Penicillin-binding Proteins and the Future of -Lactam Antibiotics: The Seventh Fleming Lecture Free

Preview this article:

There is no abstract available.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-129-5-1247
1983-05-01
2024-03-28
Loading full text...

Full text loading...

/deliver/fulltext/micro/129/5/mic-129-5-1247.html?itemId=/content/journal/micro/10.1099/00221287-129-5-1247&mimeType=html&fmt=ahah

References

  1. Amanuma H., Strominger J. L. 1980; Purification and properties of penicillin-binding proteins 5 and 6 from Escherichia coli membranes. Journal of Biological Chemistry 255:11173–11180
    [Google Scholar]
  2. Ambler R. P. 1980; The structure of β-lactamases. Philosophical Transactions of the Royal Society B289:321–331
    [Google Scholar]
  3. Barbour A. G. 1981; Properties of the penicillinbinding proteins in Neisseria gonorrhoeae. Antimicrobial Agents and Chemotherapy 19:316–322
    [Google Scholar]
  4. Blumberg P. M., Strominger J. L. 1974; Interaction of penicillin with the bacterial cell : penicillinbinding proteins and penicillin-sensitive enzymes. Bacteriological Reviews 38:291–335
    [Google Scholar]
  5. Broome-Smith J. K., Spratt B. G. 1982; Deletion of the penicillin-binding protein 6 gene of Escherichia coli. Journal of Bacteriology 152:904–906
    [Google Scholar]
  6. Brown D. F. J., Reynolds P. E. 1980; Intrinsic resistance to β-lactam antibiotics in Staphylococcus aureus. FEBS Letters 122:275–278
    [Google Scholar]
  7. Curtis N. A. C., Orr D., Ross G. W., Boulton M. G. 1979; Affinities of penicillins and cephalosporins for the penicillin-binding proteins of Escherichia coli K12 and their antibacterial activity. Antimicrobial Agents and Chemotherapy 16:533–539
    [Google Scholar]
  8. Delucia M. L., Kelly J. A., Mangion M. M., Moews P. C., Knox J. R. 1980; Tertiary and secondary structure analysis of penicillin-binding proteins. Philosophical Transactions of the Royal Society B289:361–376
    [Google Scholar]
  9. Demerec M. 1945; Production of Staphylococcus strains resistant to various concentrations of penicillin. Proceedings of the National Academy of Sciences of the United States of America 31:16–24
    [Google Scholar]
  10. De Pedro M., Schwarz U. 1981; Heterogeneity of newly inserted and preexisting murein in the sac-culus of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America 78:5856–5860
    [Google Scholar]
  11. De Pedro M. A., Schwarz U., Nishimura Y., Hirota Y. 1980; On the biological role of penicillin-binding proteins 4 and 5. FEMS Microbiology Letters 9:219–221
    [Google Scholar]
  12. Dougherty T. J., Koller A. E., Tomasz A. 1980; Penicillin-binding proteins of penicillin-susceptible and intrinsically resistant Neisseria gonorrhoeae. Antimicrobial Agents and Chemotherapy 18:730–737
    [Google Scholar]
  13. Frére J.-M., Duez C., Ghuysen J.-M., Vande-Kerckhove J. 1976; Occurrence of a serine residue in the penicillin-binding site of the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61. FEBS Letters 70:257–260
    [Google Scholar]
  14. Ghuysen J.-M, Frére J.-M., Leyh-Bouille M., Perkins H. R., Nieto M. 1980; The active centres in penicillin-sensitive enzymes. Philosophical Transactions of the Royal Society B289:285–301
    [Google Scholar]
  15. Godfrey A. J., Bryan L. E., Rabin H. R. 1981; β-Lactam resistant Pseudomonas aeruginosa with modified penicillin-binding proteins emerging during cystic fibrosis treatment. Antimicrobial Agents and Chemotherapy 19:705–711
    [Google Scholar]
  16. Hayes M. V., Curtis N. A. C., Wyke A. W., Ward J. B. 1981; Decreased affinity of a penicillin-binding protein for β-lactam antibiotics in a clinical isolate of Staphylococcus aureus resistant to methicillin. FEMS Microbiology Letters 10:119–122
    [Google Scholar]
  17. Ishino F., Matsuhashi M. 1981; Peptidoglycan synthetic enzyme activities of highly purified penicillin-binding protein 3 in Escherichia coli: a septumforming reaction sequence. Biochemical and Biophysical Research Communications 101:905–911
    [Google Scholar]
  18. Ishino F., Mitsui S., Tamaki S., Matsuhashi M. 1980; Duel enzyme activities of cell wall peptidoglycan synthesis, peptidoglycan transglycosylase and penicillin-sensitive transpeptidase, in purified preparations of Escherichia coli penicillin-binding protein 1A. Biochemical and Biophysical Research Communications 97:287–293
    [Google Scholar]
  19. Ishino F., Tamaki S., Spratt B. G., Matsuhashi M. 1982; A mecillinam-sensitive peptidoglycan crosslinking reaction in Escherichia coli. Biochemical and Biophysical Research Communications 109:689–696
    [Google Scholar]
  20. Izaki K., Matsuhashi M., Strominger J. F. 1966; Glycopeptide transpeptidase and d-alanine carboxypeptidase: penicillin-sensitive enzymatic reactions. Proceedings of the National Academy of Sciences of the United States of America 55:656–663
    [Google Scholar]
  21. Jaurin B., Grundstrom T. 1981; ampC cephalo-sporinase of Escherichia coli K12 has a different evolutionary origin from that of β-lactamases of the penicillinase type. Proceedings of the National Academy of Sciences of the United Staled of America 78:4897–4901
    [Google Scholar]
  22. Kelly J. A., Moews P. C., Knox J. R., Frère J.-M., Ghuysen J.-M. 1982; Penicillin target enzyme and the antibiotic binding site. Science 218:479–481
    [Google Scholar]
  23. Knott-Hunziker V., Waley S. G., Orlek B. S., Sammes P. G. 1979; Penicillinase active sites: labelling of serine-44 in β-lactamase I by β-bromo-penicillanic acid. FEBS Letters 99:59–61
    [Google Scholar]
  24. Markiewicz Z., Broome-Smith J. K., Schwarz U., Spratt B. G. 1982; Spherical E. coli due to elevated levels of d-alanine carboxypeptidase. Nature; London: 297:702–704
    [Google Scholar]
  25. Maruyama I. N., Nakamura M., Soma M., Nishimura Y., Hirota Y. 1982; Entire nucleotide sequence of Escherichia coli structural gene coding for penicillin-binding protein 3. Abstracts of EMBO Meeting on β-lactam Antibiotics,El Escorial p. 21:
    [Google Scholar]
  26. Matsuhashi M., Nakagawa J., Tomioka S., Ishino F., Tamaki S. 1982; Mechanism of peptidoglycan synthesis by penicillin-binding proteins in bacteria and effects of antibiotics. In Drug Resistance in Bacteria Genetics, Biochemistry and Molecular Biology pp. 297–310 Mitsuhashi S. Edited by Tokyo: Japan Scientific Societies Press;
    [Google Scholar]
  27. Moews P. C., Knox J. R., Waxman D. J., Strominger J. F. 1981; Secondary structure relations between beta-lactamases and penicillinsensitive d-alanine carboxypeptidases. International Journal of Peptide and Protein Research 17:211–218
    [Google Scholar]
  28. Nakagawa J., Tamaka S., Matsuhashi M. 1979; Purified penicillin binding proteins IBs from Escherichia coli membrane showing activities of both peptidoglycan polymerase and peptidoglycan crosslinking enzyme. Agricultural and Biological Chemistry 43:1379–1380
    [Google Scholar]
  29. Pratt J. M., Holland 1.B., Spratt B. G. 1981; Precursor forms of penicillin-binding proteins 5 and 6 of E. coli cytoplasmic membrane. Nature; London: 293307–309
    [Google Scholar]
  30. Spratt B. G. 1975; Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America 72:2999–3003
    [Google Scholar]
  31. Spratt B. G. 1977a; Properties of the penicillinbinding proteins of Escherichia coli Kl2. European Journal of Biochemistry 72:341–352
    [Google Scholar]
  32. Spratt B. G. 1977b; Penicillin-binding proteins of Escherichia coli: general properties and character-ization of mutants. In Microbiology 1977 pp. 182–190 Schlessinger D. Edited by Washington: American Society for Microbiology;
    [Google Scholar]
  33. Spratt B. G. 1977C; Temperature-sensitive cell division mutants of Escherichia coli with thermolabile penicillin-binding proteins. Journal of Bacteriology 131:293–305
    [Google Scholar]
  34. Spratt B. G. 1978; Escherichia coli resistance to β-lactam antibiotics through a decrease in the affinity of a target for lethality. Nature; London: 274713–715
    [Google Scholar]
  35. Spratt B. G. 1979; Identification of the killing targets for /Mactam antibiotics in Escherichia coli. In Microbial Drug Resistance pp. 349–360 Mitsuhashi S. Edited by Tokyo: University of Tokyo Press;
    [Google Scholar]
  36. Spratt B. G. 1980a; Biochemical and genetical approaches to the mechanism of action of penicillin. Philosophical Transactions of the Royal Society B289:273–283
    [Google Scholar]
  37. Spratt B. G. 1980b; Deletion of the penicillinbinding protein 5 gene of Escherichia coli. Journal of Bacteriology 14:1190–1192
    [Google Scholar]
  38. Spratt B. G., Pardee A. B. 1975; Penicillin-binding proteins and cell shape in E. coli. Nature; London: 254516–517
    [Google Scholar]
  39. Spratt B. G., Strominger J. F. 1976; Identification of the major penicillin-binding proteins of Escherichia coli as d-alanine carboxypeptidase IA. Journal of Bacteriology 127:660–663
    [Google Scholar]
  40. Spratt B. G., Jobanputra J., Schwarz U. 1977; Mutants of Escherichia coli which lack a component of penicillin-binding protein 1 are viable. FEBS Letters 79:374–378
    [Google Scholar]
  41. Spratt B. G., Boyd A., Stoker N. G. 1980; Defective and plaque-forming lambda transducing bacteriophage carrying penicillin-binding protein-cell shape genes: genetic and physical mapping and identification of the gene products from the lip-dacA-rodA-pbpA-leuS region of the Escherichia coli chromosome. Journal of Bacteriology 143:569–581
    [Google Scholar]
  42. Suzuki H., Nishimura Y., Hirota Y. 1978; On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillinbinding proteins. Proceedings of the National Academy of Sciences of the United States of America 75:664–668
    [Google Scholar]
  43. Suzuki H., Van Heijenoort Y., Tamura T., Mizoguchi J., Hirota Y., Van Heijenoort J. 1980; In vitro peptidoglycan polymerization catalysed by penicillin binding protein IB of Escherichia coli K12. FEBS Letters 110:245–249
    [Google Scholar]
  44. Takeda Y., Nishimura A., Nishimura Y., Yamada M., Yasuda S., Suzuki H., Hirota Y. 1981; Synthetic ColEl plasmids carrying genes for penicillin-binding proteins in Escherichia coli. Plasmid 6:86–98
    [Google Scholar]
  45. Taku A., Stuckey M., Fan D. P. 1982; Purification of the peptidoglycan transglycosylate of Bacillus megaterium. Journal of Biological Chemistry 257:5018–5022
    [Google Scholar]
  46. Tamaki S., Nakajima S., Matsuhashi M. 1977; Thermosensitive mutation in Escherichia coli simul-taneously causing defects in penicillin-binding protein IBs and in enzyme activity for peptidoglycan synthesis in vitro. Proceedings of the National Academy of Sciences of the United States of America 74:5472–5476
    [Google Scholar]
  47. Tamura T., Imae Y., Strominger J. L. 1976; Purification to homogeneity and properties of two D-alanine carboxypeptidases I from Escherichia coli. Journal of Biological Chemistry 251:414–423
    [Google Scholar]
  48. Tipper D. J., Strominger J. L. 1965; Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-d-alanyl-d-alanine. Proceedings of the National Academy of Sciences of the United States of America 54:1133–1141
    [Google Scholar]
  49. Tomasz A. 1980; On the mechanism of the irreversible antimicrobial effects of β-lactams. Philosophical Transactions of the Royal Society B289:303–308
    [Google Scholar]
  50. Waxman D. J., Strominger J. L. 1979; Cleavage of a COOH-terminal hydrophobic region from D-alanine carboxypeptidase, a penicillin-sensitive bacterial membrane enzyme. Journal of Biological Chemistry 254:4863–4875
    [Google Scholar]
  51. Waxman D. J., Strominger J. L. 1980; Sequence of active site peptides from the penicillin-sensitive D-alanine carboxypeptidase of Bacillus subtilis. Journal of Biological Chemistry 255:3964–3976
    [Google Scholar]
  52. Waxman D. J., Amanuma H., Strominger J. L. 1982; Amino acid sequence homologies between Escherichia coli penicillin-binding protein 5 and class A β-lactamases. FEBS Letters 139:159–163
    [Google Scholar]
  53. Wyke A. W., Ward J. B., Hayes M. V., Curtis N. A. C. 1981; A role in vivo for penicillin-binding protein 4 of Staphylococcus aureus. European Journal of Biochemistry 119:389–393
    [Google Scholar]
  54. Zighelboim S., Tomasz A. 1980; Penicillin-binding proteins of multiply antibiotic-resistant South African strains of Streptococcus pneumoniae. Antimicrobial Agents and Chemotherapy 17:434–442
    [Google Scholar]
  55. Zimmermann W. 1980; Penetration of β-lactam antibiotics into their target enzymes in Pseudomonas aeruginosa : comparison of a highly sensitive mutant with its parent strain. Antimicrobial Agents and Chemotherapy 18:94–100
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-129-5-1247
Loading
/content/journal/micro/10.1099/00221287-129-5-1247
Loading

Data & Media loading...

Most cited Most Cited RSS feed