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. 1978 Aug;14(2):257–266. doi: 10.1128/aac.14.2.257

Inhibition of Cell Division of Escherichia coli by a New Synthetic Penicillin, Piperacillin

Kyoko Iida 1, Seiichi Hirata 2, Seiichi Nakamuta 3, Masaatsu Koike 1
PMCID: PMC352443  PMID: 358919

Abstract

The mechanism of the action of piperacillin against Escherichia coli was investigated. This drug converted cells to filaments, but did not show lytic action in a range of concentrations below 25 μg/ml. In some of the filaments, stretched constrictions with various diameters were observed. Addition of piperacillin to a synchronous culture inhibited cell division immediately at any stage of the cell cycle. The results of morphological examination of synchronous cultures show that the percentage of filaments with a stretched constriction corresponds to that of normally septated cells before addition of the drug. Furthermore, peptidoglycan synthesis and cross-linking were not inhibited by this drug. It is likely that this drug inhibits only septum formation, but not the growth of wall, and that stretched constrictions are a result of longitudinal growth of septation caused by the drug. Examination of affinity of the drug to penicillin-binding proteins shows that protein 3 is the most sensitive, proteins 2 and 7 are moderately so, and protein 1 is sensitive only to high concentrations of the drug.

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Selected References

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  1. Beck B. D., Park J. T. Activity of three murein hydrolases during the cell division cycle of Escherichia coli K-12 as measured in toluene-treated cells. J Bacteriol. 1976 Jun;126(3):1250–1260. doi: 10.1128/jb.126.3.1250-1260.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Blumberg P. M., Strominger J. L. Interaction of penicillin with the bacterial cell: penicillin-binding proteins and penicillin-sensitive enzymes. Bacteriol Rev. 1974 Sep;38(3):291–335. doi: 10.1128/br.38.3.291-335.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bonner W. M., Laskey R. A. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974 Jul 1;46(1):83–88. doi: 10.1111/j.1432-1033.1974.tb03599.x. [DOI] [PubMed] [Google Scholar]
  4. Burdett I. D., Murray R. G. Septum formation in Escherichia coli: characterization of septal structure and the effects of antibiotics on cell division. J Bacteriol. 1974 Jul;119(1):303–324. doi: 10.1128/jb.119.1.303-324.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Greenwood D., O'Grady F. Comparison of the responses of Escherichia coli and proteus mirabilis to seven beta-lactam antibodies. J Infect Dis. 1973 Aug;128(2):211–222. doi: 10.1093/infdis/128.2.211. [DOI] [PubMed] [Google Scholar]
  6. Greenwood D., O'Grady F. The two sites of penicillin action in Escherichia coli. J Infect Dis. 1973 Dec;128(6):791–794. doi: 10.1093/infdis/128.6.791. [DOI] [PubMed] [Google Scholar]
  7. Hakenbeck R., Messer W. Activity of murein hydrolases in synchronized cultures of Escherichia coli. J Bacteriol. 1977 Mar;129(3):1239–1244. doi: 10.1128/jb.129.3.1239-1244.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Iida K., Koike M. Effect of dihydroxymethyl furatrizine on cell division of Escherichia coli. Microbiol Immunol. 1977;21(9):481–494. doi: 10.1111/j.1348-0421.1977.tb00314.x. [DOI] [PubMed] [Google Scholar]
  9. Izaki K., Matsuhashi M., Strominger J. L. Glycopeptide transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive enzymatic reactions. Proc Natl Acad Sci U S A. 1966 Mar;55(3):656–663. doi: 10.1073/pnas.55.3.656. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. LENNOX E. S. Transduction of linked genetic characters of the host by bacteriophage P1. Virology. 1955 Jul;1(2):190–206. doi: 10.1016/0042-6822(55)90016-7. [DOI] [PubMed] [Google Scholar]
  11. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  12. LUFT J. H. Improvements in epoxy resin embedding methods. J Biophys Biochem Cytol. 1961 Feb;9:409–414. doi: 10.1083/jcb.9.2.409. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Matsuhashi S., Kamiryo T., Blumberg P. M., Linnett P., Willoughby E., Strominger J. L. Mechanism of action and development of resistance to a new amidino penicillin. J Bacteriol. 1974 Feb;117(2):578–587. doi: 10.1128/jb.117.2.578-587.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. 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]
  15. Schwarz U., Asmus A., Frank H. Autolytic enzymes and cell division of Escherichia coli. J Mol Biol. 1969 May 14;41(3):419–429. doi: 10.1016/0022-2836(69)90285-x. [DOI] [PubMed] [Google Scholar]
  16. 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]
  17. 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]
  18. 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]
  19. 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]
  20. 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]
  21. 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]
  22. Tamura T., Imae Y., Strominger J. L. Purification to homogeneity and properties of two D-alanine carboxypeptidases I From Escherichia coli. J Biol Chem. 1976 Jan 25;251(2):414–423. [PubMed] [Google Scholar]
  23. Tipper D. J., Strominger J. L. Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Proc Natl Acad Sci U S A. 1965 Oct;54(4):1133–1141. doi: 10.1073/pnas.54.4.1133. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Tomasz A., Waks S. Mechanism of action of penicillin: triggering of the pneumococcal autolytic enzyme by inhibitors of cell wall synthesis. Proc Natl Acad Sci U S A. 1975 Oct;72(10):4162–4166. doi: 10.1073/pnas.72.10.4162. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Ueo K., Fukuoka Y., Hayashi T., Yasuda T., Taki H., Tai M., Watanabe Y., Saikawa I., Mitsuhashi S. In vitro and in vivo antibacterial activity of T-1220, a new semisynthetic penicillin. Antimicrob Agents Chemother. 1977 Oct;12(4):455–460. doi: 10.1128/aac.12.4.455. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. VENABLE J. H., COGGESHALL R. A SIMPLIFIED LEAD CITRATE STAIN FOR USE IN ELECTRON MICROSCOPY. J Cell Biol. 1965 May;25:407–408. doi: 10.1083/jcb.25.2.407. [DOI] [PMC free article] [PubMed] [Google Scholar]

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