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. 1979 Nov;16(5):533–539. doi: 10.1128/aac.16.5.533

Affinities of penicillins and cephalosporins for the penicillin-binding proteins of Escherichia coli K-12 and their antibacterial activity.

N A Curtis, D Orr, G W Ross, M G Boulton
PMCID: PMC352901  PMID: 393164

Abstract

The affinities of a range of penicillins and cephalosporins for ther penicillin-binding proteins of Escherichia coli K-12 have been studied, and the results were compared with the antibacterial activity of the compounds against E. coli K-12 and an isogenic permeability mutant. Different penicillins and cephalosporins exhibited different affinities for the "essential" penicillin-binding proteins of E. coli K-12, in a manner which directly correlated with their observed effects upon bacterial morphology. Furthermore, the affinities of the compounds for their "primary" lethal penicillin-binding protein targets showed close agreement with their antibacterial activities against the permeability mutant.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Curtis N. A., Brown C., Boxall M., Boulton M. G. Inhibition of Escherichia coli K-12 by beta-lactam antibiotics with poor antibacterial activity: interaction of permeability and intrinsic activity against penicillin-binding proteins. Antimicrob Agents Chemother. 1979 Mar;15(3):332–336. doi: 10.1128/aac.15.3.332. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. English A. R., Retsema J. A., Girard A. E., Lynch J. E., Barth W. E. CP-45,899, a beta-lactamase inhibitor that extends the antibacterial spectrum of beta-lactams: initial bacteriological characterization. Antimicrob Agents Chemother. 1978 Sep;14(3):414–419. doi: 10.1128/aac.14.3.414. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Iwaya M., Strominger J. L. Simultaneous deletion of D-alanine carboxypeptidase IB-C and penicillin-binding component IV in a mutant of Escherichia coli K12. Proc Natl Acad Sci U S A. 1977 Jul;74(7):2980–2984. doi: 10.1073/pnas.74.7.2980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Matsuhashi M., Takagaki Y., Maruyama I. N., Tamaki S., Nishimura Y., Suzuki H., Ogino U., Hirota Y. Mutants of Escherichia coli lacking in highly penicillin-sensitive D-alanine carboxypeptidase activity. Proc Natl Acad Sci U S A. 1977 Jul;74(7):2976–2979. doi: 10.1073/pnas.74.7.2976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Matsuhashi M., Tamaki S., Curtis S. J., Strominger J. L. Mutational evidence for identity of penicillin-binding protein 5 in Escherichia coli with the major D-alanine carboxypeptidase IA activity. J Bacteriol. 1979 Jan;137(1):644–647. doi: 10.1128/jb.137.1.644-647.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Matsuhashi M., Tamaki S. Enzymatic studies on the mechanism of action of cefoxitin. Correlation between the affinities of cefoxitin to penicillin-binding proteins and its rates of inhibition of the respective penicillin-sensitive reactions in E. coli. J Antibiot (Tokyo) 1978 Dec;31(12):1292–1295. doi: 10.7164/antibiotics.31.1292. [DOI] [PubMed] [Google Scholar]
  7. Nguyen-Distèche M., Pollock J. J., Ghuysen J. M., Puig J., Reynolds P., Perkins H. R., Coyette J., Salton M. R. Sensitivity to ampicillin and cephalothin of enzymes involved in wall peptide crosslinking in Escherichia coli K12, strain 44. Eur J Biochem. 1974 Feb 1;41(3):457–463. doi: 10.1111/j.1432-1033.1974.tb03287.x. [DOI] [PubMed] [Google Scholar]
  8. Nomura H., Fugono T., Hitaka T., Minami I., Azuma T., Morimoto S., Masuda T. Semisynthetic beta-lactam antibiotics. 6. 1 Sulfocephalosporins and their antipseudomonal activities. J Med Chem. 1974 Dec;17(12):1312–1315. doi: 10.1021/jm00258a017. [DOI] [PubMed] [Google Scholar]
  9. Richmond M. H., Clark D. C., Wotton S. Indirect method for assessing the penetration of beta-lactamase-nonsusceptible penicillins and cephalosporins in Escherichia coli strains. Antimicrob Agents Chemother. 1976 Aug;10(2):215–218. doi: 10.1128/aac.10.2.215. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Spratt B. G. Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc Natl Acad Sci U S A. 1975 Aug;72(8):2999–3003. doi: 10.1073/pnas.72.8.2999. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Spratt B. G., Jobanputra V. Mutants of Escherichia coli which lack a component of penicillin-binding protein 1 are viable. FEBS Lett. 1977 Jul 15;79(2):374–378. doi: 10.1016/0014-5793(77)80824-7. [DOI] [PubMed] [Google Scholar]
  12. Spratt B. G., Pardee A. B. Penicillin-binding proteins and cell shape in E. coli. Nature. 1975 Apr 10;254(5500):516–517. doi: 10.1038/254516a0. [DOI] [PubMed] [Google Scholar]
  13. Spratt B. G. Properties of the penicillin-binding proteins of Escherichia coli K12,. Eur J Biochem. 1977 Jan;72(2):341–352. doi: 10.1111/j.1432-1033.1977.tb11258.x. [DOI] [PubMed] [Google Scholar]
  14. Spratt B. G., Strominger J. L. Identification of the major penicillin-binding proteins of Escherichia coli as D-alanine carboxypeptidase IA. J Bacteriol. 1976 Jul;127(1):660–663. doi: 10.1128/jb.127.1.660-663.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Spratt B. G. Temperature-sensitive cell division mutants of Escherichia coli with thermolabile penicillin-binding proteins. J Bacteriol. 1977 Jul;131(1):293–305. doi: 10.1128/jb.131.1.293-305.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Spratt B. G. The mechanism of action of mecillinam. J Antimicrob Chemother. 1977 Jul;3 (Suppl B):13–19. doi: 10.1093/jac/3.suppl_b.13. [DOI] [PubMed] [Google Scholar]
  17. Suzuki H., Nishimura Y., Hirota Y. On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillin-binding proteins. Proc Natl Acad Sci U S A. 1978 Feb;75(2):664–668. doi: 10.1073/pnas.75.2.664. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Tamaki S., Nakajima S., Matsuhashi M. Thermosensitive mutation in Escherichia coli simultaneously causing defects in penicillin-binding protein-1Bs and in enzyme activity for peptidoglycan synthesis in vitro. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5472–5476. doi: 10.1073/pnas.74.12.5472. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Tybring L., Melchior N. H. Mecillinam (FL 1060), a 6beta-amidinopenicillanic acid derivative: bactericidal action and synergy in vitro. Antimicrob Agents Chemother. 1975 Sep;8(3):271–276. doi: 10.1128/aac.8.3.271. [DOI] [PMC free article] [PubMed] [Google Scholar]

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