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EnglishThe interaction with the host plasminogen/plasmin system represents a novel component in themolecular cross-talk between bifidobacteria and human host. Here, we demonstrated that theplasminogen-binding bifidobacterial speciesB. longum,B. bifidum,B. breveandB. lactissharethe key glycolytic enzyme enolase as a surface receptor for human plasminogen. Enolase wasvisualized on the cell surface of the model strainB. lactisBI07. The His-tagged recombinantprotein showed a high affinity for human plasminogen, with an equilibrium dissociation constant inthe nanomolar range. By site-directed mutagenesis we demonstrated that the interaction betweentheB. lactisBI07 enolase and human plasminogen involves an internal plasminogen-binding sitehomologous to that of pneumococcal enolase. According to our data, the positively chargedresidues Lys-251 and Lys-255, as well as the negatively charged Glu-252, of theB. lactisBI07enolase are crucial for plasminogen binding. Acting as a human plasminogen receptor, thebifidobacterial surface enolase is suggested to play an important role in the interaction processwith the host.
| Titolo: | Bifidobacterial enolase, a cell surface receptor for human plasminogen involved in the interaction with the host. |
| Autore/i: | CANDELA, MARCO; BIAGI, ELENA; CENTANNI, MANUELA; TURRONI, SILVIA; VICI, MANUELA; MUSIANI, FRANCESCO; VITALI, BEATRICE; Bergmann S.; Hammerschmidt S.; BRIGIDI, PATRIZIA |
| Autore/i Unibo: | |
| Anno: | 2009 |
| Rivista: | |
| Digital Object Identifier (DOI): | http://dx.doi.org/10.1099/mic.0.028795-0 |
| Abstract: | The interaction with the host plasminogen/plasmin system represents a novel component in themolecular cross-talk between bifidobacteria and human host. Here, we demonstrated that theplasminogen-binding bifidobacterial speciesB. longum,B. bifidum,B. breveandB. lactissharethe key glycolytic enzyme enolase as a surface receptor for human plasminogen. Enolase wasvisualized on the cell surface of the model strainB. lactisBI07. The His-tagged recombinantprotein showed a high affinity for human plasminogen, with an equilibrium dissociation constant inthe nanomolar range. By site-directed mutagenesis we demonstrated that the interaction betweentheB. lactisBI07 enolase and human plasminogen involves an internal plasminogen-binding sitehomologous to that of pneumococcal enolase. According to our data, the positively chargedresidues Lys-251 and Lys-255, as well as the negatively charged Glu-252, of theB. lactisBI07enolase are crucial for plasminogen binding. Acting as a human plasminogen receptor, thebifidobacterial surface enolase is suggested to play an important role in the interaction processwith the host. |
| Data prodotto definitivo in UGOV: | 2009-11-24 12:23:47 |
| Data stato definitivo: | 2020-02-27T17:38:19Z |
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