2008
DOI: 10.1099/mic.0.2008/017145-0
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Isolation and characterization of α-enolase, a novel fibronectin-binding protein from Streptococcus suis

Abstract: Streptococcus suis is an important swine pathogen that causes meningitis, endocarditis, arthritis and septicaemia. As a zoonotic agent, S. suis also causes similar diseases in humans. Binding of pathogenic bacteria to extracellular matrix components enhances their adhesion to and invasion of host cells. In the present study we isolated and identified a novel fibronectin-binding protein from S. suis. The native protein (designated SsEno) possessed not only high homology with other bacterial enolases but also en… Show more

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Cited by 145 publications
(118 citation statements)
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“…NhhA is a surface-located multi-functional protein expressed by Neisseria meningitides: NhhA is able to bind human epithelial cells, laminin, and heparin sulfate (47). The M protein virulence determinant of Streptococcus pyogenes is known to mediate binding to a range of extracellular matrix proteins and serum proteins including plasminogen (48), while ␣-enolase, a virulence factor of Streptococcus suis mediates binding to fibronectin, plasminogen and endothelial cells (49). Collectively, our findings suggest that P116 is a multifunctional virulence determinant involved in the M. hyopneumoniae disease process.…”
Section: Discussionmentioning
confidence: 99%
“…NhhA is a surface-located multi-functional protein expressed by Neisseria meningitides: NhhA is able to bind human epithelial cells, laminin, and heparin sulfate (47). The M protein virulence determinant of Streptococcus pyogenes is known to mediate binding to a range of extracellular matrix proteins and serum proteins including plasminogen (48), while ␣-enolase, a virulence factor of Streptococcus suis mediates binding to fibronectin, plasminogen and endothelial cells (49). Collectively, our findings suggest that P116 is a multifunctional virulence determinant involved in the M. hyopneumoniae disease process.…”
Section: Discussionmentioning
confidence: 99%
“…The recombinant protein binds to plasminogen and with high affinity (dissociation constant [K d ] of 21 nM). Furthermore, antibodies to this protein inhibit the adhesion and invasion of S. suis into microvascular endothelial cells (54). The pentose phosphate pathway enzyme, 6-phosphogluconate dehydrogenase, also acts as an adhesin in various pneumococcal strains (47).…”
Section: Bacterial Moonlighting Proteins Which Act As Adhesins and Inmentioning
confidence: 99%
“…To accomplish this, we used enolase antibodies and specific inhibitors, as extensively used in previous studies (18,22,23). Unlike antibodies against a control B. burgdorferi membrane protein, BBA52 (29), antibodies raised against recombinant enolase were able to decrease Pg binding to B. burgdorferi cells (Fig.…”
Section: B Burgdorferi Binds Plasminogen Via Enolasementioning
confidence: 99%
“…Since enolase is one of the well-known Pg-binding proteins detected in many pathogenic organisms (18,27,33,34,37,38), we next assessed whether enolase is involved in B. burgdorferi-Pg interaction. To accomplish this, we used enolase antibodies and specific inhibitors, as extensively used in previous studies (18,22,23).…”
Section: B Burgdorferi Binds Plasminogen Via Enolasementioning
confidence: 99%