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Literature summary for 3.5.1.104 extracted from
- Mutations of the Listeria monocytogenes peptidoglycan N-deacetylase and O-acetylase result in enhanced lysozyme sensitivity, bacteriolysis, and hyperinduction of innate immune pathways (2011), Infect. Immun., 79, 3596-3606.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Listeria monocytogenes | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Pgd | - |
Listeria monocytogenes |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | mutants lacking N-acetylglucosamine deacetylase Pgd and mutants in both Pgd and O-acetylmuramic acid transferase are attenuated approximately 2 and 3.5 logs, respectively, in vivo. In bone-marrow derived macrophages, the mutants demonstrate intracellular growth defects and increased induction of cytokine transcriptional responses that emanate from a phagosome and the cytosol. Mutants are lysozyme-sensitive and undergo bacteriolysis in the macrophage cytosol, resulting in AIM2-dependent pyroptosis. Each of the in vitro phenotypes is rescued upon infection of LysM macrophages. The addition of extracellular lysozyme to LysM macrophages restores cytokine induction, host cell death, and Listeria monocytogenes growth inhibition. This suggests that extracellular lysozyme can access the macrophage cytosol and act on intracellular lysozyme-sensitive bacteria | Listeria monocytogenes |
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