Role of fibronectin-binding MSCRAMMs in bacterial adherence and entry into mammalian cells

Joh, Danny; Wann, Elisabeth R.; Kreikemeyer, Bernd; Speziale, Pietro; Höök, Magnus

doi:10.1016/s0945-053x(99)00025-6

Cited by 248 publications

(221 citation statements)

References 135 publications

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“…The ability to bind to fibronectin is a characteristic that has been reported for many pathogens (Joh et al, 1999). As fibronectin plays an important role in diverse normal physiological processes, its targeting appears to be an example of the exploitation of a host cell process in the establishment, maintenance or dissemination of infection (Knodler et al, 2001).…”

Section: Discussionmentioning

confidence: 99%

“…Its composition varies among different organs, but the main components are fibronectin, collagen, elastin, laminin and glycosaminoglycans (Kreis & Vale, 1993). Many of these proteins can potentially serve as surface receptors for bacterial binding to host cells via their adhesins (Joh et al, 1999;SchwarzLinek et al, 2004;Westerlund & Korhonen, 1993). S. suis is able to adhere to fibronectin and different types of collagens (Esgleas et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

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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%

Section: Introductionmentioning

confidence: 99%

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

et al. 2008

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“…By using MSCRAMMs, the bacteria can adhere to damaged areas of the endothelium, or directly to the endothelial cell via the adhesin-receptor mechanism or via bridging ligands (122). The bacteria may then be phagocytized into endothelial cells (102,196) and/or reach the underlining tissue (154).…”

Section: Pathogenesismentioning

confidence: 99%

Molecular Epidemiology of Methicillin-Resistant Staphylococcus aureus in Finland

Salmenlinna¹,

Lyytikäinen

Kotilainen

et al. 2000

European Journal of Clinical Microbiology & Infectious Dise

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“…The binding of pathogenic Streptococcus pyogenes and Staphylococcus aureus to epithelial cells via fibronectin facilitates their entry into cells [15][16][17]. The structural organization of the best characterized fibronectinbinding proteins of streptococci and staphylococci are similar [18]. Proteins from both bacteria are surface proteins that have a signal peptide sequence for secretion, a LPXTG motif for cell wall anchoring, and a fibronectin-binding domain composed of several amino acid repeat sequences.…”

Section: Introductionmentioning

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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Role of fibronectin-binding MSCRAMMs in bacterial adherence and entry into mammalian cells

Cited by 248 publications

References 135 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

Molecular Epidemiology of Methicillin-Resistant Staphylococcus aureus in Finland

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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