Amino acid substitutions at ambler position Gly238 in the SHV-1 β-lactamase: Exploring sequence requirements for resistance to penicillins and cephalosporins

Antimicrobial Agents and Chemotherapy

Volumn 46, Issue 12, 2002, Pages 3971-3977

  Hujer, Andrea M ^a   Hujer, Kristine M ^a   Helfand, Marion S ^a   Anderson, Vernon E ^c   Bonomo, Robert A ^a,b,d  

^a UNIVERSITY HOSPITALS OF CLEVELAND   (United States)

^b Infectious Diseases Section   (United States)

^c CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d LOUIS STOKES CLEVELAND VA MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMPICILLIN; BETA LACTAMASE; CEFALORIDINE; CEFOTAXIME; CEFTAZIDIME; CEPHALOSPORIN; NITROCEFIN; OXYIMINOCEPHALOSPORIN; PENICILLIN G; PIPERACILLIN; UNCLASSIFIED DRUG; BETA LACTAMASE PIT 2; BETA-LACTAMASE PIT-2;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANTIBIOTIC RESISTANCE; ANTIBIOTIC SENSITIVITY; ARTICLE; AUTORADIOGRAPHY; CRYSTAL STRUCTURE; DNA SEQUENCE; DRUG STRUCTURE; ENZYME KINETICS; ENZYME LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI; GENE MUTATION; HYDROGEN BOND; MINIMUM INHIBITORY CONCENTRATION; MUTAGENESIS; NONHUMAN; PENICILLIN RESISTANCE; PHENOTYPE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; STEADY STATE; DRUG EFFECT; GENETICS; METABOLISM; MICROBIOLOGICAL EXAMINATION;

BETA-LACTAMASES; CEPHALOSPORIN RESISTANCE; MICROBIAL SENSITIVITY TESTS; MUTAGENESIS; PENICILLIN RESISTANCE;

EID: 0036894095     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.46.12.3971-3977.2002     Document Type: Article

References (30)

1. Ambler, R. P., A. F. 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 the class A β-lactamases. Biochem. J. 276(Pt. 1):269-270.
2. 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.
3. Bush, K., G. A. Jacoby, and A. A. Medeiros. 1995. A functional classification scheme for β-lactamases and its correlation with molecular structure. Antimicrob. Agents Chemother. 39:1211-1233.
4. Cantu III, C., W. Huang, and T. Palzkill. 1997. Cephalosporin substrate specificity determinants of TEM-1 β-lactamase. J. Biol. Chem. 272:29144-29150.
5. Cantu III, C., W. Huang, and T. Palzkill. 1996. Selection and characterization of amino acid substitutions at residues 237 to 240 of TEM-1 β-lactamase with altered substrate specificity for aztreonam and ceftazidime. J. Biol. Chem. 271:22538-22545.
6. Cantu III, C., and T. Palzkill. 1998. The role of residue 238 of TEM-1 β-lactamase in the hydrolysis of extended-spectrum antibiotics. J. Biol. Chem. 273:26603-26609.
7. Hujer, A. M., K. M. Hujer, and R. A. Bonomo. 2001. Mutagenesis of amino acid residues in the SHV-1 β-lactamase: The premier role of Gly238Ser in penicillin and cephalosporin resistance. Biochim. Biophys. Acta 1547:37-50.
8. Hujer, A. M., M. G. P. Page, M. S. Helfand, B. Yeiser, and R. A. Bonomo. 2002. Development of a sensitive and specific enzyme-linked immunosorbent assay for detecting and quantifying CMY-2 and SHV β-lactamases. J. Clin. Microbiol. 40:1947-1957.
9. Huletsky, A., J. R. Knox, and R. C. Levesque. 1993. Role of Ser-238 and Lys-240 in the hydrolysis of third-generation cephalosporins by SHV-type β-Lactamases probed by site-directed mutagenesis and three-dimensional modeling. J. Biol. Chem. 268:3690-3697.
10. 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.
11. Kuzin, A. P., M. Nukaga, Y. Nukaga, A. M. Hujer, R. A. Bonomo, and J. R. Knox. 1999. Structure of the SHV-1 β-lactamase. Biochemistry 38:5720-5727.
12. Labia, R., A. Morand, K. Tiwari, J. Sirot, D. Sirot, and A. Petit. 1988. Interactions of new plasmid-mediated β-lactamases with third-generation cephalosporins. Rev. Infect. Dis. 10:885-891.
13. Lee, K.-Y., J. D. Hopkins, T. F. O'Brien, and M. Syvanen. 1991. Gly238Ser substitution changes the substrate specificity of the SHV class A β-lactamase. Proteins Struct. Funct. Genet. 11:45-51.
14. Lenfant, F., R. Labia, and J. M. Masson. 1990. Probing the active site of β-lactamase R-TEM1 by informational suppression. Biochimie 72:495-503.
15. Lin, S., M. Thomas, D. M. Shlaes, S. D. Rudin, J. R. Knox, V. E. Anderson, and R. A. Bonomo. 1998. Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 β-lactamase, an SHV-family class A enzyme. Biochem. J. 333(Pt. 2):395-400.
16. Medeiros, A. A. 1997. Evolution and dissemination of β-lactamases accelerated by generations of β-lactam antibiotics. Clin. Infect. Dis. 24(Suppl. 1):S19-S45.
17. Orencia, M. C., J. S. Yoon, J. E. Ness, W. P. Stemmer, and R. C. Stevens. 2001. Predicting the emergence of antibiotic resistance by directed evolution and structural analysis. Nat. Struct. Biol. 8:238-242.
18. Palzkill, T., Q. 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. Paterson, D. L., L. B. Rice, and R. A. Bonomo. 2001. Rapid method of extraction and analysis of extended-spectrum β-lactamases from clinical strains of Klebsiella pneumoniae. Clin. Microbiol. Infect. 7:709-711.
20. 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.
21. Philippon, A., R. Labia, and G. A. Jacoby. 1989. Extended-spectrum β-lactamases. Antimicrob. Agents Chemother. 33:1131-1136.
22. Raquet, X., J. Lamotte-Brasseur, E. Fonze, S. Goussard, P. Courvalin, and J. M. Frere. 1994. TEM β-lactamase mutants hydrolysing third-generation cephalosporins: A kinetic and molecular modeling analysis. J. Mol. Biol. 244:625-639.
23. Raquet, X., M. Vanhove, J. Lamotte-Brasseur, S. Goussard, P. Courvalin, and J. M. Frere. 1995. Stability of TEM β-lactamase mutants hydrolyzing third generation cephalosporins. Proteins Struct. Funct. Genet. 23:63-72.
24. Rasheed, J. K., G. J. Anderson, H. Yigit, A. M. Queenan, A. Domenech-Sanchez, J. M. Swenson, J. W. Biddle, M. J. Ferraro, G. A. Jacoby, and F. C. Tenover. 2000. Characterization of the extended-spectrum β-lactamase reference strain, Klebsiella pneumoniae K6 (ATCC 700603), which produces the novel enzyme SHV-18. Antimicrob. Agents Chemother. 44:2382-2388.
25. Rice, L. B., L. L. Carias, A. M. Hujer, M. Bonafede, R. Hutton, C. Hoyen, and R. A. Bonomo. 2000. High-level expression of chromosomally encoded SHV-1 β-lactamase and an outer membrane protein change confer resistance to ceftazidime and piperacillin-tazobactam in a clinical isolate of Klebsiella pneumoniae. Antimicrob. Agents Chemother. 44:362-367.
26. Rice, L. B., E. C. Eckstein, J. DeVente, and D. M. Shlaes. 1996. Ceftazidime-resistant Klebsiella pneumoniae isolates recovered at the Cleveland Department of Veterans Affairs Medical Center. Clin. Infect. Dis. 23:118-124.
27. Rice, L. B., S. H. Willey, G. A. Papanicolaou, A. A. Medeiros, E. M. Eliopoulos, R. C. Moellering, Jr., and G. A. Jacoby. 1990. Outbreak of ceftazidime resistance caused by extended-spectrum β-lactamases at a Massachusetts chronic care facility. Antimicrob. Agents Chemother. 34:2193-2199.
28. Saves, I., O. Burlet-Schlitz, L. Maveyraud, J. P. Samama, J. C. Prome, and J. M. Masson. 1995. Mass spectral kinetic study of acylation and deacylation during the hydrolysis of penicillins and cefotaxime by β-lactamase TEM-1 and the G238S mutant. Biochemistry 34:11660-11667.
29. 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.
30. Yuan, M., L. M. Hall, P. H. Savelkoul, C. M. Vandenbroucke-Grauls, and D. M. Livermore. 2000. SHV-13, a novel extended-spectrum β-lactamase, in Klebsiella pneumoniae isolates from patients in an intensive care unit in Amsterdam. Antimicrob. Agents Chemother. 44:1081-1084.