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Triggering of pneumococcal autolysis by lysozyme

P Cottagnoud¹, A Tomasz

¹Laboratory of Microbiology, Rockefeller University, New York, NY 10021.

The Journal of Infectious Diseases

|March 1, 1993

Summary

Lysozyme accelerates the autolysis of Streptococcus pneumoniae in stationary phase by triggering its autolytic enzyme, not by degrading cell walls. Its role in host defense against pneumococcal infection requires further investigation.

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Area of Science:

Microbiology
Bacteriology
Enzymology

Background:

Streptococcus pneumoniae is a significant bacterial pathogen.
Bacterial autolysis is a crucial process in the bacterial life cycle and host-pathogen interactions.
Lysozyme is an enzyme with known antimicrobial properties.

Purpose of the Study:

To elucidate the mechanism by which lysozyme affects Streptococcus pneumoniae.
To investigate lysozyme's impact on bacterial multiplication and stationary-phase autolysis.
To determine if lysozyme directly degrades pneumococcal cell walls.

Main Methods:

Culturing Streptococcus pneumoniae with and without lysozyme.
Assessing bacterial multiplication rates.
Analyzing cell wall composition and susceptibility to autolysin.
Testing lysozyme's effect on nonautolysing mutants and heat-inactivated lysozyme.

Main Results:

Lysozyme did not affect the multiplication rate of growing pneumococcal cultures.
Lysozyme significantly reduced the lag period before stationary-phase autolysis.
Lysozyme showed no hydrolytic activity on intact pneumococcal cell walls.
Lysozyme's effect on autolysis was dependent on the presence of the pneumococcal autolytic enzyme (autolysin) and did not require enzymatic activity of lysozyme itself.

Conclusions:

Lysozyme accelerates stationary-phase autolysis in Streptococcus pneumoniae by triggering the bacteria's own autolytic enzyme.
The mechanism involves enzyme activation rather than direct cell wall hydrolysis.
The precise role of lysozyme in host defense against pneumococcal infections remains unclear.

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