Inhibition of cell division of Escherichia coli by a new synthetic penicillin, piperacillin.

Antimicrobial agents and chemotherapy ·Vol. 14 ·No. 2 ·1978-08-00 ·Pages 257-66

Iida K, Hirata S, Nakamuta S, Koike M

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 mug/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.

MeSH Terms

Bacterial Proteins/metabolism Carrier Proteins/metabolism Cell Division/drug effects Cell Wall/drug effects,metabolism Escherichia coli/cytology,drug effects,metabolism Microscopy, Electron, Scanning Penicillins/metabolism,pharmacology Peptidoglycan Peptidyl Transferases/metabolism

Chemicals

Bacterial Proteins Carrier Proteins Penicillins Peptidoglycan Peptidyl Transferases

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Iida K

Hirata S

Nakamuta S

Koike M

References (26)

26 references, click to expand

Transduction of linked genetic characters of the host by bacteriophage P1.
Virology. 1955 Jul;1(2):190-206 PMID: 13267987
A SIMPLIFIED LEAD CITRATE STAIN FOR USE IN ELECTRON MICROSCOPY.
J Cell Biol. 1965 May;25:407-8 PMID: 14287192
Improvements in epoxy resin embedding methods.
J Biophys Biochem Cytol. 1961 Feb;9:409-14 PMID: 13764136
Protein measurement with the Folin phenol reagent.
J Biol Chem. 1951 Nov;193(1):265-75 PMID: 14907713
Effect of dihydroxymethyl furatrizine on cell division of Escherichia coli.
Microbiol Immunol. 1977;21(9):481-94 PMID: 339039
Temperature-sensitive cell division mutants of Escherichia coli with thermolabile penicillin-binding proteins.
J Bacteriol. 1977 Jul;131(1):293-305 PMID: 326764
Mutants of Escherichia coli which lack a component of penicillin-binding protein 1 are viable.
FEBS Lett. 1977 Jul 15;79(2):374-8 PMID: 330236
Activity of murein hydrolases in synchronized cultures of Escherichia coli.
J Bacteriol. 1977 Mar;129(3):1239-44 PMID: 321419
Properties of the penicillin-binding proteins of Escherichia coli K12,.
Eur J Biochem. 1977 Jan;72(2):341-52 PMID: 319999
In vitro and in vivo antibacterial activity of T-1220, a new semisynthetic penicillin.
Antimicrob Agents Chemother. 1977 Oct;12(4):455-60 PMID: 921239
Interaction of penicillin with the bacterial cell: penicillin-binding proteins and penicillin-sensitive enzymes.
Bacteriol Rev. 1974 Sep;38(3):291-335 PMID: 4608953
The two sites of penicillin action in Escherichia coli.
J Infect Dis. 1973 Dec;128(6):791-4 PMID: 4358124
Purification to homogeneity and properties of two D-alanine carboxypeptidases I From Escherichia coli.
J Biol Chem. 1976 Jan 25;251(2):414-23 PMID: 1391
Septum formation in Escherichia coli: characterization of septal structure and the effects of antibiotics on cell division.
J Bacteriol. 1974 Jul;119(1):303-24 PMID: 4209778
Comparison of the responses of Escherichia coli and proteus mirabilis to seven beta-lactam antibodies.
J Infect Dis. 1973 Aug;128(2):211-22 PMID: 4579140
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):457-63 PMID: 4593965
Mechanism of action and development of resistance to a new amidino penicillin.
J Bacteriol. 1974 Feb;117(2):578-87 PMID: 4590478
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):4162-6 PMID: 674
A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels.
Eur J Biochem. 1974 Jul 1;46(1):83-8 PMID: 4850204
Autolytic enzymes and cell division of Escherichia coli.
J Mol Biol. 1969 May 14;41(3):419-29 PMID: 4896021
Glycopeptide transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive enzymatic reactions.
Proc Natl Acad Sci U S A. 1966 Mar;55(3):656-63 PMID: 5329013
Penicillin-binding proteins and cell shape in E. coli.
Nature. 1975 Apr 10;254(5500):516-7 PMID: 1091862
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 PMID: 1103132
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):1250-60 PMID: 780345
Identification of the major penicillin-binding proteins of Escherichia coli as D-alanine carboxypeptidase IA.
J Bacteriol. 1976 Jul;127(1):660-3 PMID: 776946
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):1133-41 PMID: 5219821

Article Info

Journal

Antimicrobial agents and chemotherapy

Abbr.

Antimicrob Agents Chemother

ISSN

0066-4804

DOI

10.1128/AAC.14.2.257

Published

1978-08-00

Pages

257-66

Language

English

Region

United States

NLM ID

0315061

PMCID

PMC352443

Subset

External Links

PubMed source DOI: 10.1128/AAC.14.2.257 PMC Full Text View journal details

Analysis Services

Inhibition of cell division of Escherichia coli by a new synthetic penicillin, piperacillin.

Contact

WeChat Official Account