JB Accepts, published online ahead of print on 8 June 2007

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J. Bacteriol. doi:10.1128/JB.00159-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Binding of human plasminogen to Bifidobacterium

Marco Candela, Simone Bergmann, Manuela Vici, Beatrice Vitali, Silvia Turroni, Bernhard J. Eikmanns, Sven Hammerschmidt, and Patrizia Brigidi^*

Department of Pharmaceutical Sciences, CIRB-center for Biotechnology, University of Bologna, Via Belmeloro 6, 40126 Bologna, Italy, University of Würzburg, Research Center for Infectious Diseases, Röntgenring 11, D-97070 Würzburg, Germany, Department of Experimental Pathology, Via S. Giacomo 14, 40126 Bologna, Italy, Institute of Microbiology and Biotechnology, University of Ulm, 89069 Ulm, Germany

^* To whom correspondence should be addressed. Email: patrizia.brigidi{at}unibo.it.

Bifidobacteria constitute up to 3% of the total microbiota and represent one of the most important health-promoting bacterial groups of human intestinal microflora. The presence of Bifidobacterium in the human gastrointestinal tract has been directly related with several health-promoting activities, however, up to date, no information about the specific mechanisms of interaction with the host is available. In order to provide some insights into the molecular mechanisms involved in the interaction process with the host, we investigated whether Bifidobacterium was able to capture human plasminogen on the cell surface. By flow cytometry, we demonstrated a dose-dependent human plasminogen-binding activity for four strains belonging to three bifidobacterial species: B. lactis, B. bifidum and B. longum. The binding of human plasminogen to Bifidobacterium was dependent on lysine residues of surface protein receptors. By using a proteomic approach, we identified five putative plasminogen-binding proteins among the cell wall fraction of the model strain B. lactis BI07. These data suggest that plasminogen binding to B. lactis is due to the concerted action of a number of proteins located on the bacterial cell surface, some of them are highly conserved cytoplasmatic proteins which play other essential cellular functions. Our findings represent a step forward in understanding the mechanisms involved in Bifidobacterium-host interaction.

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