title: Antibacterial mechanisms of lysozyme on Streptococcus mutans.
abstract: Lysozyme is a dominant member of the antibacterial complex of human saliva and has the potential to kill bacteria by direct lysis or by mechanisms (not completely understood) that are independent of its muramidase activity. The muramidase-independent bactericidal activity appears to depend upon its cationic character. Bacterial death may be due to inhibition of nutrient transport (eg. glucose) and disruption of membrane integrity. This review also describes common bactericidal mechanisms of several cationic peptides/proteins to support the cationic-dependent bactericidal model of lysozyme.
authors: Tri-Service General Hospital, Taipei, ROC.
authors: Y B
authors: YB
authors: Wang
mesh_terms: D002412:Cations; D002463:Cell Membrane Permeability / Q000187:drug effects; D006801:Humans; D009113:Muramidase / Q000502:physiology*; D010455:Peptides; D012471:Salivary Proteins and Peptides / Q000502:physiology; D013295:Streptococcus mutans / Q000378:metabolism
chemical_list: D002412:Cations; D010455:Peptides; D012471:Salivary Proteins and Peptides; D009113:Muramidase