Selection of naturally occurring extended-spectrum TEM β-lactamase variants by fluctuating β-lactam pressure

Antimicrobial Agents and Chemotherapy

Volumn 44, Issue 8, 2000, Pages 2182-2184

  Blazquez, Jesús ^a   Morosini, María Isabel ^a   Negri, María Cristina ^a   Baquero, Fernando ^a  

^a HOSPITAL RAMÓN Y CAJAL   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

AMOXICILLIN; BETA LACTAMASE; CEFTAZIDIME;

ANTIBACTERIAL ACTIVITY; ARTICLE; BACTERIUM CULTURE; BACTERIUM ISOLATION; CULTURE MEDIUM; ENZYME ACTIVITY; ESCHERICHIA COLI; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; PRIORITY JOURNAL;

ANTI-BACTERIAL AGENTS; BETA-LACTAM RESISTANCE; BETA-LACTAMASES; BETA-LACTAMS; ESCHERICHIA COLI; POINT MUTATION; SELECTION (GENETICS);

EID: 0033944301     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.44.8.2182-2184.2000     Document Type: Article

References (22)

1. Ambler, R. P., F. W. Coulson, J. M. Frere, J. M. Ghuysen, B. Joris, M. Forsman, R. C. Levesque, G. Tiraby, and S. G. Waley. 1991. A standard numbering scheme for class A β-lactamases. Biochem. J. 276:269-272.
2. Blázquez, J., M. R. Baquero, R. Cantón, I. Alós, 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.
3. Blázquez, J., M. I. Morosini, M. C. Negri, M. González-Leiza, and F. Baquero. 1995. Single amino acid replacements in positions altered in naturally occurring extended-spectrum TEM β-lactamases. Antimicrob. Agents Chemother. 39:145-149.
4. Blázquez, J., M. C. Negri, M. I. Morosini, J. M. Gómez-Gómez, and F. Baquero. 1998. A237T as a modulating mutation in naturally occurring extended-spectrum TEM-type β-lactamases. Antimicrob. Agents Chemother. 42:1042-1044.
5. Bush, K. 1989. Classification of β-lactamases: groups 1, 2a, 2b, and 2b′. Antimicrob. Agents Chemother. 33:264-270.
6. Bush, K., G. A. Jacoby, and A. A. Medeiros. 1995. A functional clasification scheme for β-lactamases and its correlation with molecular structure. Antimicrob. Agents Chemother. 39:1211-1233.
7. Cantu, C., W. Huang, and T. Palzkill. 1996. Selection and characterization of amino acid substitutions at residues 237-240 of TEM-1 β-lactamase with altered substrate specificity for aztreonam and ceftazidime. J. Biol. Chem. 271:22538-22545.
8. Chaibi, E. B., S. Farzaneh, J. Peduzzi, M. Barthelemy, and R. Labia. 1996. An additional ionic bond suggested by molecular modelling of TEM-2 might induce a slight discrepancy between catalytic properties of TEM-1 and TEM-2 beta-lactamases. FEMS Microbiol. Lett. 143:121-125.
9. Dickerson, R. E. 1977. Energy and evolution in the folding of proteins. In M. Kimura (ed.), Molecular evolution and polymorphism. National Institute of Genetics, Mishima, Japan.
10. Farzaneh, S., E. B. Chaibi, J. Peduzzi, M. Barthelemy, R. Labia, J. Blázquez, and F. Baquero. 1996. Implication of Ile-69 and Thr-182 residues in kinetic characteristics of IRT-3 (TEM-32) β-lactamase. Antimicrob. Agents Chemother. 40:2434-2436.
11. Huang, W., and T. Palzkill. 1997. A natural polymorphism in β-lactamase is a global suppressor. Proc. Natl. Acad. Sci. USA 94:8801-8806.
12. Kauffmann, S. A. 1993. The structure of adaptive landscapes underlying protein evolution, p. 121-172. In The origins of order. Oxford University Press, Oxford, United Kingdom.
13. Mainard-Smith, J. 1970. Natural selection and the concept of protein space. Nature 225:573.
14. Medeiros, A. A. 1997. Evolution and dissemination of β-lactamases accelerated by generations of β-lactam antibiotic. Clin. Infect. Dis. 24:S19-S45.
15. National Committee for Clinical Laboratory Standards. 1993. Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically. Approved standard M7-A3. National Committee for Clinical Laboratory Standards, Wayne, Pa.
16. Oliphant, A. R., and K. Struhl. 1989. An efficient method for generating proteins with altered enzymatic properties: application to β-lactamase. Proc. Natl. Acad. Sci. USA 86:9094-9098.
17. Palzkill, T., and D. Botstein. 1992. Identitication of amino acid substitutions that alter the substrate specificity of TEM-1 β-lactamase. J. Bacteriol. 174: 5237-5243.
18. Palzkill, T., Q. Le, K. V. Venkatachalam, 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.
19. Petrosino, J. F., and T. Palzkill. 1996. Systematic mutagenesis of the active site omega loop of TEM-1 β-lactamase. J. Bacteriol. 178:1821-1828.
20. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
21. Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463-5467.
22. Venkatachalam, 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.