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EnglishBifidobacteria constitute up to 3% of the total microbiota and represent one of the most important health-promoting bacterial groups of the human intestinal microflora. The presence ofBifidobacteriumin the humangastrointestinal tract has been directly related to several health-promoting activities; however, to date, noinformation about the specific mechanisms of interaction with the host is available. In order to provide someinsight into the molecular mechanisms involved in the interaction with the host, we investigated whetherBifidobacteriumwas able to capture human plasminogen on the cell surface. By using flow cytometry, wedemonstrated a dose-dependent human plasminogen-binding activity for four strains belonging to threebifidobacterial species:Bifidobacterium lactis,B. bifidum, andB. longum. The binding of human plasminogen toBifidobacteriumwas dependent on lysine residues of surface protein receptors. By using a proteomic approach,we identified five putative plasminogen-binding proteins in the cell wall fraction of the model strainB. lactisBI07. The data suggest that plasminogen binding toB. lactisis due to the concerted action of a number ofproteins located on the bacterial cell surface, some of which are highly conserved cytoplasmic proteins whichhave other essential cellular functions. Our findings represent a step forward in understanding the mecha-nisms involved in theBifidobacterium-host interaction.
| Titolo: | Binding of human plasminogen to Bifidobacterium |
| Autore/i: | CANDELA, MARCO; Bergmann S.; VICI, MANUELA; VITALI, BEATRICE; TURRONI, SILVIA; Eikmanns B. J.; Hammerschmidt S.; BRIGIDI, PATRIZIA |
| Autore/i Unibo: | |
| Anno: | 2007 |
| Rivista: | |
| Digital Object Identifier (DOI): | http://dx.doi.org/10.1128/JB.00159-07 |
| Abstract: | Bifidobacteria constitute up to 3% of the total microbiota and represent one of the most important health-promoting bacterial groups of the human intestinal microflora. The presence ofBifidobacteriumin the humangastrointestinal tract has been directly related to several health-promoting activities; however, to date, noinformation about the specific mechanisms of interaction with the host is available. In order to provide someinsight into the molecular mechanisms involved in the interaction with the host, we investigated whetherBifidobacteriumwas able to capture human plasminogen on the cell surface. By using flow cytometry, wedemonstrated a dose-dependent human plasminogen-binding activity for four strains belonging to threebifidobacterial species:Bifidobacterium lactis,B. bifidum, andB. longum. The binding of human plasminogen toBifidobacteriumwas dependent on lysine residues of surface protein receptors. By using a proteomic approach,we identified five putative plasminogen-binding proteins in the cell wall fraction of the model strainB. lactisBI07. The data suggest that plasminogen binding toB. lactisis due to the concerted action of a number ofproteins located on the bacterial cell surface, some of which are highly conserved cytoplasmic proteins whichhave other essential cellular functions. Our findings represent a step forward in understanding the mecha-nisms involved in theBifidobacterium-host interaction. |
| Data prodotto definitivo in UGOV: | 2007-10-17 10:50:32 |
| Data stato definitivo: | 2020-02-27T17:54:07Z |
| Appare nelle tipologie: | 1.01 Articolo in rivista |
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