Kinship and diversification of bacterial penicillin-binding proteins and β-lactamases

Antimicrobial Agents and Chemotherapy

Volumn 42, Issue 1, 1998, Pages 1-17

  Massova, Irina ^a   Mobashery, Shahriar ^a  

^a WAYNE STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BETA LACTAMASE; BINDING PROTEIN; PENICILLIN BINDING PROTEIN;

AMINO ACID SEQUENCE; CATALYSIS; CELL WALL; DATA BASE; ENTEROCOCCUS; ENZYME STRUCTURE; EVOLUTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; SHORT SURVEY; STREPTOCOCCUS; STRUCTURE ACTIVITY RELATION;

EID: 0031973490     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/aac.42.1.1     Document Type: Short Survey

References (57)

1. Adachi, H., T. Ohta, and H. Matsuzawa. 1991. Site-directed mutants, at position 166, of RTEM-1 β-lactamase that form a stable acyl-enzyme intermediate with penicillin. J. Biol. Chem. 266:3186-3191.
2. Bulychev, A., I. Massova, K. Miyashita, and S. Mobashery. 1997. Evolution of the versatile β-lactam hydrolase activity: from biosynthetic enzymes to drug resistance factors. J. Am. Chem. Soc. 119:7619-7625.
3. Bush, K., and G. Jacoby. 1997. Nomenclature of TEM β-lactamases. J. Antimicrob. Chemother. 39:1-3.
4. 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.
5. Bush, K., S. A. Smith, S. Ohringer, S. K. Tanaka, and D. P. Bonner. 1987. Improved sensitivity in assays for binding of novel β-lactam antibiotics to penicillin-binding proteins of Escherichia coli. Antimicrob. Agents Chemother. 31:1271-1273.
6. Carfi, A., E. Duee, M. Galleni, J. M. Frère, and O. Dideberg. (1bme Brookhaven Protein Data Bank) Though structures are available, the publications have not appeared in the literature yet.
7. Carfi, A., J. P. Soto, E. Duee, M. Galleni, J. M. Frère, and O. Dideberg. (1bme Brookhaven Protein Data Bank) Though structures are available, the publications have not appeared in the literature yet.
8. Carfi, A., S. Pares, E. Duee, M. Galleni, C. Duez, J. M. Frère, and O. Dideberg. 1995. The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 14:4914.
9. Chen, C. C., J. Rahil, R. F. Pratt, and O. Herzberg. 1993. Structure of a phosphonate-inhibited β-lactamase. An analog of the tetrahedral transition state/intermediate of β-lactam hydrolysis. J. Mol. Biol. 234:165-178.
10. Cohen, M. L. 1992. Epidemiology of drug resistance: implications for a post-antimicrobial era. Science 257:1050-1055.
11. Concha, N. O., B. A. Rasmussen, K. Bush, and O. Herzberg. 1996. Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis. Structure 4:823-836.
12. Davies, J. 1994. Inactivation of antibiotics and the dissemination of resistance genes. Science 264:375-382.
13. 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 0.3 nm resolution. Biochem. J. 245: 911-913.
14. Dideberg, O., M. Libert, J. M. Frère, P. Charlier, H. Zhao, and J. R. Knox. 1985. Crystallization and preliminary X-ray data for the exocellular β-lactamase of Bacillus licheniformis 749/C. J. Mol. Biol. 181:145-146.
15. Escobar, W. A., A. K. Tan, and A. L. Fink. 1991. Site-directed mutagenesis of β-lactamase leading to accumulation of a catalytic intermediate. Biochemistry 30:10783.
16. Georgopapadakou, N. H. 1993. Penicillin-binding proteins and bacterial resistance to β-lactams. Antimicrob. Agents Chemother. 37:2045-2053.
17. Ghuysen, J. M. 1991. Serine β-lactamases and penicillin-binding proteins. Annu. Rev. Microbiol. 45:37-67.
18. Ghuysen, J. M. 1994. Molecular structures of penicillin-binding proteins and β-lactamases. Trends Microbiol. 2:372-380.
19. Ghuysen, J. M. 1997. Penicillin-binding proteins. Wall peptidoglycan assembly and resistance to penicillin: facts, doubts and hopes. Int. J. Antimicrob. Agents 8:45-60.
20. Ghuysen, J. M., P. Charlier, J. Coyette, C. Duez, E. Fonzé, C. Fraipont, C. Goffin, B. Joris, and M. Nguyen-Distèche. 1996. Penicillin and beyond: evolution, protein fold, multimodular polypeptides, and multiprotein complexes. Microb. Drug Resist. 2:163-175.
21. Grebe, T., and R. Hakenbeck. 1996. Penicillin-binding proteins 2b and 2x of Streptococcus pneumoniae are primary resistance determinants for different classes of β-lactam antibiotics. Antimicrob. Agents Chcmother. 40:829-834.
22. Hardt, K., B. Joris, S. Lepage, R. Brasseur, J. O. Lampen, J. M. Frère, A. L. Fink, and J. M. Ghuysen. 1997. The penicillin sensory transducer, BlaR, involved in the inducibility of β-lactamase synthesis in Bacillus licheniformis is embedded in the plasma membrane via a four-α-helix bundle. Mol. Microbiol. 23:935-944.
23. Hardy, L. W., and J. F. Kirsch. 1984. pH dependence and solvent deuterium oxide kinetic isotope effect on Bacillus cereus β-lactamase I catalyzed reactions. Biochemistry 23:1275.
24. Herzberg, O. 1991. Refined crystal structure of β-lactamase from Staphylococcus aureus PC1 at 2.0 Å resolution. J. Mol. Biol. 217:701-719.
25. Holland, H. D. 1997. Geochemistry-evidence for life on Earth more than 3850-million years ago. Science 275:38-39.
26. Jasmin, M., J. M. Wilkin, and J. M. Frère. 1995. Bacterial DD-transpeptidases and penicillin. Essays Biochem. 29:1-24.
27. Jelsch, C., F. Lenfant, J. M. Masson, and J. P. Samama. 1992. β-Lactamase TEM1 of E. coli. Crystal structure determination at 2.5 Å resolution. FEBS Lett. 299:135-142.
28. Jelsch, C., L. Mourey, J. M. Masson, and J. P. Samama. 1993. Crystal structure of Escherichia coli TEM1 β-lactamase at 1.8 Å resolution. Proteins 16:364-383.
29. Kelly, J. A., O. Dideberg, P. Charlier, J. P. Wery, M. Libert, P. C. Moews, J. R. Knox, C. Duez, C. Fraipont, B. Joris, J. Dusart, J. M. Frère, and J. M. Ghuysen. 1986. On the origin of bacterial resistance to penicillin: comparison of a β-lactamase and a penicillin target. Science 231:1429-1431.
30. Kelly, J. A., and A. P. Kuzin. 1995. The refined crystallographic structure of a DD-peptidase penicillin-target enzyme at 1.6 Å resolution. J. Mol. Biol. 254:223-236.
31. Knox, J. R., and P. C. Moews. 1991. β-Lactamase of Bacillus licheniformis 749/C. Refinement at 2 Å resolution and analysis of hydration. J. Mol. Biol. 220:435-455.
32. Knox, J. R., P. C. Moews, and J. M. Frère. 1996. Molecular evolution of bacterial β-lactam resistance. Chem. Biol. 3:937-947.
33. Kuwaharaarai, K., N. Kondo, S. Hori, E. Tatedasuzuki, and K. Hiramatsu. 1996. Suppression of methicillin resistance in a mecA-containing pre-methicillin-resistant Staphylococcus aureus strain is caused by the mecI-mediated repression of PBP 2′ production. Antimicrob. Agents Chemother. 40:2680-2685.
34. Kuzin, A. P., H. Liu, J. A. Kelly, and J. R. Knox. 1995. Binding of cephalothin and cefotaxime to D-Ala-D-Ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum β-lactamases. Biochemistry 34:9532-9540.
35. Lobkovsky, E., E. M. Billings, P. C. Moews, J. Rahil, R. F. Pratt, and J. R. Knox. 1994. Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: mechanistic interpretation of a β-lactamase transition-state analog. Biochemistry 33:6762-6772.
36. Lobkovsky, E., P. C. Moews, H. Liu, H. Zhao, J. M. Frère, and J. R. Knox. 1993. Evolution of an enzyme activity: crystallographic structure at 2-Å resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase. Proc. Natl. Acad. Sci. USA 90:11257-11261.
37. Manchester, L. C., B. Poeggeler, F. L. Alvares, G. B. Ogden, and R. J. Reiter. 1995. Melatonin immunoreactivity in the photosynthetic prokaryote Rhodospirillum rubrum: implications for an ancient antioxidant system. Cell. Mol. Biol. Res. 41:391-395.
38. Maveyraud, L., I. Massova, C. Brick, 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.
39. Medeiros, A. A. 1997. Evolution and dissemination of β-lactamases accelerated by generations of β-lactam antibiotics. Clin. Infect. Dis. 24(Suppl.):S19-S45.
40. Moews, P. C., J. R. Knox, O. Dideberg, P. Charlier, and J. M. Frère. 1990. β-Lactamase of Bacillus licheniformis 749/C at 2 Å resolution. Proteins Struct. Funct. 7:156-171.
41. Molecular Simulations Inc. Insight II package. Molecular Simulations, Inc., San Diego, Calif.
42. Needleman, S. B., and C. D. Wunsch. 1970. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol. 48:443-453.
43. Oefner, C., A. D'Arcy, J. J. Daly, K. Gubernator, R. L. Charnas, I. Heinze, C. Hubschwerlen, and F. K. Winkler. 1990. Refined crystal structure of β-lactamase from Citrobacter freundii indicates a mechanism for β-lactam hydrolysis. Nature 343:284-288.
44. Pares, S., N. Mouz, Y. Petillot, R. Hakenbeck, and O. Dideberg. 1996. X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Nature Struct. Biol. 3:284-289.
45. r-encoding gene of Enterococcus hirae S185: modular design and structural organization of the protein. J. Bacteriol. 175:2844-2852.
46. Samama, J.-P. Unpublished data by personal communication.
47. Samraoui, B., B. J. Sutton, R. J. Todd, P. J. Artymiuk, S. G. Waley, and D. C. Phillips. 1986. Tertiary structural similarity between a class A β-lactamase and a penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase. Nature 320:378-380.
48. Sirot, D., C. Recule, E. B. Chaibi, L. Bret, J. Croize, C. Chanal-Claris, R. Labia, and J. Sorot. 1997. A complex mutant of TEM-1 β-lactamase with mutations encountered in both IRT-4 and extended-spectrum TEM-15, produced by an Escherichia coli clinical isolate. Antimicrob. Agents Chemother. 41:1322-1325.
49. Sneath, P. H. A., and R. R. Sokal. 1973. Sequential, agglomerative, nonoverlapping clustering methods, p. 230-234. In D. Kennedy and R. B. Park (ed.), Numerical taxonomy. The principles and practice of numerical classification. W. H. Freeman & Co., San Francisco, Calif.
50. Sonnhammer, E. L. L., and D. Kahn. 1994. The modular arrangement of proteins as inferred from analysis of homology. Protein Sci. 3:482-492.
51. Sougakoff, W., V. Jarlier, J. Delettre, N. Colloc'h, G. L'Hermite, P. Nordmann, and T. Naas. 1996. Purification, crystallization, and preliminary X-ray diffraction analysis of the carbapenem-hydrolyzing class A β-lactamase Sme-1 from Serratia marcescens. J. Struct. Biol. 116:313-316.
52. Strynadka, N. C., H. Adachi, S. E. Jensen, K. Johns, A. Sielecki, C. Betzel, K. Sutoh, and M. N. James. 1992. Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution. Nature 359:700-705.
53. Taibi-Tronche, P., I. Massova, S. B. Vakulenko, S. A. Lerner, and S. Mobashery. 1996. Evidence for structural elasticity of class-A β-lactamases in the course of catalytic turnover of the novel cephalosporin cefepime. J. Am. Chem. Soc. 118:7441-7448.
54. Thunnissen, A. M., and B. W. Dijkstra. 1996. Cure for a crisis? Nature Struct. Biol. 3:218-221.
55. Tripos, Inc. Sybyl molecular modeling software. Tripos, Inc., St. Louis, Mo.
56. World Health Organization. 1996. The world health report 1996. Fighting disease, fostering development. World Health Organization, Geneva, Switzerland.
57. Zorzi, W., X. Y. Zhou, O. Dardenne, J. Lamotte, D. Raze, J. Pierre, L. Gutmann, and J. Coyette. 1996. Structure of the low-affinity penicillin-binding protein 5 PBP5fm in wild-type and highly penicillin-resistant strains of Enterococcus faecium. J. Bacteriol. 178:4948-4957.