Triggering of pneumococcal autolysis by lysozyme.
Lysozyme had no effect on the rate of multiplication of growing cultures of Streptococcus pneumoniae, but it greatly reduced the lag period that precedes autolysis of these bacteria in stationary phase. Several experiments were done to understand the mechanism of this effect. Lysozyme had no hydrolytic activity on intact cell walls, and cell walls of pneumococci grown with or without lysozyme had identical composition and susceptibility to the pneumococcal autolysin. The acceleration of stationary-phase autolysis by lysozyme involved triggering of the pneumococcal autolytic enzyme since lysozyme had no detectable effect on nonautolysing (LytA-) mutants and heat-inactivated lysozyme completely lacking enzymatic activity was as effective as the nondenatured enzyme in facilitating stationary-phase autolysis. The role of lysozyme in host defense against pneumococcal infection remains elusive.
Cottagnoud
P
P
Laboratory of Microbiology, Rockefeller University, New York, NY 10021.
Tomasz
A
A
D000818:Animals; D001433:Bacteriolysis; D002473:Cell Wall / Q000737:chemistry / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D004305:Dose-Response Relationship, Drug; D006358:Hot Temperature; D066298:In Vitro Techniques; D009113:Muramidase / Q000378:metabolism*; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000502:physiology; D010455:Peptides / Q000032:analysis; D010457:Peptidoglycan / Q000378:metabolism; D011008:Pneumococcal Infections / Q000134:cerebrospinal fluid; D011817:Rabbits; D013296:Streptococcus pneumoniae / Q000378:metabolism*; D013997:Time Factors
D010455:Peptides; D010457:Peptidoglycan; D009113:Muramidase; D009238:N-Acetylmuramoyl-L-alanine Amidase