/j.ijantimicag.2014.01.005.
160. Philippon A. 2009. Antibiotic resistance in other non-fermentative strict aerobic Gram-negative bacilli, p 175-211. In Courvalin P, Leclercq R, Rice LB (ed), Antibiogram. ASM Press, Washington, DC.
161. Ho PL, Cheung TK, Yam WC, Yuen KY. 2002. Characterization of a laboratory-generated variant of BPS β-lactamase from Burkholderia pseudomallei that hydrolyses ceftazidime. J Antimicrob Chemother 50: 723-726. http://dx.doi.org/10.1093/jac/dkf208.
162. Tribuddharat C, Moore RA, Baker P, Woods DE. 2003. Burkholderia pseudomallei class A β-lactamase mutations that confer selective resistance against ceftazidime or clavulanic acid inhibition. Antimicrob Agents Chemother 47:2082-2087. http://dx.doi.org/10.1128/AAC.47.7.2082-2087.2003.
163. Rholl DA, Papp-Wallace KM, Tomaras AP, Vasil ML, Bonomo RA, Schweizer HP. 2011. Molecular investigations of PenA-mediated β-lactam resistance in Burkholderia pseudomallei. Front Microbiol 2:139. http://dx.doi.org/10.3389/fmicb.2011.00139.
164. Schweizer HP. 2012. Mechanisms of antibiotic resistance in Burkholderia pseudomallei: implications for treatment of melioidosis. Future Microbiol 7:1389-1399. http://dx.doi.org/10.2217/fmb.12.116.
165. Hwang J, Cho KH, Song H, Yi H, Kim HS. 2014. Deletion mutations conferring substrate spectrum extension in the class A β-lactamase. An- timicrob Agents Chemother 58:6265-6269. http://dx.doi.org/10.1128/AAC.02648-14.
166. Chantratita N, Rholl DA, Sim B, Wuthiekanun V, Limmathurotsakul D, Amornchai P, Thanwisai A, Chua HH, Ooi WF, Holden MT, Day NP, Tan P, Schweizer HP, Peacock SJ. 2011. Antimicrobial resistance to ceftazidime involving loss of penicillin-binding protein 3 in Burkholderia pseudomallei. Proc Natl Acad Sci U S A 108:17165-17170. http://dx.doi.org/10.1073/pnas.1111020108.
167. Török ME, Chantratita N, Peacock SJ. 2012. Bacterial gene loss as a mechanism for gain of antimicrobial resistance. Curr Opin Microbiol 15:583-587. http://dx.doi.org/10.1016/j.mib.2012.07.008.
168. Aunkham A, Schulte A, Winterhalter M, Suginta W. 2014. Porin involvement in cephalosporin and carbapenem resistance of Burkholderia pseudomallei. PLoS One 9:e95918. http://dx.doi.org/10.1371/journal.pone.0095918.
169. Brooke JS. 2012. Stenotrophomonas maltophilia: an emerging global opportunistic pathogen. Clin Microbiol Rev 25:2-41. http://dx.doi.org/10.1128/CMR.00019-11.
170. Parker AC, Smith CJ. 1993. Genetic and biochemical analysis of a novel Ambler class A β-lactamase responsible for cefoxitin resistance in Bacteroides species. Antimicrob Agents Chemother 37:1028-1036. http://dx.doi.org/10.1128/AAC.37.5.1028.
171. García N, Gutierrez G, Lorenzo M, Garcia JE, Piriz S, Quesada A. 2008. Genetic determinants for cfxA expression in Bacteroides strains isolated from human infections. J Antimicrob Chemother 62:942-947. http://dx.doi.org/10.1093/jac/dkn347.
172. Madinier I, Fosse T, Giudicelli J, Labia R. 2001. Cloning and biochemical characterization of a class A β-lactamase from Prevotella intermedia. Antimicrob Agents Chemother 45:2386-2389. http://dx.doi.org/10.1128/AAC.45.8.2386-2389.2001.
173. 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.
174. Bellais S, Poirel L, Leotard S, Naas T, Nordmann P. 2000. Genetic diversity of carbapenem-hydrolyzing metallo-β-lactamases from Chryseobacterium (Flavobacterium) indologenes. Antimicrob Agents Chemother 44:3028-3034. http://dx.doi.org/10.1128/AAC.44.11.3028 -3034.2000.
175. Paterson DL, Bonomo RA. 2005. Extended-spectrum β-lactamases: a clinical update. Clin Microbiol Rev 18:657-686. http://dx.doi.org/10.1128/CMR.18.4.657-686.2005.
176. Hidalgo L, Hopkins KL, Wareham DW, Gutierrez B, Gonzàlez-Zorn B. 2012. Association of extended-spectrum β-lactamase VEB-5 and 16S rRNA methyltransferase armA in Salmonella enterica from the United Kingdom. Antimicrob Agents Chemother 56:4985-4987. http://dx.doi.org/10.1128/AAC.00381-12.
177. Zong Z, Partridge SR, Iredell JR. 2009. A blaVEB-1 variant, blaVEB-6, associated with repeated elements in a complex genetic structure. Antimicrob Agents Chemother 53:1693-1697. http://dx.doi.org/10.1128/AAC.01313-08.
178. Pollitt S, Zalkin H. 1983. Role of primary structure and disulfide bond formation in β-lactamase secretion. J Bacteriol 153:27-32.
179. Schultz SC, Dabadie-McFarkand G, Neitzel JJ, Richards JH. 1987. Stability of wild-type and mutant RTEM-1 β-lactamase: effect of the disulfide bond. Proteins 2:290 -297. http://dx.doi.org/10.1002/prot.340020405.
180. Bellais S, Poirel L, Naas T, Girlich D, Nordmann P. 2000. Geneticbiochemical analysis and distribution of the Ambler class A β-lactamase CME-2, responsible for extended-spectrum cephalosporin resistance in Chryseobacterium (Flavobacterium) meningosepticum. Antimicrob Agents Chemother 44:1-9. http://dx.doi.org/10.1128/AAC.44.1.1-9.2000.
181. Nordmann P, Mariotte S, Naas T, Labia R, Nicolas MH. 1993. Biochemical properties of a carbapenem-hydrolyzing β-lactamase from Enterobacter cloacae and cloning of the gene into Escherichia coli. Antimicrob Agents Chemother 37:939-946. http://dx.doi.org/10.1128/AAC.37.5.939.
182. Kuzin AP, Nukaga M, Nukaga Y, Hujer AM, Bonomo RA, Knox JR. 1999. Structure of the SHV-1 β-lactamase. Biochemistry 38:5720-5727. http://dx.doi.org/10.1021/bi990136d.
183. Nukaga M, Mayama K, Hujer AM, Bonomo RA, Knox JR. 2003. Ultrahigh resolution structure of a class A β-lactamase: on the mechanism and specificity of the extended-spectrum SHV-2 enzyme. J Mol Biol 328:289-301. http://dx.doi.org/10.1016/S0022-2836(03)00210-9.
184. Bouthors AT, Dagoneau-Blanchard N, Naas T, Nordmann P, Jarlier V, Sougakoff W. 1998. Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 β-lactamase hydrolysing third-generation cephalosporins. Biochem J 330:1443-1449. http://dx.doi.org/10.1042/bj3301443.
185. Chen CC, Herzberg O. 1992. Inhibition of β-lactamase by clavulanate. Trapped intermediates in cryocrystallographic studies. J Mol Biol 224: 1103-1113.
186. Jelsch C, Mourey L, Masson JM, Samama JP. 1993. Crystal structure of Escherichia coli TEM-1 β-lactamase at 1.8 A resolution. Proteins 16:364-383. http://dx.doi.org/10.1002/prot.340160406.
187. Liang YH, Gao R, Su XD. 2012. Structural insights into the broadened substrate profile of the extended-spectrum β-lactamase OXY-1-1 from Klebsiella oxytoca. Acta Crystallogr D Biol Crystallogr 68:1460-1467. http://dx.doi.org/10.1107/S090744491203466X.
188. Qing Y, Cao KY, Fang ZL, Huang YM, Zhang XF, Tian GB, Huang X. 2014. Outbreak of PER-1 and diversity of β-lactamases among ceftazidime- resistant Pseudomonas aeruginosa clinical isolates. J Med Microbiol 63:386-392. http://dx.doi.org/10.1099/jmm.0.069427-0.
189. Opazo A, Vali L, Al Obaid K, Dashti AA, Amyes SG. 2014. Novel genetic structure harbouring blaPER-1 in ceftazidime-resistant Acinetobacter baumannii isolated from Kuwait. Int J Antimicrob Agents 43:383-384. http://dx.doi.org/10.1016/j.ijantimicag.2014.01.001.
190. Mnif B, Ktari S, Chaari A, Medhioub F, Rhimi F, Bouaziz M, Hammami A. 2013. Nosocomial dissemination of Providencia stuartii isolates carrying blaOXA-48, blaPER-1, blaCMY-4 and qnrA6 in a Tunisian hospital. J Antimicrob Chemother 68:329-332. http://dx.doi.org/10.1093/jac/dks386.
191. Fabre M, Hauck Y, Soler C, Koeck JL, van Ingen J, van Soolingen D, Vergnaud G, Pourcel C. 2010. Molecular characteristics of "Mycobacterium canettii" the smooth Mycobacterium tuberculosis bacilli. Infect Genet Evol 10:1165-1173. http://dx.doi.org/10.1016/j.meegid.2010.07.016.
192. Papp-Wallace KM, Taracila M, Hornick JM, Hujer AM, Hujer KM, Distler AM, Endimiani A, Bonomo RA. 2010. Substrate selectivity and a novel role in inhibitor discrimination by residue 237 in the KPC-2 β-lactamase. Antimicrob Agents Chemother 54:2867-2877. http://dx.doi.org/10.1128/AAC.00197-10.
193. Bouthors AT, Delettré J, Mugnier P, Jarlier V, Sougakoff W. 1999. Site-directed mutagenesis of residues 164, 170, 171, 179, 220, 237 and 242 in PER-1 β-lactamase hydrolysing expanded-spectrum cephalosporins. Protein Eng 12:313-318. http://dx.doi.org/10.1093/protein/12.4.313.
194. Bouthors AT, Jarlier V, Sougakoff W. 1998. Amino acid substitutions at positions 69, 165, 244 and 275 of the PER-1 β-lactamase do not impair enzyme inactivation by clavulanate. J Antimicrob Chemother 42:399-401. http://dx.doi.org/10.1093/jac/42.3.399-a.
195. Goffin C, Ghuysen JM. 1998. Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol Mol Biol Rev 62:1079-1093.
196. Edgar RC. 2004. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32:1792-1797. http://dx.doi.org/10.1093/nar/gkh340.
197. Waterhouse AM, Procter JB, Martin DM, Clamp M, Barton GJ. 2009. Jalview version 2-a multiple sequence alignment editor and analysis workbench. Bioinformatics 25:1189-1191. http://dx.doi.org/10.1093/bioinformatics/btp033.