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Inhibition of mammalian cathepsins byPlesiomonas shigelloides

To study molecular mechanisms underlying self-defense of the bacterial pathogenPlesiomonas 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 aerobi...

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Bibliographic Details
Published in:Folia microbiologica 2006-09, Vol.51 (5), p.393-400
Main Authors: Pavlova, A., Křováček, K., Čižnár, I., Gonzalez-Rey, C.
Format: Article
Language:English
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Summary:To study molecular mechanisms underlying self-defense of the bacterial pathogenPlesiomonas 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.[PUBLICATION ABSTRACT]
ISSN:0015-5632
1874-9356
DOI:10.1007/BF02931582