Lysis and killing of bacteria by lysosomal proteinases.
The bacteriolytic and bactericidal effects of the human proteinases cathepsin B, cathepsin D, cathepsin G, and elastase were investigated. Cathepsin G and elastase were 5 to 10% as active as egg white lysozyme in the lysis of Micrococcus lysodeikticus. All four enzymes slowly lysed the lysozyme-resistant Staphylococcus aureus. The gram-negative Acinetobacter 199A was rendered sensitive to lysozyme by all of the proteinases. Only elastase caused marked proteolysis of the outer membrane, which would permit access by lysozyme to the underlying peptidoglycan. When the surface layer of regularly arranged a protein was removed, however, the outer membrane proteins became susceptible to the other proteinases. Cathepsin G, elastase, and cathepsin D were bactericidal to Acinetobacter 199A. The bactericidal activity of cathepsin D was shown to be dependent on enzymatic activity, unlike that of cathepsin G, which was related to its cationic nature.
D000150:Acinetobacter / Q000276:immunology / Q000648:ultrastructure; D000818:Animals; D001433:Bacteriolysis; D002403:Cathepsins / Q000494:pharmacology*; D002462:Cell Membrane / Q000276:immunology; D008247:Lysosomes / Q000201:enzymology*; D008837:Micrococcus / Q000276:immunology; D009113:Muramidase / Q000494:pharmacology; D010196:Pancreatic Elastase / Q000494:pharmacology*; D010447:Peptide Hydrolases / Q000494:pharmacology; D011817:Rabbits; D013211:Staphylococcus aureus / Q000276:immunology
D009113:Muramidase; D002403:Cathepsins; D010447:Peptide Hydrolases; D010196:Pancreatic Elastase