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J. Biol. Chem., Vol. 281, Issue 25, 17246-17252, June 23, 2006

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A Serpin from the Gut Bacterium Bifidobacterium longum Inhibits Eukaryotic Elastase-like Serine Proteases^*

From the Nestlé Research Center, Vers-chez-les-Blanc, P. O. Box 44, CH-1000 Lausanne 26, Switzerland

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 10⁴ M^-1 s^-1 and 2.1 x 10⁴ 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.

Received for publication, February 22, 2006 , and in revised form, April 19, 2006.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence may be addressed: Dept. of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Ave., Boston MA 02140. Tel.: 617-432-3211; Fax: 617-432-4383; E-mail: dmitri_ivanov{at}hms.harvard.edu. ² To whom correspondence may be addressed. Tel.: 41-21-785-83-64; Fax: 41-21-785-85-44; E-mail: fabrizio.arigoni{at}rdls.nestle.com.

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