The molecular basis of fibronectin‐mediated bacterial adherence to host cells

Schwarz‐Linek, Ulrich; Höök, Magnus; Potts, Jennifer R.

doi:10.1111/j.1365-2958.2004.04027.x

Cited by 226 publications

(199 citation statements)

References 77 publications

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“…In the case of S. suis, it has been demonstrated recently that S. suis adhesion to and intracellular invasion of PBMEC increases more than 500 and 700 %, respectively, when bacteria are precoated with fibronectin (Vanier et al, 2007a). Although the mechanisms by which fibronectin-binding proteins trigger the internalization of bacteria by mammalian cells are not completely understood, it has been suggested that binding of fibronectin to a host integrin might initiate a complex cascade of cell signalling that leads to reorganization of cytoskeletal components and consequent internalization of the bacteria (Schwarz-Linek et al, 2004). Accordingly, S. suis invasion of endothelial cells is actin-dependent (Vanier et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterization of α-enolase, a novel fibronectin-binding protein from Streptococcus suis

et al. 2008

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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 enolase activity. We cloned, expressed and purified SsEno and showed that it is ubiquitously expressed by all S. suis serotypes and we identified its surface localization using immunoelectron microscopy. ELISA demonstrated that SsEno binds specifically to fibronectin and plasminogen in a lysine-dependent manner. Additional surface plasmon resonance assays demonstrated that SsEno binds to fibronectin or plasminogen with low nanomolar affinity. Inhibition experiments with anti-SsEno antibodies also showed that bacterial SsEno is important for the adhesion to and invasion of brain microvascular endothelial cells by S. suis. Overall, the present work is the first study, to our knowledge, to demonstrate a fibronectinbinding activity of a bacterial enolase, and shows that, similar to other bacterial fibronectin-binding proteins, SsEno may contribute to the virulence of S. suis. INTRODUCTIONStreptococcus suis is a major swine pathogen that causes septicaemia, meningitis, endocarditis and arthritis (Higgins & Gottschalk, 2005). Of the 35 known serotypes, serotype 2 is the most frequently isolated and associated with disease (Higgins & Gottschalk, 2005). It has been proposed that two serotypes (serotypes 32 and 34) be excluded from S. suis and redesignated Streptococcus orisratti (Hill et al., 2005). S. suis, especially serotype 2, has also been described as an important zoonotic agent that affects people in close contact with infected pigs or pork-derived products (Lun et al., 2007). Indeed, an important number of cases of human disease with a high rate of mortality in China were linked directly to a concurrent outbreak of S. suis infection in pigs (Ye et al., 2006).Little is known about S. suis virulence factors. The capsule polysaccharide (CPS) is a critical virulence factor, given that unencapsulated isogenic mutants are completely avirulent and rapidly cleared from the circulation in pig and mouse infection models (Charland et al., 2000;Smith et al., 1999). However, non-virulent strains are also encapsulated, indicating that the virulence of this pathogen is a multifactorial process . Other potential virulence factors have also been described in S. suis, including a haemolysin (suilysin), a 136 kDa muramidase-released protein (MRP), a 110 kDa extracellular factor (EF) protein, a hyaluronidase, a superoxide dismutase, various proteases, a serum opacity factor and different adhesins (Baums et al., 2006;.The pathogenesis of S. suis infection is not fully understood and likely involves many steps . Binding between b...

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Section: Discussionmentioning

confidence: 99%

Isolation and characterization of α-enolase, a novel fibronectin-binding protein from Streptococcus suis

et al. 2008

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“…This highly conserved segment occurs once in the most C-terminal FnBRs of FnBPs, with the exception of FnBPA and FnBPB from S. aureus and FnZ from Streptococcus equisimilis (7). Potentially, several copies of Fib1 can be bound to the FnBR region of FnBPs (11).…”

Section: Discussionmentioning

confidence: 99%

“…1A) (8 -10). The FnBRs of SfbI are homologous to tandem repeats in FnBPs of other streptococci and Staphylococcus aureus, and new boundaries for FnBRs of both streptococci and staphylococci have recently been suggested based on structural data (7,11). FnBRs are intrinsically disordered and undergo a conformational change on binding to Fn (12)(13)(14).…”

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confidence: 99%

High Affinity Streptococcal Binding to Human Fibronectin Requires Specific Recognition of Sequential F1 Modules

Schwarz‐Linek

Pilka

Pickford

et al. 2004

Journal of Biological Chemistry

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Fibronectin (Fn) binding by the Streptococcus pyogenes protein SfbI has been shown to trigger integrindependent internalization of this pathogen by human epithelial and endothelial cells. Here, using nuclear magnetic resonance spectroscopy and isothermal titration calorimetry in a dissection approach, the basis for the specificity and high affinity of the interaction between the N-terminal domain of Fn and SfbI is revealed. Each of the five Fn type 1 modules is directly involved in the interaction and is recognized by short consecutive motifs within the repeat region of SfbI. Crucially, these motifs must be combined in the correct order to form a high affinity ligand for the N-terminal domain of Fn.

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“…Previous studies have shown that various Gram-positive bacteria express multiple receptors that bind to fibronectin and have a critical role in the infectious process [21]. However, information highlighting what role fibronectin binding by S. mutans plays in the pathogenesis of infective endocarditis is sparse.…”

Section: Discussionmentioning

confidence: 99%

Inactivation of a gene for a fibronectin-binding protein of the oral bacterium Streptococcus mutans partially impairs its adherence to fibronectin

Miller-Torbert

Sharma

Holt

2008

Microbial Pathogenesis

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A sequence of 1,647 base pairs in length of S. mutans DNA that encodes for a 63 kDa protein with significant amino acid similarity with fibronectin-binding proteins of S. pyogenes and S. gordonii was cloned. The putative recombinant fibronectin-binding protein of S. mutans was purified using affinity chromatography and the cloned protein was used to prepare polyclonal antibodies against the recombinant protein. In immunoblot assays, antibodies against the S. pyogenes fibronectinbinding protein, FBP54, were cross-reactive with the S. mutans protein that was designated SmFnB. Additionally, antibodies to the S. mutans SmFnB protein reacted with the S. pyogenes FBP54 protein.The S. mutans SmFnB protein was found to bind to immobilized fibronectin in a concentration dependant manner. A mutant strain of S. mutans M51 that was constructed by alleleic exchange did not express the SmFnB protein. This mutant strain, S. mutans ΔSmFnB, was determined in an ELISA to bind to immobilized fibronectin 30% less when compared to the parental strain S. mutans M51. The results are consistent with the conclusion that the 63 kDa SmFnB protein of S. mutans is a fibronectin-binding protein that may contribute to the interaction of S. mutans with damaged heart tissue during pathogenesis of infective endocarditis. Also, the study suggests that multiple molecules may mediate the interaction of S. mutans with fibronectin.

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The molecular basis of fibronectin‐mediated bacterial adherence to host cells

Cited by 226 publications

References 77 publications

Isolation and characterization of α-enolase, a novel fibronectin-binding protein from Streptococcus suis

Isolation and characterization of α-enolase, a novel fibronectin-binding protein from Streptococcus suis

High Affinity Streptococcal Binding to Human Fibronectin Requires Specific Recognition of Sequential F1 Modules

Inactivation of a gene for a fibronectin-binding protein of the oral bacterium Streptococcus mutans partially impairs its adherence to fibronectin

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