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.

Bifidobacterial enolase, a cell surface receptor for human plasminogen involved in the interaction with the host.

CANDELA, MARCO;BIAGI, ELENA;CENTANNI, MANUELA;TURRONI, SILVIA;VICI, MANUELA;MUSIANI, FRANCESCO;VITALI, BEATRICE;BRIGIDI, PATRIZIA
2009

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.
MICROBIOLOGY
Candela M.; Biagi E.; Centanni M.; Turroni S.; Vici M.; Musiani F.; Vitali B.; Bergmann S.; Hammerschmidt S.; Brigidi P.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11585/79826
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