Inhibition of mammalian cathepsins by Plesiomonas shigelloides
Language English Country United States Media print
Document type Journal Article
PubMed
17176758
DOI
10.1007/bf02931582
Knihovny.cz E-resources
- MeSH
- Antigens, Bacterial MeSH
- Cysteine Endopeptidases MeSH
- Cysteine Proteinase Inhibitors metabolism pharmacology MeSH
- Cathepsin B antagonists & inhibitors MeSH
- Cathepsin L MeSH
- Cathepsins antagonists & inhibitors MeSH
- Humans MeSH
- Papain antagonists & inhibitors MeSH
- Periplasm metabolism MeSH
- Plesiomonas immunology metabolism pathogenicity MeSH
- Antigen Presentation MeSH
- Mammals MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Antigens, Bacterial MeSH
- CTSL protein, human MeSH Browser
- Cysteine Endopeptidases MeSH
- Cysteine Proteinase Inhibitors MeSH
- Cathepsin B MeSH
- Cathepsin L MeSH
- Cathepsins MeSH
- Papain MeSH
To study molecular mechanisms underlying self-defense of the bacterial pathogen Plesiomonas shigelloides against host inflammatory and immune responses, we evaluated its interactions with mammalian papain-like cathepsins that are essential for host immunity. When grown under anaerobic, but not aerobic, conditions, P. shigelloides was shown to bind and inhibit papain, a model representative of the papain family of cysteine proteinases. This points to mammalian cathepsins as likely physiological targets of a novel cysteine-proteinase inhibitor expressed on bacterial cell surface. Both papain and mammalian cathepsins L and B were inhibited by periplasmic extracts of aerobically and anaerobically grown bacteria, the inhibitory activity being higher in the latter. Inhibition by both intact cells and periplasmic samples was rapid and efficient. The results suggest a possible defensive role of bacterial inhibitors of cathepsins during invasion of a mammalian host. The bacteria thus may modulate host protective responses through inhibiting cathepsins involved in antigen processing and presentation.
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