Characterization of a new TEM-derived β-lactamase produced in a Serratia marcescens strain

Antimicrobial Agents and Chemotherapy

Volumn 41, Issue 11, 1997, Pages 2374-2382

  Perilli, Mariagrazia ^a   Felici, Antonio ^a,f   Franceschini, Nicola ^a   De Santis, Annalisa ^a   Pagani, Laura ^b   Luzzaro, Francesco ^c   Oratore, Arduino ^a   Rossolini, Gian M ^d   Knox, James R ^e   Amicosante, Gianfranco ^a  

^a UNIVERSITY OF L'AQUILA   (Italy)

^b UNIVERSITY OF PAVIA   (Italy)

^c OSPEDALE DI CIRCOLO   (Italy)

^d UNIVERSITY OF SIENA   (Italy)

^e UNIVERSITY OF CONNECTICUT   (United States)

^f GSK   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

6BETA IODOPENICILLANIC ACID; AMPICILLIN; AZTREONAM; BETA LACTAMASE; CARBENICILLIN; CEFALORIDINE; CEFALOTIN; CEFAZOLIN; CEFOTAXIME; CEFTAZIDIME; CLAVULANIC ACID; GLUTAMIC ACID; NITROCEFIN; OXACILLIN; PENICILLIN DERIVATIVE; PENICILLIN G; PIPERACILLIN; SULBACTAM; TRIPEPTIDE;

ANTIBIOTIC RESISTANCE; ARTICLE; CONTROLLED STUDY; CRYSTALLOGRAPHY; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME STRUCTURE; ENZYME SYNTHESIS; EPIDEMIC; MOLECULAR MODEL; NONHUMAN; NUCLEOTIDE SEQUENCE; POINT MUTATION; PRIORITY JOURNAL; SERRATIA MARCESCENS;

EID: 0030685111     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/aac.41.11.2374     Document Type: Article

References (43)

1. Ambler, R. P., J.-M. Frère, J.-M. Ghuysen, B. Joris, R. C. Levesque, G. Tiraby, S. G. Waley, and A. F. W. Coulson. 1991. A standard numbering scheme for class A β-lactamases. Biochem. J. 276:269-272.
2. Amersham Life Science. Step-by-step protocols. Sequenase Version 2.0. DNA polymerase for sequencing PCR products, 2nd ed. Amersham Life Science, Arlington Heights, Ill.
3. Blazquez, J., M. R. Baquero, R. Canton, I. Alos, and F. Baquero. 1993. Characterization of a new TEM-type β-lactamase resistant to clavulanate, sulbactam, and tazobactam in a clinical isolate of Escherichia coli. Antimicrob. Agents Chemother. 37:2059-2063.
4. Bonomo, R. A., C. G. Dawes, J. R. Knox, and D. M. Shlaes. 1995. A complementary role of mutations at positions 69 and 242 in class A β-lactamase. Biochim. Biophys. Acta 1247:113-120.
5. Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
6. Bradford, P. A., C. Urban, A. Jaiswal, N. Mariano, B. A. Rasmussen, S. J. Projan, J. J. Rahal, and K. Bush. 1995. SHV-7, a novel cefotaxime-hydrolyzing β-lactamase, identified in Escherichia coli isolates from hospitalized nursing home patients. Antimicrob. Agents Chemother. 39:899-905.
7. Bush, K. 1989. Characterization of β-lactamases. Antimicrob. Agents Chemother. 33:259-263.
8. Chanal, C., M. C. Poupart, D. Sirot, R. Labia, J. Sirot, and R. Cluzel. 1992. Nucleotide sequences of CAZ-2, CAZ-6, and CAZ-7 β-lactamase genes. Antimicrob. Agents Chemother. 36:1817-1820.
9. De Meester, F., J.-M. Frère, S. G. Waley, S. J. Cartwright, R. Virden, and F. Lindberg. 1986. 6-β-Iodopenicillanate as a probe for the classification of β-lactamases. Biochem. J. 239:575-580.
10. Dideberg, O., P. Charlier, J.-P. Wery, P. Dehottay, J. Dusart, T. Erpicum, J.-M. Frère, and J.-M. Ghuysen. 1987. The crystal structure of the β-lactamase of Streptomyces albus G at 3 Å resolution. Biochem. J. 245:911-913.
11. Fonze, E., P. Charlier, Y. To'th, M. Vermeire, X. Raquet, A. Dubus, and J.-M. Frère. 1995. β-Lactamase structure solved by molecular replacement and refined structure of the S235A mutant. Acta Crystallogr. Sect. D 51: 682-694.
12. Hall, A., and J. R. Knowles. 1976. Directed selective pressure on a β-lactamase to analyze molecular changes involved in development of enzyme function. Nature (London) 264:803-804.
13. Herzberg, O. 1991. Refined crystal structure of β-lactamase. J. Mol. Biol. 217:701-719.
14. Huletsky, A., J. R. Knox, and R. C. Levesque. 1993. The role of Ser238 and Lys240 in the hydrolysis of third-generation cephalosporins by SHV-type β-lactamases probed by site-directed mutagenesis and three dimensional modeling. J. Biol. Chcm. 268:3690-3697.
15. Imtiaz, U., E. M. Billings, J. R. Knox, E. K. Manavathu, S. A. Lerner, and S. Mobashery. 1993. Inactivation of class A β-lactamases by clavulanic acid: the role of arginine-244 in a non-concerted sequence of events. J. Am. Chem. Soc. 115:4435-4442.
16. Jacoby, G. A., and A. A. Medeiros. 1991. More extended-spectrum β-lactamases. Antimicrob. Agents Chemother. 35:1697-1704.
17. Jelsch, C., L. Mourey, J.-M. Masson, and J. P. Samama. 1993. Crystal structure of E. coli TEM-1 β-lactamase at 1.8 Å resolution. Proteins Struct. Funct. Genet. 16:364-383.
18. Jones, T. A. 1985. Interactive computer graphics: FRODO. Methods Enzymol. 115:157-170.
19. Kado, C. I., and S. T. Liu. 1981. Rapid procedure for detection and isolation of large and small plasmids. J. Bacteriol. 145:1365-1373.
20. Knox, J. R. 1995. Extended-spectrum and inhibitor-resistant TEM-type β-lactamases: mutations, specificity, and three-dimensional structure. Antimicrob. Agents Chemother. 39:2593-2601.
21. Knox, J. R., P. C. Moews, W. Escobar, and A. L. Fink. 1993. A catalytically-impaired β-lactamase: kinetics and structure of the Bacillus licheniformis E166A mutant. Protein Eng. 6:11-18.
22. Kraulis, P. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:946-950.
23. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
24. Lamotte-Brasseur, J., G. Dive, O. Dideberg, P. Charlier, J. M. Frère, and J. M. Ghuysen. 1991. Mechanism of acyl transfer by the class A serine β-lactamase of Streptomyces albus G. Biochem. J. 279:213-221.
25. Lamotte-Brasseur, J., J. R. Knox, J. A. Kelly, P. Charlier, E. Fonze, O. Dideberg, and J.-M. Frère. 1994. The structures and catalytic mechanisms of active-site serine β-lactamases. Genet. Eng. Rev. 12:189-229.
26. Lee, K. Y., J. D. Hopkins, T. F. O'Brien, and M. Syvanen. 1991. Gly-238-Ser substitution changes the substrate specificity of the SHV class A β-lactamases. Proteins Struct. Funct. Genet. 11:45-51.
27. Lindström, E. B., H. G. Boman, and B. B. Steele. 1970. Resistance of Escherichia coli to penicillins. J. Bacteriol. 101:218-231.
28. Mabilat, C., S. Goussard, W. Sougakoff, R. C. Spencer, and P. Courvalin. 1990. Direct sequencing of the amplified structural gene and promoter for the extended-broad-spectrum β-lactamase TEM-9 (RHH-1) of Klebsiella pneumoniae. Plasmid 23:27-34.
29. Matagne, A., and J. M. Frère. 1995. Contribution of mutant analysis to the understanding of enzyme catalysis: the case of class A β-lactamases. Biochim. Biophys. Acta 1246:109-127.
30. Maveyraud, L., I. Massova, C. Birck, K. Miyashita, J. P. Samama, and S. Mobashery. 1996. Crystal structure of 6α-(hydroxymethyl)-penicillanate complexed to the TEM-1 β-lactamase from Escherichia coli: evidence on the mechanism of action of a novel inhibitor designed by a computer-aided process. J. Am. Chem. Soc. 118:7435-7440.
31. Moews, P. C., J. R. Knox, O. Dideberg, P. Charlier, and J. M. Frè. 1990. β-Lactamase of Bacillus licheniformis 749/C at 2 Å resolution. Proteins Struct. Funct. Genet. 7:156-171.
32. National Committee for Clinical Laboratory Standards. 1990. Reference methods for the determination of minimum inhibitory concentrations (MICs) of aerobic bacteria by broth macrodilution, broth microdilution, and agar dilution. Approved standard M7-A2. National Committee for Clinical Laboratory Standards, Villanova, Pa.
33. Pagani, L., F. Luzzaro, P. Ronza, A. Rossi, P. Micheletti, F. Porta, and E. Romero. 1994. Outbreak of extended-spectrum β-lactamase producing Serratia marcescens in an intensive care unit. FEMS Immunol. Med. Microbiol. 10:39-46.
34. Palzkill, T., and D. Botstein. 1992. Identification of amino acid substitutions that alter the substrate specificity of TEM-1 β-lactamase. J. Bacteriol. 174: 5237-5243.
35. Palzkill, T., Q.-Q. Le, K. V. Vankatachalam, M. LaRocco, and H. Ocera. 1994. Evolution of antibiotic resistance: several different amino acid substitutions in an active-site loop alter the substrate profile of β-lactamase. Mol. Microbiol. 12:217-229.
36. Raquet, X., J. Lamotte-Brasseur, E. Fronzè, S. Goussard, P. Courvalin, and J.-M. Frère. 1994. TEM β-lactamase mutants hydrolysing third-generation cephalosporins. J. Mol. Biol. 244:625-639.
37. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Modular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
38. Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463-5467.
39. Shlaes, D. M., and C. Currie-McCumber. 1992. Mutations altering substrate specificity in OHIO-1, an SHV-1 family β-lactamase. Biochem. J. 284:411-415.
40. Sowek, J. A., S. B. Singer, S. Ohringer, M. F. Mally, T. J. Dougherty, J. Z. Gougoutas, and K. Bush. 1991. Substitution of lysine at position 104 or 240 of TEM β-lactamase enhances the effect of serine 164 substitution of hydrolysis or affinity for cephalosporins and the monobactam, aztreonam. Biochemistry 30:3179-3188.
41. Strynadka, N. C. J., H. Adachi, S. E. Jensen, K. Johns, A. Sielecki, C. Betzel, K. Sutoh, and M. N. G. James. 1992. Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution. Nature (London) 359:700-705.
42. Vankatachalam, K. V., W. Huang, M. LaRocco, and T. Palzkill. 1994. Characterization of TEM-1 β-lactamase mutants from positions 238 to 241 with increased catalytic efficiency for ceftazidime. J. Biol. Chem. 269: 23444-23450.
43. Viadiu, H., J. Osuna, A. L. Fink, and X. Soberon. 1995. A new TEM β-lactamase double mutant with broadened specificity reveals substrate-dependent functional interactions. J. Biol. Chem. 270:781-787.