Cell wall degradation of Staphylococcus aureus by lysozyme.
In contrast to former findings lysozyme was able to attack the cell walls of Staphylococcus aureus under acid conditions. However, experiments with 14C-labelled cell walls and ribonuclease indicated that, under these conditions, lysozyme acted less as an muralytic enzyme but more as an activator of pre-existing autolytic wall enzymes. Electron microscopic studies showed that under these acid conditions the cell walls were degraded by a new mechanism (i.e. "attack from the inside"). This attack on the cell wall started asymmetrically within the region of the cross wall and induced the formation of periodically arranged lytic sites between the cytoplasmic membrane and the cell wall proper. Subsequently, a gap between the cell wall and the cytoplasmic membrane resulted and large cell wall segments became detached and suspended in the medium. The sequence of lytic events corresponded to processes known to take place during wall regeneration and wall formation. In the final stage of lysozyme action at pH 5 no cell debris but "stabilized protoplasts" were to be seen without detectable alterations of the primary shape of the cells. At the same time long extended ribbon-like structures appeared outside the bacteria. The origin as well as the chemical nature of this material is discussed. Furthermore, immunological implications are considered.
D002473:Cell Wall / Q000378:metabolism / Q000648:ultrastructure; D006863:Hydrogen-Ion Concentration; D008854:Microscopy, Electron; D009113:Muramidase / Q000378:metabolism*; D012260:Ribonucleases / Q000378:metabolism; D013211:Staphylococcus aureus / Q000378:metabolism / Q000648:ultrastructure*
D012260:Ribonucleases; D009113:Muramidase