A serpin from the gut bacterium Bifidobacterium longum inhibits eukaryotic elastase-like serine proteases
| Autor: | Francis Foata, Celine Emonet, Michael Affolter, Makda Fisseha, Sunil Kochhar, Fabrizio Arigoni, Michelle Delley, Stéphanie Blum-Sperisen, Dmitri N. Ivanov |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Proteases
animal structures Bifidobacterium longum Serine Proteinase Inhibitors Swine Proteolysis medicine.medical_treatment Molecular Sequence Data Biology Serpin Biochemistry Microbiology Feces Mice medicine Escherichia coli Animals Humans Amino Acid Sequence Molecular Biology Pancreatic elastase Serpins Protease medicine.diagnostic_test Pancreatic Elastase Sequence Homology Amino Acid Elastase Cell Biology biology.organism_classification carbohydrates (lipids) Gastrointestinal Tract Kinetics Neutrophil elastase embryonic structures biology.protein Bifidobacterium Leukocyte Elastase |
| Zdroj: | The Journal of biological chemistry. 281(25) |
| ISSN: | 0021-9258 |
| Popis: | Serpins form a large class of protease inhibitors involved in regulation of a wide spectrum of physiological processes. Recently identified prokaryotic members of this protein family may provide a key to the evolutionary origins of the unique serpin fold and the associated inhibitory mechanism. We performed a biochemical characterization of a serpin from Bifidobacterium longum, an anaerobic Gram-positive bacterium that naturally colonizes human gastrointestinal tract. The B. longum serpin was shown to efficiently inhibit eukaryotic elastase-like proteases with a stoichiometry of inhibition close to 1. Porcine pancreatic elastase and human neutrophil elastase were inhibited with the second order association constants of 4.7 x 10(4) m(-1) s(-1) and 2.1 x 10(4) m(-1) s(-1), respectively. The B. longum serpin is expected to be active in the gastrointestinal tract, because incubation of the purified recombinant serpin with mouse feces produces a stable covalent serpin-protease adduct readily detectable by SDS-PAGE. Bifidobacteria may encounter both pancreatic elastase and neutrophil elastase in their natural habitat and protection against exogenous proteolysis may play an important role in the interaction between these commensal bacteria and their host. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|