Correlation between the Bacterioclastic Action of a Bis-quaternary Ammonium Compound and Outer Membrane Proteins

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Author(s)

    • SUMITOMO TOMOKO
    • Department of Biological Science and Technology, Faculty of Engineering, The University of Tokushima
    • NAGAMUNE HIDEAKI
    • Department of Biological Science and Technology, Faculty of Engineering, The University of Tokushima
    • MAEDA TAKUYA
    • Department of Biological Science and Technology, Faculty of Engineering, The University of Tokushima
    • KOURAI HIROKI
    • Department of Biological Science and Technology, Faculty of Engineering, The University of Tokushima

Abstract

Bis-quaternary ammonium compounds (bis-QACs) have the ability to cause a rapid and abundant leakage of the turbid materials from cells, and such a bacterioclastic ability leads to a potent bactericidal activity. In order to clarify the detailed mechanism of the bactericidal action of bis-QACs, the correlation between the bacterioclastic action of 4, 4'-(1, 6-hexamethylenedithio) bis (1-octylpyridinium bromide) (4DTBP-6, 8) and the leakage of outer membrane pore protein E (OmpE) was investigated. Using the antiserum against a fusion protein consisting of GST and the OmpE protein of <I>Escherichia coil</I> encoded by the ompE gene, it was seen that the leakage of <I>OmpE</I> from <I>E. coil</I> cells was caused by treatment with low concentrations (much lower than the critical vesiculation concentration) of 4DTBP-6, 8. Furthermore, it was confirmed that 4DTBP-6, 8 caused an increase in the turbidity of the cell suspension of <I>Klebsiella pneumoniae, Salmonella typhimurium</I> and <I>Serratia marcescences</I>, and led to the leakage of several proteins which have a high percentage of homology with OmpE of <I>E. coll</I>. By immunoelectron microscopy investigation, it was revealed that the vesiculation from <I>E. coil</I> treated with 4DTBP-6, 8 contains OmpE. In addition, the bacteriolytic action of 4DTBP-6, 8 was investigated. The results suggested that the lysis of cells by bis-QACs was not an enzymatic action such as that by autolysin but a physical bacterioclastic action. Judging from these results, it is suggested that the leakage of OmpE is one of the major bacterioclastic actions of bis-QACs, and deals the bacterial cells a fatal blow.

Journal

  • Biocontrol Sci.  

    Biocontrol Sci. 11(3), 115-124, 2006-09-01 

    The Society for Antibacterial and Antifungal Agents, Japan

References:  23

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Cited by:  2

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Codes

  • NII Article ID (NAID)
    10018251759
  • NII NACSIS-CAT ID (NCID)
    AA11169621
  • Text Lang
    ENG
  • Article Type
    Journal Article
  • ISSN
    13424815
  • Data Source
    CJP  CJPref  J-STAGE 
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