β-Lactamases of Aerobic Gram-Negative Bacteria: Description, Principles of Classification, Methods of Detection and Typing | CMAC

β-Lactamases of Aerobic Gram-Negative Bacteria: Description, Principles of Classification, Methods of Detection and Typing

Clinical Microbiology and Antimicrobial Chemotherapy. 2001; 3(3):223-242

​ Edelstein M.V.
β-lactamases antimicrobial resistance Gram-negative bacteria microbiological diagnostics
Section
Antimicrobial resistance
Type
Journal article
Publication
Clinical Microbiology and Antimicrobial Chemotherapy. 2001; 3(3):223-242

Abstract

β-Lactamases are represented by extensive range of genetically and functionally different enzymes that are able to destroy β-lactams that leads to development of resistance to these antibiotics in β-lactamases producing bacteria. Intrinsic production of β-lactamases is a common phenomenon for wide range of microorganisms. But at the present time the wide spread of plasmid-mediated β-lactamases that leads to secondary (acquired) resistance to β-lactams becoming more common. The aim of this review is to describe the main structural and functional groups of β-lactamases of aerobic Gram-negative bacteria, with especial attention to plasmid-mediated TEM- and SHV-types β-lactamases, their evolution and role in the development of resistance to different β-lactams. The recent methods of detection and typing of β-lactamases are described.

  • 1. Webb E. C., editor. Enzyme nomenclature. London: Academic Press Inc. (London) Ltd.; 1984. p.366-74.
  • 2. Bush K. The evolution of b-lactamases. Antibiotic Resistance: Origins, Evolution, Selection and Spread. John Willey & Sons; 1997. p.152-69.
  • 3. Livermore D.M. b-lactamases in laboratory and clinical resistance. Clin Microb Reviews 1995; 8:557-84.
  • 4. Bush K., Jacoby G., Medeiros A. Functional classification scheme for b-lactamases and its correlation with molecular structure. Antimicrob Agents Chemother 1995; 39:1211-33.
  • 5. Rasmussen B.A., Bush K. Carbapenem-hydrolyzing b-lactamases. Antimicrob Agents Chemother 1997; 41:223-32.
  • 6. Abraham E.P., Chain E. An enzyme from bacteria able to destroy penicillin. Nature 1940; 373:837.
  • 7. Fleming P.C., Goldner M., Glass D.G. Observations on the nature, distribution, and significance of cephalosporinase. Lancet 1963; I:1399-401.
  • 8. Richmond M.H., Sykes R.B. The b-lactamases of gram-negative bacteria and their possible physiological role. Adv Microb Physiol 1973; 9:31-88.
  • 9. Sykes R.B., Matthew M. The b-lactamases of gram-negative bacteria and their role in resistance to b-lactam antibiotics. J Antimicrob Chemother 1976; 2:115-57.
  • 10. Mitsuhashi S., Inoue M. Mechanisms of resistance to beta-lactam antibiotics. In: Mitsuhashi S., editors. Beta-lactam antibiotics. New York: Springer-Verlag; 1981. р.41-56.
  • 11. Ambler R.P. The structure of b-lactamases. Philos Trans R Soc Lond (Biol.) 1980; 289:321-31.
  • 12. Livermore D.M., Williams J.D. b-lactams: mode of action and mechanisms of bacterial resistance. In: Lorian V., editor. Antibiotics in laboratory medicine. Baltimore: Williams & Wilkins; 1991. p.503-78.
  • 13. Livermore D.M. Mechanisms of resistance to b-lactam antibiotics. Scand J Infect Dis 1991; 78 (Suppl.):7-16.
  • 14. Matagne A., Lamotte-Brasseur J., Frere J.M. Catalytic properties of class A b-lactamases: efficiency and diversity. Biochem J 1998; 1:581-98.
  • 15. Tzouvelekis L.S., Tzelepi E., Tassios P.T., Legakis N.J. CTX-M-type b-lactamases: an emerging group of extended-spectrum enzymes. Int J Antimicrob Agents 2000; 14:137-42.
  • 16. Bonomo R.A., Rice L.B. Inhibitor resistant class A beta-lactamases. Frontiers Bioscience 1999; 4:34-41.
  • 17. Nicolas-Chanoine M.H. Inhibitor-resistant b-lactamases. J Antimicrob Chemother 1997; 40:1-3.
  • 18. Prinarakis E.E., Miriagou V., Tzelepi N., Gazouli M., Tzouvelekis L.S. Emergence of an inhibitor-resistant b-lactamase (SHV-10) derived from an SHV-5 variant. Antimicrob Agents Chemother1997; 41:838-40.
  • 19. Huovinen S., Huovinen P., Jacoby G.A. Detection of plasmid-mediated b-lactamases with DNA probes. Antimicrob Agents Chemother 1988; 32:175-9.
  • 20. Roy C., Segura C., Tirado M., Reig R., Hermida M., Tervel D., et al. Frequency of plasmid determined beta-lactamases in 680 consecutively isolated strains of Enterobacteriaceae. Eur J Clin Microbiol Infect Dis 1986; 4:146-7.
  • 21. Simpson I.N., Harper P.B., O’Callaghan C.H. Principal b-lactamases responsible for resistance to b-lactam antibiotics in urinary tract infections. Antimicrob Agents Chemother 1980; 17:929-36.
  • 22. Du Bois S.K., Marriott M.S., Amyes S.G. TEM- and SHV-derived extended-spectrum b-lactamases: relationship between selection, structure and function. J Antimicrob Chemother 1995; 35:7-22.
  • 23. Wiedemann B., Kliebe C., Kresken M. The epidemiology of b-lactamases. J Antimicrob Chemother 1989; 24 (Suppl. B.):1-22.
  • 24. Chen S.T., Clowes R.S. Variation between the nucleotide sequences of Tn1, Tn2, and Tn3 and expression of b-lactamase in Pseudomonas aeruginosa and Escherichia coli. J Bacteriol 1987; 169:913-6.
  • 25. Goussard S., Courvalin P. Sequences of the genes blaT-1B and blaT-2. Gene 1991; 102:71-3.
  • 26. Thomson C.J., Amyes S.G. Molecular epidemiology of the plasmid-encoded TEM-1 b-lactamase in Scotland. Epidemiol Infect 1993; 110:117-25.
  • 27. Bonnet R., De Champs C., Sirot D., Chanal C., Labia R., Sirot J. Diversity of TEM mutants in Proteus mirabilis. Antimicrob Agents Chemother 1999; 43:2671-7.
  • 28. Palzkill T., Thomson K.S., Sanders C.C., Moland E.S., Huang W., Milligan T.W. New variant of TEM-10 b-lactamase gene produced by a clinical isolate of Proteus mirabilis. Antimicrob Agents Chemother 1995; 39:1199-200.
  • 29. Heritage J., M’Zali F.H., Gascoyne-Binzi D., Hawkey P.M. Evolution and spread of SHV extended-spectrum b-lactamases in gram-negative bacteria. J Antimicrob Chemother 1999; 44:309-18.
  • 30. Huletsky A., Couture F., Levesque R.C. Nucleotide sequence and phylogeny of SHV-2 b-lactamase. Antimicrob Agents Chemother 1990; 34:1725-32.
  • 31. Knox J.R. Extended-spectrum and inhibitor-resistant TEM-type b-lactamases: mutations, specificity, and three-dimensional structure. Antimicrob Agents Chemother 1995; 39:2593-601.
  • 32. Kuzin A.P., Nukaga M., Nukaga Y., Hujer A.M., Bonomo R.A., Knox J.R. Structure of the SHV-1 b-lactamase. Biochemistry 1999; 4:5720-7.
  • 33. Siu L.K., Ho P.L., Yuen K.Y., Wong S.S., Chau P.Y. Transferable hyperproduction of TEM-1 b-lactamase in Shigella flexneri due to a point mutation in the pribnow box. Antimicrob. Agents Chemother 1997; 41:468-70.
  • 34. Wu P.J., Shannon K., Phillips I. Mechanisms of hyperproduction of TEM-1 b-lactamase by clinical isolates of Escherichia coli. J Antimicrob Chemother 1995; 36:927-39.
  • 35. Payne D.J., Marriot M.S., Amyes S.G.B. Characterisation of a unique ceftazidime hydrolysing b-lactamase, TEM-E2. J Med Microbiol 1990; 32:131-4.
  • 36. Heritage J., Hawkey P.M., Todd N., Lewis I.J. Transposition of the gene encoding a TEM-12 extended-spectrum b-lactamase. Antimicrob Agents Chemother 1992; 36:1981-6.
  • 37. Knothe H., Shah P., Kremery V., Antal M., Mitsuhashi S. Transferable resistance to cefotaxime, cefoxitin, cefamandole and cefuroxime in clinical isolates of Klebsiella pneumoniae and Serratia marcescens. Infection 1983; 11:315-7.
  • 38. Kliebe C., Nies B. A., Meyer J.F., Tolxdorff-Neutzling R.M., Wiedemann B. Evolution of plasmid-coded resistance to broad-spectrum cephalosporins. Antimicrob Agents Chemother 1985; 28:302-7.
  • 39. Jacoby G.A., Medeiros A.A. More extended-spectrum b-lactamases. Antimicrob Agents Chemother 1991; 35:1697-704.
  • 40. Yuan M., Aucken H., Hall L.M., Pitt T.L., Livermore D.M. Epidemiological typing of klebsiellae with extended-spectrum b-lactamases from European intensive care units. J Antimicrob Chemother 1998; 41:527-39.
  • 41. Сидоренко С. В. Механизмы антибиотикорезистентности. В кн: Страчунский Л.С., Белоусов Ю.Б., Козлова С.Н., под ред. Антибактериальная терапия. Практическое руководство. Москва: Фармединфо; 2000. с. 1-6.
  • 42. Arlet G., Rouveau M., Casin I., Bouvet P. J., Lagrange P. H., Philippon A. Molecular epidemiology of Klebsiella pneumoniae strains that produce SHV-4 b-lactamase and which were isolated in 14 French hospitals. J Clin Microbiol 1994; 32:2553-8.
  • 43. Hibbert-Rogers L.C., Heritage J., Todd N., Hawkey P.M. Convergent evolution of TEM-26, a b-lactamase with extended-spectrum activity. J Antimicrob Chemother 1994; 33:707-20.
  • 44. Peixe L.V., Sousa J.C., Perez-Diaz J.C., Baquero F. A bla(TEM-1b)-derived TEM-6 b-lactamase: a case of convergent evolution. Antimicrob Agents Chemother 1997; 41:1206.
  • 45. Jacoby G.A., Sutton L. Properties of plasmids responsible for production of extended-spectrum b-lactamases. Antimicrob Agents Chemother 1991; 35:164-9.
  • 46. Jacoby G., Bush K. Amino Acid Sequences for TEM, SHV and OXA Extended-Spectrum and Inhibitor Resistant b-lactamases. [cited 2000 Jul 24] Available from: URL: http://www.lahey.org/studies/webt.htm.
  • 47. Ambler R.P. A standard numbering scheme for the class A b-lactamases. Biochem J 1991; 276:269-72.
  • 48. Brun-Buisson C., Legrand P., Philippon A., Montravers S., Ansquer M., Duval J. Transferable enzymatic resistance to third-generation cephalosporins during nosocomial outbreak of multiresistant Klebsiella pneumoniae. Lancet 1987; II:302-6.
  • 49. Thomson C.J., Shanahan P.M., Amyes S.G. Nucleotide sequences of inhibitor-resistant TEM b-lactamases. J Antimicrob Chemother 1998; 41:572-3.
  • 50. Chaibi E.B., Sirot D., Paul G., Labia R. Inhibitor-resistant TEM b-lactamases: phenotypic, genetic and biochemical characteristic. J Antimicrob Chemother 1999; 43:447-58.
  • 51. Henquell C., Sirot D., Chanal C., De Champs C., Chatron P., Lafeuille B., Texier P., Sirot J., Cluzel R. Frequency of inhibitor-resistant TEM b-lactamases in Escherichia coli isolates from urinary tract infections in France. J Antimicrob Chemother 1994; 34:707-14.
  • 52. Bret L., Chanal C., Sirot D., Labia R., Sirot J. Characterization of an inhibitor-resistant enzyme IRT-2 derived from TEM-2 b-lactamase produced by Proteus mirabilis strains. J Antimicrob Chemother 1996; 38:183-91.
  • 53. Bermudes H., Jude F., Chaibi E.B., Arpin С., Bebear C., Labia R., Quentin C. Molecular characterization of TEM-59 (IRT-17), a novel inhibitor-resistant TEM-derived b-lactamase in a clinical isolate of Klebsiella oxytoca. Antimicrob Agents Chemother 1999; 43:1657-61.
  • 54. Lemozy J., Sirot D., Chanal C., Huc C., Labia R., Dabernat H., Sirot J. First characterization of inhibitor-resistant TEM (IRT) b-lactamases in Klebsiella pneumoniae strains. Antimicrob Agents Chemother 1995; 39:2580-2.
  • 55. Sirot D., Recule C., Chaibi E.B., Bret L., Croize J., Chanal-Claris C., Labia R., Sirot J. A complex mutant of TEM-1 b-lactamase with mutations encountered in both IRT-4 and extended-spectrum TEM-15, produced by an Escherichia coli clinical isolate. Antimicrob Agents Chemother 1997; 41:1322-5.
  • 56. Fiett J., Palucha A., Miaczynska B., Stankiewicz M., Przondo-Mordarska H., Hryniewicz W., Gniadkowski M. A novel complex mutant beta-lactamase, TEM-68, identified in a Klebsiella pneumoniae isolate from an outbreak of extended-spectrum beta-lactamase-producing Klebsiellae. Antimicrob Agents Chemother 2000; 44:1499-505.
  • 57. Winokur P.L., Eidelstein M.V., Stetsiouk O., Stratchounski L., Blahova J., Reshedko G.K., Croco M.A.T., Hollis R.J., Pfaller M.A., Jones R.N. Russian Klebsiella pneumoniae isolates that express extended-spectrum b-lactamases. Clin Microbiol Infect 2000; 6:103-8.
  • 58. Payne D.J., Farmer T.H. Biochemical and enzime kinetic Applications for the Characterization of b-lactamases. In: Woodford N., Johnson A.P,. editors. Molecular Bacteriology. Protocols and Clinical Applications. Totowa, New Jersey: Humana Press; 1998. p.513-35.
  • 59. Bolmstrom A., Nordstrom U., Kolar D. Etest for fingerprinting of bacteria producing b-lactamases. Proceedings of the 19th International Congress of Chemotherapy; Montreal; 1995. Abstr. P4226.
  • 60. Speldooren V., Heym B., Labia R., Nicolas-Chanoine M.-H. Discriminatory detection of inhibitor-resistant b-lactamases in Escherichia coli by single-strand conformation polymorphism-PCR. Antimicrob Agents Chemother 1998; 42:879-84.
  • 61. Paniara O., Platsouka E., Dimopoulou H., Tzelepi E., Miragou V., Tzouvelekis L.S. Diversity of beta-lactam resistance levels among related Klebsiella pneumoniae strains isolated in an intensive care unit. J Chemother 2000; 12:204-7.
  • 62. Cormican M.G., Marshall S.A., Jones R.N. Detection of extended-spectrum b-lactamase (ESBL)-producing strains by the E test ESBL screen. J Clin. Microbiol 1996; 34:1880-4.
  • 63. M’Zali F.H., Chanawong A., Kerr K.G., Birkenhead D., Hawkey P.M. Detection of extended-spectrum b-lactamases in members of the family Enterobacteriaceae: comparison of the MAST DD test, the double disc and the E test ESBL. J. Antimicrob. Chemother 2000; 45:881-5.
  • 64. Appleton A., Hall S. Evaluation of a novel diagnostic disc method for detection of extended-spectrum b-lactamases. Proceedings of the 3rd European Congress of Chemotherapy; Madrid; 2000. Abstr. T304.
  • 65. Mathew A., Harris A.M., Marshall M.J., Ross G.W. The use of analytical isoelectric focusing for detection and identification of beta-lactamases. J Gen Microbiol 1975; 88:169-78.
  • 66. Arstila T., Jacoby G.A., Huovinen P. Evaluation of five different methods to prepare bacterial extracts for the identification of b-lactamases by isoelectric focusing. J Antimicrob Chemother 1993; 32:809-16.
  • 67. Huovinen S. Rapid isoelectric focusing of plasmid-mediated beta-lactamases with Pharmacia PhastSystem. Antimicrob Agents Chemother 1988; 32:1730-2.
  • 68. Payne D.J., Thomson C.J. Molecular Approaches for the Detection and Identification of b-lactamases. Molecular Bacteriology. In: Woodford N., Johnson A.P., editors. Protocols and Clinical Applications. Totowa, New Jersey: Humana Press; 1998. p. 495-512.
  • 69. M’Zali F.H., Gascoyne-Binzi D.M., Heritage J., Hawkey P.M. Detection of mutations conferring extended-spectrum activity on SHV b-lactamases using polymerase chain reaction single strand conformational polymorphism (PCR-SSCP). J Antimicrob Chemother 1996; 37: 797-802.
  • 70. Cockerill III F.R. Genetic methods for assessing antimicrobial resistance. Antimicrob Agents Chemother 1999; 43:199-212.
  • 71. Saunders N.A., Clewley J.P. DNA amplification: general concepts and methods. In: Woodford N., Johnson A.P., editors. Molecular Bacteriology. Protocols and Clinical Applications. Totowa, New Jersey: Humana Press; 1998. p.63-82.
  • 72. Mabilat C., Goussard S. PCR detection and identification of genes for extended-spectrum b-lactamases. In: Persing D., Smith T., editors. Diagnostic Molecular Microbiology. Principles and Aplications. Washington: ASM, 1993; p.553-9.
  • 73. Bradfordford P.A. Automated thermal cycling is superior to traditional methods for nucleotide sequencing of blaSHV genes. Antimicrob Agents Chemother 1999; 43:2960-3.
  • 74. Ouellette M., Rossi J.J., Bazin R., Roy P.H. Oligonucleotide probes for the detection of TEM-1 and TEM-2 b-lactamase genes and their transposons. Can J Microbiol 1987; 33:205-11.
  • 75. Mabilat C., Courvalin P. Development of «oligotyping» for characterization and molecular epidemiology of TEM b-lactamases in members of the family Enterobacteriaceae. Antimicrob Agents Chemother 1990; 34:2210-6.
  • 76. Tham T.N., Mabilat C., Courvalin P., Guesdon J.L. Biotinylated oligonucleotide probes for the detection and the characterization of TEM-type extended broad spectrum b-lactamases in Enterobacteriaceae. FEMS Microbiol Lett 1990; 57:109-15
  • 77. Henquell C., Chanal C., Sirot D., Labia R., Sirot J. Molecular characterization of nine different types of mutants among 107 inhibitor-resistant TEM b-lactamases from clinical isolates of Escherichia coli. Antimicrob Agents Chemother 1995; 39:427-30.
  • 78. Tenover F.C., Huang M.B., Rasheed J.K., Persing D.H. Development of PCR assays to detect ampicillin resistance genes in cerebrospinal fluid samples containing Haemophilus influenzae. J Clin Microbiol 1994; 32: 2729-37.
  • 79. Sanchez-Pescador R., Stempien M.S., Urdea M.S. Rapid chemiluminescent nucleic acid assays for detection of TEM-1 b-lactamase-mediated penicillin resistance in Neisseria gonorrhoeae and other bacteria. J Clin Microbiol 1988; 26:1934-8.
  • 80. Taylor G.R., editor. Laboratory methods for the detection of mutations and polymorphisms in DNA. Boca Raton: CRC Press.; 1997. p.37-9.
  • 81. Arlet G., Brami G., Decre D., Flippo A., Gaillot O., Lagrange P.H., Philippon A. Molecular characterisation by PCR-restriction fragment length polymorphism of TEM 
  • 82. b-lactamases. FEMS Microbiol Lett 1995; 134:203-8.
  • 83. Arlet G., Goussard S., Courvalin P., Philippon P. Sequences of the genes for the TEM-20, TEM-21, TEM-22, and TEM-29 extended-spectrum b-lactamases. Antimicrob Agents Chemother 1999; 43:969-71.
  • 84. Canica M.M., Lu C.Y., Krishnamoorthy R., Paul G.C. Molecular diversity and evolution of blaTEM genes encoding b-lactamases resistant to clavulanic acid in clinical E.coli. J Mol Evol 1997; 44:57-65.
  • 85. Nuesch-Inderbinen M.T., Hachler H., Kayser F.H. Detection of genes coding for extended-spectrum SHV beta-lactamases in clinical isolates by a molecular genetic method, and comparison with the E test. Eur J Clin Microbiol Infect Dis 1996; 15:399-402.
  • 86. Hujer K.M., Hujer A.M., Bonomo R.A. Site-saturation mutagenesis of the 238 position in the SHV-1 beta-lactamase. Proceedings of the 39th Interscience Conference on Antimicrobial Agents and Chemotherapy. San Francisco; 1999. Abstr. 2051.
  • 87. Orita M., Ivahana H., Kanazawa H., Hayashi K., Sekiya T. Detection of polymorphisms of human DNA by gel electrophoresis as single-strand conformation polymorphisms. Proc Natl Acad Sci USA 1989; 86:2766-70.
  • 88. Widjojoatmojo M.N., Fluit A.C., Verhoef J. Rapid Identification of Bacteria by PCR-Single-Strand Conformation Polymorphism. J Clin Microbiol 1994; 32:3002-7.
  • 89. M’Zali F.H., Heritage J., Gascoyne-Binzi D.M., Snelling A.M., Hawkey P.M. PCR single strand conformational polymorphism can be used to detect the gene encoding SHV-7 extended-spectrum b-lactamase and to identify different SHV genes within the same strain. J Antimicrob Chemother 1998; 41:123-5.
  • 90. Chanawong A., M’Zali F.H., Heritage J., Lulitanond A., Hawkey P.M. Characterisation of extended-spectrum b-lactamases of the SHV family using a combination of PCR-single strand conformational polymorphism (PCR–SSCP) and PCR-restriction fragment length polymorphism (PCR–RFLP). FEMS Microbiol Lett; 1:85-9.
  • 91. Edelstein M.V., Stratchounski L.S. Development of single-strand conformational polymorphism (SSCP) PCR Method for discriminatory detection of genes coding for TEM-family b-lactamases. Proceedings of the 38th Interscience Conference on Antimicrobial Agents and Chemotherapy. San Diego; 1998. Abstr. E-96.
  • 92. Edelstein M., Edelstein I., Suvorov M., Kozlov R. Differentiation of SHV-type b-lactamases by REF–SSCP analysis of entire blaSHV gene sequence Proceedings of the 10th European Congress of Clinical Microbiology and Infectious Diseases. Stockholm; 2000. Abstr. TuP233.
  • 93. Kim J., Kwon Y. Development of ligase chain reaction (LCR)-PCR method for discriminatory detection of genes coding for SHV variants. Proceedings of the 39th Interscience Conference on Antimicrobial Agents and Chemotherapy. San Francisco; 1999. Abstr. 2051.
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