Localization and characterization of the ligand-binding domain of the fibrinogen-binding protein (FgBP) of Streptococcus equi subsp. equi

Meehan, Mary; Muldowney, Deirdre A.; Watkins, N. J.; Owen, Philip

doi:10.1099/00221287-146-5-1187

Cited by 40 publications

(80 citation statements)

References 37 publications

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“…However, the protein shows little significant sequence similarity to other M(-like) proteins, except for the Fg\IgG-binding DemA protein from Streptococcus dysgalactiae, where some similarities in the A-repeat and C-terminal regions have been noted (Vasi et al, 2000). Maximum ligand binding is not dependent on the presence of the A and\or B repeats, but is critically dependent on residues within the first 19 N-terminal amino acids and also on an extended region of (stabilizing) coiled-coil structure (Meehan et al, 1998(Meehan et al, , 2000a. This contrasts with the situation for M1 and M5 proteins of group A streptococci where the centrally located B repeats appear to be critical for Fg binding (Ringdahl et al, 2000).…”

Section: Abbreviationsmentioning

confidence: 99%

“…The sequence of the corresponding gene (fbp) has been determined and shown to encode a protein of 534 amino acids (58 344 Da), which possesses some structural and sequence similarities to other streptococcal cell wall proteins. Based on experimentation and computer predictions, these have been shown to include a 36-residue signal sequence, a cell wall\membrane anchoring domain and two blocks (A and B) of degenerate repeated sequences (Meehan et al, 1998(Meehan et al, , 2000a. In addition, computer-assisted secondary structure analysis predicts that FgBP, like M proteins, possesses a high proportion (over 60 %) of α-helical coiled-coil (dimer) structure (Meehan et al, 1998).…”

Section: Abbreviationsmentioning

confidence: 99%

“…Bacterial cell envelopes were isolated from stationary-phase S. equi cells, using a method based on French pressure cell lysis, as described previously (Meehan et al, 1998). Native (wild-type) FgBP was purified from mutanolysin extracts of S. equi envelopes using horse Fg affinity chromatography, as previously described by Meehan et al (1998) (Meehan et al, 1998(Meehan et al, , 2000a see Fig. 1a).…”

Section: Isolation Of Bacterial Cell Envelopes and Purification Of Fgbpmentioning

confidence: 99%

“…Fg-affinity blotting using HRP-labelled horse Fg in 2 % (w\v) dried skimmed milk was performed as described previously (Meehan et al, 1998(Meehan et al, , 2000a. For IgG-affinity blotting, nitrocellulose blots were blocked with a solution of 2n5% (w\v) dried skimmed milk followed by incubation, as appropriate, with unlabelled horse IgG-Fab, unlabelled or HRP-labelled horse IgG-Fc, HRPlabelled Fc of human or rabbit origin, or HRP labelled Fab fragments of either human or rabbit origin (2-10 µg ml − ").…”

Section: Isolation Of Bacterial Cell Envelopes and Purification Of Fgbpmentioning

confidence: 99%

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The fibrinogen-binding protein (FgBP) of Streptococcus equi subsp. equi additionally binds IgG and contributes to virulence in a mouse model

et al. 2001

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The major cell-wall-associated protein of the equine pathogen Streptococcus equi subsp. equi is an M-like fibrinogen-binding protein (FgBP) which binds equine fibrinogen (Fg) avidly, through residues located at the extreme Nterminus of the molecule. In this study, it is shown that FgBP additionally binds equine IgG-Fc. When tested against polyclonal IgG from ten other animal species, it was found that FgBP binds human, rabbit, pig and cat IgG, but does not bind mouse, rat, goat, sheep, cow or chicken IgG. Through the use of a panel of recombinant FgBP truncates containing defined deletions of sequence, it was shown that residues in the central regions of FgBP are important in IgG binding. An fbp knockout mutant which does not express FgBP on the cell surface was also constructed. Mutant cells failed to autoaggregate, bound no detectable equine Fg or IgG-Fc, were rapidly killed in horse blood, and showed greatly decreased virulence in a mouse model. Results suggest that FgBP is the major surface structure responsible for binding either Fg or IgG, that the molecule has pronounced antiphagocytic properties, and that it is a likely factor contributing to the virulence of wild-type S. equi subsp. equi.

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Section: Abbreviationsmentioning

confidence: 99%

Section: Abbreviationsmentioning

confidence: 99%

Section: Isolation Of Bacterial Cell Envelopes and Purification Of Fgbpmentioning

confidence: 99%

Section: Isolation Of Bacterial Cell Envelopes and Purification Of Fgbpmentioning

confidence: 99%

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The fibrinogen-binding protein (FgBP) of Streptococcus equi subsp. equi additionally binds IgG and contributes to virulence in a mouse model

et al. 2001

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“…Judging from amino acid sequence homology to several established Fbps, such as FBP54 of S. pyogenes (Meehan et al, 2000), Fbp68 should be able to bind to fibronectin. Therefore, the fibronectin-binding properties of Fbp68 were characterized by far-immuno dot-blotting as well as by binding to fibrinogen, collagen and vitronectin.…”

Section: Binding Of Fbp68 To Fibronectin and Other Extracellular Matrmentioning

confidence: 99%

Identification and characterization of a fibronectin-binding protein from Clostridium difficile

et al. 2003

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A 68 kDa fibronectin-binding protein (Fbp68) from Clostridium difficile displaying significant homology to several established or putative Fbps from other bacteria was identified. The one-copy gene is highly conserved in C. difficile isolates. Fbp68 was expressed in Escherichia coli in fusion with glutathione S-transferase; the fusion protein and the native Fbp68 were purified. Immunoblot analysis and cell fractionation experiments revealed that Fbp68 is present on the surface of the bacteria. Far-immuno dot-blotting demonstrated that Fbp68 was capable of fixing fibronectin. Indirect immunofluorescence and ELISA were employed to demonstrate that C. difficile could bind both soluble and immobilized fibronectin. With competitive adherence inhibition assays it was shown that antibodies raised against Fbp68 partially inhibited attachment of C. difficile to fibronectin and Vero cells. Furthermore, Vero cells could fix purified membrane-immobilized Fbp68. Thus Fbp68 appears to be one of the several adhesins identified to date in C. difficile.

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Antibody and cytokine-associated immune responses to S. equi antigens entrapped in PLA nanospheres

Florindo¹,

Pandit²,

Gonçalves³

et al. 2009

Biomaterials

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Localization and characterization of the ligand-binding domain of the fibrinogen-binding protein (FgBP) of Streptococcus equi subsp. equi

Cited by 40 publications

References 37 publications

The fibrinogen-binding protein (FgBP) of Streptococcus equi subsp. equi additionally binds IgG and contributes to virulence in a mouse model

The fibrinogen-binding protein (FgBP) of Streptococcus equi subsp. equi additionally binds IgG and contributes to virulence in a mouse model

Identification and characterization of a fibronectin-binding protein from Clostridium difficile

Antibody and cytokine-associated immune responses to S. equi antigens entrapped in PLA nanospheres

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