Characterization of two putative fibronectin-binding proteins of Clostridium perfringens

Katayama, Seiichi; Nozu, Nanami; Okuda, Masaya; Hirota, Shinsuke; Yamasaki, Tsutomu; Hitsumoto, Yasuo

doi:10.1016/j.anaerobe.2009.03.001

Cited by 17 publications

(16 citation statements)

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“…This was identified in the sequenced C. difficile genome on the basis of similarity to a putative PavA/FBP54-like fibronectin-binding protein annotated in the Bacillus subtilis genome (Hennequin et al, 2003). The C. perfringens genome contains at least two putative FnBP genes of a calculated molecular mass of 25 and 66 kDa, which have been termed fbpA and fbpB (Katayama et al, 2009). The gene was cloned and the protein expressed and found to bind to both soluble and insoluble fibronectin.…”

Section: The Clostridiamentioning

confidence: 99%

“…The gene was termed fbp68 as it encodes a 68-kDa protein, which is 66% identical to S. pyogenes FBP54. Both C. perfringens proteins have been expressed and shown to bind specifically to fibronectin, but with an estimated low affinity (Katayama et al, 2009). The Fbp68 protein is found on the cell surface and can aid in the attachment of bacteria to cells (Hennequin et al, 2003).…”

Section: The Clostridiamentioning

confidence: 99%

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Fibronectin: a multidomain host adhesin targeted by bacterial fibronectin-binding proteins

et al. 2011

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Fibronectin, a large and essential multidomain glycoprotein, with multiple adhesive properties, functioning as a key link between cells and their extracellular matrices, is now recognized to be the target for a large number of bacterial proteins, which are generally considered to function as bacterial adhesins. In the last decade, an avalanche of bacterial fibronectin-binding proteins (FnBPs) has been identified, and the bioinformatics, structural biology, biological function and role in the virulence of a growing number of both Gram-positive and Gram-negative proteins have begun to emerge. The evidence suggests that fibronectin has a wider biological remit than was previously thought and that bacterial FnBPs have actions over and above that of simple adhesion. This article provides an update on our current understanding of FnBPs from both Gram-negative and Gram-positive bacteria and their proposed roles in bacterial colonization, bacterial virulence and bacteria-host interactions.

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Section: The Clostridiamentioning

confidence: 99%

Section: The Clostridiamentioning

confidence: 99%

Fibronectin: a multidomain host adhesin targeted by bacterial fibronectin-binding proteins

et al. 2011

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“…To generate His‐tagged rFbpA and rFbpB proteins the C. perfringens strain 13 genes fbp A and fbp B were first amplified by PCR as described previously (20). The resultant DNA fragments were cloned into the pET16‐b vector (Merck KGaA, Darmstadt, Germany) and transformed into the E. coli BL21‐CodonPlus (DE3) RIL strain.…”

Section: Methodsmentioning

confidence: 99%

“…Indeed, the bacteria Staphylococcus (7-9), Streptococcus (10)(11)(12)(13), Listeria (14)(15)(16), and Clostridium difficile (17) have been shown to have Fbp. C. perfringens is also thought to have Fbps since Fn has been observed to specifically bind to this bacterium (18). Genomic analysis of C. perfringens strain 13 has revealed that this bacterium contains two genes (CPE0703: fbpA and CPE1847: fbpB) that encode putative Fbp (19).…”

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Fibronectin‐binding proteins of Clostridium perfringens recognize the III₁‐C fragment of fibronectin

Yamasaki

Hitsumoto

Katayama

et al. 2010

Microbiology and Immunology

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The Clostridium perfringens strain 13 genome contains two genes (fbpA, fbpB) that encode putative Fbp. Both rFbpA and rFbpB were purified and their reactivity with human serum Fn was analyzed. To determine the region of the Fn molecule recognized by rFbp, a plate binding assay using N‐terminal 70‐kDa peptide, III1‐C peptide, and 110‐kDa peptide containing III2–10 of Fn was performed. Both rFbp bound to the III1‐C peptide of Fn but not to the other peptides. However, the III1‐C fragment of Fn is known to be cryptic in serum Fn. Then, rFbp‐BP from Fn were purified by rFbp‐affinity chromatography. The yield of purified proteins was approximately 1% of the applied Fn on a protein basis. Western blotting analysis of the rFbp‐BP, using four different anti‐Fn monoclonal antibodies, revealed that the rFbp‐BP carried partial Fn antigenicity. Bindings of rFbp to rFbp‐BP were inhibited by the presence of the III1‐C peptide, suggesting that rFbp‐BP express the III1‐C fragment. The binding of Fn to III1‐C was inhibited by the presence of either rFbpA or rFbpB. This result that suggests C. perfringens Fbps may inhibit the formation of Fn‐matrix in vivo.

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The ability of disease and non-disease producing strains of Clostridium perfringens from chickens to adhere to extracellular matrix molecules and Caco-2 cells

Martin

Smyth

2010

Anaerobe

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Characterization of two putative fibronectin-binding proteins of Clostridium perfringens

Cited by 17 publications

References 13 publications

Fibronectin: a multidomain host adhesin targeted by bacterial fibronectin-binding proteins

Fibronectin: a multidomain host adhesin targeted by bacterial fibronectin-binding proteins

Fibronectin‐binding proteins of Clostridium perfringens recognize the III₁‐C fragment of fibronectin

The ability of disease and non-disease producing strains of Clostridium perfringens from chickens to adhere to extracellular matrix molecules and Caco-2 cells

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Characterization of two putative fibronectin-binding proteins of Clostridium perfringens

Cited by 17 publications

References 13 publications

Fibronectin: a multidomain host adhesin targeted by bacterial fibronectin-binding proteins

Fibronectin: a multidomain host adhesin targeted by bacterial fibronectin-binding proteins

Fibronectin‐binding proteins of Clostridium perfringens recognize the III1‐C fragment of fibronectin

The ability of disease and non-disease producing strains of Clostridium perfringens from chickens to adhere to extracellular matrix molecules and Caco-2 cells

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Fibronectin‐binding proteins of Clostridium perfringens recognize the III₁‐C fragment of fibronectin