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Plasminogen-dependent proteolytic activity in Bifidobacterium lactis.
Marco Candela1, Giacomo Miccoli1, Simone Bergmann2,3
1Department of Pharmaceutical Sciences, CIRB-centre for Biotechnology, University of Bologna, Via Belmeloro 6, 40126 Bologna, Italy.
Microbiology (Reading, England)
|August 1, 2008
Summary
Bifidobacterium lactis BI07 binds plasminogen, creating surface plasmin. This activity degrades host substrates, potentially aiding gastrointestinal tract colonization by this beneficial bacteria.
Area of Science:
- Microbiology
- Gastroenterology
- Biochemistry
Background:
- Bifidobacteria are crucial for gut health.
- Recent studies show Bifidobacterium species bind plasminogen.
- The functional role of this interaction is not fully understood.
Purpose of the Study:
- To investigate the plasminogen-dependent proteolytic activity of Bifidobacterium lactis BI07.
- To determine if B. lactis BI07 can degrade host-specific substrates via plasminogen.
Main Methods:
- Investigated plasminogen binding to B. lactis BI07.
- Assessed the conversion of plasminogen to plasmin on the bacterial surface.
- Examined the degradation of extracellular matrix, fibronectin, and fibrinogen by B. lactis BI07.
Main Results:
- B. lactis BI07 recruits plasminogen to its cell surface.
- Host plasminogen activators convert bound plasminogen to plasmin.
- This surface-plasmin effectively degrades host substrates like fibronectin and fibrinogen.
Conclusions:
- B. lactis BI07 possesses surface-associated plasmin activity dependent on host plasminogen.
- This proteolytic capability may facilitate the colonization of the gastrointestinal tract.
- Bifidobacteria can modulate the host plasminogen/plasmin system.
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