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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 135 (1983), S. 120-124 
    ISSN: 1432-072X
    Keywords: Staphylococcus aureus ; Chloramphenicoltreatment ; Cell wall ; Wall degradation ; Lysozyme ; Autolysins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The effectiveness of host defence against staphylococcal infections depends on the capability of phagocytes to degrade the bacterial cell walls. Treatment with bacteriostatic agents like chloramphenicol could cause problems since under these drugs staphylococcal walls will be substantially thickened. This study presents evidence that the additional wall material built in the presence of chloramphenicol could moreover be rendered more resistant to lysosomal enzymes: In vitro at pH 5.6, lysozyme from hen egg-white proved to degrade the chloramhenicol-wall material at a velocity reduced to 20% of that of the normal wall. Thus, during the degradation of chloramphenicol-treated staphylococcal cell walls the phagocytes have to deal not only with a quantitative but also with a qualitative problem. Possible reasons for the reduced degradability as to chloramphenicol-induced alterations of the wall composition as well as to activating effects of lysozyme on cell wall autolysins are discussed in view of microbiological and medical implications.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-072X
    Keywords: staphylococci ; Cell wall organization ; Cytoplasmic membrane organization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract By disintegration of the cell wall of staphylococci a definite interlayer located between the cytoplasmic membrane and the cell wall proper could be demonstrated for the first time (=MW-interlayer). This MW-interlayer contains a sort of “cloddy” material in which clusters of embedded ring-like disks are hexagonally arranged in a crystal-like manner. The ring-like disks, approximately 40 Å in diameter and with center-to-center spacings of approximately 75 Å, lie in direct contact either with a rhombically arranged fibrillar network of the outer parts of the cytoplasmic membrane or they themselves are part of (or interconnected by) such an apparently rhombical network. The crystal-like arranged ring-like disks of the interlayer between the cytoplasmic membrane and the cell wall shall be called MW-particles in order to differentiate them from intramembrane particles and particles on the outer surface of the cell wall. At present, nothing more than speculation on the function of the MW-particles located within the space where final processes of the cell wall polymerization are taking place is possible.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-072X
    Keywords: Bacteriolysis ; Staphylococci ; Penicillin ; Cell wall ; Autolysins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In contrast to what has been postulated, penicillin G at its optimal lytic concentration of 0.1 μg per ml did not lead to a detectable activation of autolytic wall processes in staphylococci in terms of the release of uniformly labelled wall fragments from cells pretreated with the drug for 1 h. Rather a considerable inhibition of this release was observed. A similarly profound inhibition of the release of peptidoglycan fragments occurred when staphylococci pretreated for 1 h with 0.1 μg penicillin per ml acted as a source of crude autolysins on peptidoglycan isolated from labelled normal cells of the same strain. This clearly demonstrated that the overall inhibition of autolytic wall processes caused by penicillin was mainly due to a decreased total autolysin action rather than to an altered wall structure. Furthermore, no substantial penicillin-induced inhibition of the incorporation of 14C-N-acetylglucosamine into the staphylococcal wall could be observed before bacteriolysis started, i. e., approximately during the first 80 min of penicillin action. These results are not consistent with any of the models hitherto proposed for the action of penicillin.
    Type of Medium: Electronic Resource
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