Biochemical characterization of β-lactamases Bla1 and Bla2 from Bacillus anthracis

Antimicrobial Agents and Chemotherapy

Volumn 47, Issue 6, 2003, Pages 2040-2042

  Materon, Isabel C ^a   Queenan, Anne Marie ^c   Koehler, Theresa M ^b   Bush, Karen ^c   Palzkill, Timothy ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF TEXAS MEDICAL SCHOOL   (United States)

^c J and J Pharmaceutical Research and Development   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMOXICILLIN; AMPICILLIN; AZTREONAM; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; BLA1 ENZYME; BLA2 ENZYME; CARBAPENEM; CARBENICILLIN; CEFALORIDINE; CEFALOTIN; CEFOTAXIME; CEFOXITIN; CEFTAZIDIME; CEPHALOSPORINASE; CLOXACILLIN; HYDROLASE; IMIPENEM; METICILLIN; NITROCEFIN; OXACILLIN; PENICILLIN G; PENICILLIN V; PENICILLINASE; PIPERACILLIN; UNCLASSIFIED DRUG;

ANTIBIOTIC RESISTANCE; ARTICLE; BACILLUS ANTHRACIS; BACTERIAL GENE; BACTERIAL STRAIN; ENZYME ACTIVITY; ESCHERICHIA COLI; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; PRIORITY JOURNAL; STEADY STATE;

ANTHRAX; ANTI-BACTERIAL AGENTS; BACILLUS ANTHRACIS; BETA-LACTAM RESISTANCE; BETA-LACTAMASES; BETA-LACTAMS; DNA, BACTERIAL; ESCHERICHIA COLI; KINETICS; MICROBIAL SENSITIVITY TESTS; RECOMBINANT PROTEINS;

EID: 0037764072     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.47.6.2040-2042.2003     Document Type: Article

References (27)

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 beta-lactamases. Biochem. J. 276:269-270.
2. Bellais, S., D. Aubert, T. Naas, and P. Nordmann. 2000. Molecular and biochemical heterogeneity of class B carbapenem-hydrolyzing β-lactamases in Chryseobacterium meningosepticum. Antimicrob. Agents Chemother. 44:1878-1886.
3. Boschi, L., P. S. Mercuri, M. L. Riccio, G. Amicosante, M. Galleni, J. M. Frere, and G. M. Rossolini. 2000. The Legionella (Fluoribacter) gormanii metallo-β-lactamase: a new member of the highly divergent lineage of molecular-subclass B3 β-lactamases. Antimicrob. Agents Chemother. 44:1538-1543.
4. 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.
5. Brook, I., T. B. Elliott, H. I. Pryor II, T. E. Sautter, B. T. Gnade, J. H. Thakar, and G. B. Knudson. 2001. In vitro resistance of Bacillus anthracis Sterne to doxycycline, macrolides and quinolones. Int. J. Antimicrob. Agents 18:559-562.
6. 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.
7. Cavallo, J. D., F. Ramisse, M. Girardet, J. Vaissaire, M. Mock, and E. Hernandez. 2002. Antibiotic susceptibilities of 96 isolates of Bacillus anthracis isolated in France between 1994 and 2000. Antimicrob. Agents Chemother. 46:2307-2309.
8. Chen, Y., J. Succi, F. C. Tenover, and T. M. Koehler. 2003. β-Lactamase genes of the penicillin-susceptible Bacillus anthracis Sterne strain. J. Bacteriol. 185:823-830.
9. Christensen, H., M. T. Martin, and S. G. Waley. 1990. Beta-lactamases as fully efficient enzymes: determination of all the rate constants in the acylenzyme mechanism. Biochem. J. 266:853-861.
10. de Seny, D., C. Prosperi-Meys, C. Bebrone, G. M. Rossolini, M. I. Page, P. Noel, J. M. Frere, and M. Galleni. 2002. Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo-beta-lactamase. Biochem. J. 363:687-696.
11. Gledhill, L., P. Williams, and B. W. Bycroft. 1991. Irreversible inactivation of beta-lactamase I from Bacillus cereus by chlorinated 6-spiroepoxypenicillins. Biochem. J. 276:801-807.
12. Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
13. Iyobe, S., H. Kusadokoro, J. Ozaki, N. Matsumura, S. Minami, S. Haruta, T. Sawai, and K. O'Hara. 2000. Amino acid substitutions in a variant of IMP-1 metallo-β-lactamase. Antimicrob. Agents Chemother. 44:2023-2027.
14. Joris, B., P. Ledent, O. Dideberg, E. Fonze, J. Lamotte-Brasseur, J. A. Kelly, J. M. Ghuysen, and J. M. Frere. 1991. Comparison of the sequences of class A β-lactamases and of the secondary structure elements of penicillin-recognizing proteins. Antimicrob. Agents Chemother. 35:2294-2301.
15. Laraki, N., N. Franceschini, G. M. Rossolini, P. Santucci, C. Meunier, E. de Pauw, G. Amicosante, J. M. Frere, and M. Galleni. 1999. Biochemical characterization of the Pseudomonas aeruginosa 101/1477 metallo-β-lactamase IMP-1 produced by Escherichia coli. Antimicrob. Agents Chemother. 43:902-906.
16. Lietz, E. J., H. Truher, D. Kahn, M. J. Hokenson, and A. L. Fink. 2000. Lysine-73 is involved in the acylation and deacylation of beta-lactamase. Biochemistry 39:4971-4981.
17. Lim, H. M., J. J. Pene, and R. W. Shaw. 1988. Cloning, nucleotide sequence, and expression of the Bacillus cereus 5/B/6 β-lactamase II structural gene. J. Bacteriol. 170:2873-2878.
18. Materon, I. C., and T. Palzkill. 2001. Identification of residues critical for metallo-beta-lactamase function by codon randomization and selection. Protein Sci. 10:2556-2565.
19. Mezes, P. S., R. W. Blacher, and J. O. Lampen. 1985. Processing of Bacillus cereus 569/H beta-lactamase I in Escherichia coli and Bacillus subtilis. J. Biol. Chem. 260:1218-1223.
20. Mohammed, M. J., C. K. Marston, T. Popovic, R. S. Weyant, and F. C. Tenover. 2002. Antimicrobial susceptibility testing of Bacillus anthracis: comparison of results obtained by using the National Committee for Clinical Laboratory Standards broth microdilution reference and Etest agar gradient diffusion methods. J. Clin. Microbiol. 40:1902-1907.
21. 2+β-lactamase. Role of the conserved cysteine in the catalytic mechanism. J. Biol. Chem. 274:13242-13249.
22. Poirel, L., T. Naas, D. Nicolas, L. Collet, S. Bellais, J. D. Cavallo, and P. Nordmann. 2000. Characterization of VIM-2, a carbapenem-hydrolyzing metallo-β-lactamase and its plasmid- and integron-borne gene from a Pseudomonas aeruginosa clinical isolate in France. Antimicrob. Agents Chemother. 44:891-897.
23. Pomerantsev, A. P., N. A. Shishkova, and L. I. Marinin. 1992. Comparison of therapeutic effects of antibiotics of the tetracycline group in the treatment of anthrax caused by a strain inheriting tet gene of plasmid pBC16. Antibiot. Khimioter. 37:31-34. (In Russian.)
24. Rasia, R. M., and A. J. Vila. 2002. Exploring the role and the binding affinity of a second zinc equivalent in B. cereus metallo-beta-lactamase. Biochemistry 41:1853-1860.
25. Sosa-Peinado, A., D. Mustafi, and M. W. Makinen. 2000. Overexpression and biosynthetic deuterium enrichment of TEM-1 beta-lactamase for structural characterization by magnetic resonance methods. Protein Expr. Purif. 19:235-245.
26. Sykes, R. B., D. P. Bonner, K. Bush, and N. H. Georgopapadakou. 1982. Azthreonam (SQ 26,776), a synthetic monobactam specifically active against aerobic gram-negative bacteria. Antimicrob. Agents Chemother. 21:85-92.
27. Yano, H., A. Kuga, R. Okamoto, H. Kitasato, T. Kobayashi, and M. Inoue. 2001. Plasmid-encoded metallo-β-lactamase (IMP-6) conferring resistance to carbapenems, especially meropenem. Antimicrob. Agents Chemother. 45:1343-1348.