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Microbiology 154 (2008), 2457-2462; DOI  10.1099/mic.0.2008/017095-0
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Microbiology 154 (2008), 2457-2462; DOI  10.1099/mic.0.2008/017095-0
© 2008 Society for General Microbiology

Plasminogen-dependent proteolytic activity in Bifidobacterium lactis

Marco Candela1, Giacomo Miccoli1, Simone Bergmann2,3, Silvia Turroni1, Beatrice Vitali1, Sven Hammerschmidt2,3 and Patrizia Brigidi1

1 Department of Pharmaceutical Sciences, CIRB-centre for Biotechnology, University of Bologna, Via Belmeloro 6, 40126 Bologna, Italy
2 University of Würzburg, Research Centre for Infectious Diseases, Röntgenring 11, D-97070 Würzburg, Germany
3 Max von Pettenkofer Institut, Ludwig-Maximilians-Universität München, Pettenkoferstr. 9a, D-80336 München, Germany

Correspondence
Patrizia Brigidi
patrizia.brigidi{at}unibo.it

Bifidobacteria represent one of the most important health-promoting bacterial groups of the intestinal microbiota. The binding of plasminogen to species of Bifidobacterium has been recently reported. To further explore the interaction between bifidobacteria and plasminogen, we investigated the role of Bifidobacterium lactis BI07 plasminogen-dependent proteolytic activity in the degradation of host-specific substrates. Our experimental data demonstrate that the recruitment of plasminogen on the bacterial cell surface and its subsequent conversion into plasmin by host-derived plasminogen activators provide B. lactis BI07 with a surface-associated plasmin activity effective in degradation of physiological substrates such as extracellular matrix, fibronectin and fibrinogen. The ability of bifidobacteria to intervene in the host plasminogen/plasmin system may contribute to facilitating colonization of the host gastrointestinal tract.

Abbreviations: EACA, {epsilon}-aminocaproic acid; ECM, extracellular matrix; Fg, fibrinogen; Fn, fibronectin; GIT, gastrointestinal tract; PA, plasminogen activator; tPA, tissue-type PA; uPA, urokinase; Plg, plasminogen






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