Multiple binding of type 3 streptococcal M protein to human fibrinogen, albumin and fibronectin

Schmidt, Karl‐Hermann; Mann, Karlheinz; Cooney, Jakki C.; Köhler, W.

doi:10.1111/j.1574-695x.1993.tb00392.x

Cited by 80 publications

(58 citation statements)

References 38 publications

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“…Both strains bound to immobilized Fn in a cell densitydependent manner, although the affinity of the FbaB Ϫ mutant, TR-47, was lower than that of wild type strain SSI-1. These results clearly show that FbaB functions as an Fn-binding protein on the surface of GAS and suggest that the remaining Fn-binding ability of TR-47 may be ascribed to M3 protein (35).…”

Section: Fig 3 Functional Analysis Of An Fbab-deficient Mutantmentioning

confidence: 63%

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Molecular Characterization of a Novel Fibronectin-binding Protein of Streptococcus pyogenesStrains Isolated from Toxic Shock-like Syndrome Patients

Terao

Kawabata

Nakata

et al. 2002

Journal of Biological Chemistry

108

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Group A Streptococcus pyogenes has surface-located fibronectin (Fn)-binding proteins known to be a major virulence factor, which adheres to and invades host cells. We present a novel Fn-binding protein of group A streptococcus serotype M3 and M18 strains isolated from patients with toxic shock-like syndrome (TSLS). By searching the whole genome sequence of an M3 strain from a TSLS patient, an open reading frame was found among the putative surface proteins. It possessed an LPXTG motif and Fn-binding repeat domains in the Cterminal region and was designated as FbaB (Fn-binding protein of group A streptococci type B). The fbaB gene was found in all M3 and M18 strains examined, although not in other M serotypes. Furthermore, FbaB protein was expressed on the cell surface of TSLS strains but not on non-TSLS ones. Enzyme-linked immunosorbent assay and ligand blotting revealed that recombinant FbaB exhibits a strong Fn-binding ability. An FbaB-deficient mutant strain showed 6-fold lower adhesion and invasion efficiencies to HEp-2 cells than the wild type. Moreover, mortality was decreased in mice infected with the mutant strain in comparison to the wild type. These data suggest that FbaB is etiologically involved in the development of invasive streptococcal diseases.

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Section: Fig 3 Functional Analysis Of An Fbab-deficient Mutantmentioning

confidence: 63%

“…1C). Approximately 80-and 88-kDa proteins were found to bind Fn at a binding capability much stronger than M3 protein, which is also an Fn-binding protein (35). However, the recovery of the 80-and 88-kDa proteins was much less than M protein at 55 kDa (Fig.…”

Section: Screening For Fn-binding Protein In Serotype M3mentioning

confidence: 97%

Molecular Characterization of a Novel Fibronectin-binding Protein of Streptococcus pyogenesStrains Isolated from Toxic Shock-like Syndrome Patients

Terao

Kawabata

Nakata

et al. 2002

Journal of Biological Chemistry

108

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“…These include protein F1, FBP54, and the M3 protein, of Streptococcus pyogenes (41)(42)(43). Protein F1 has a similar structural organization to the Fnbps of S. aureus, including C-terminal Fn-binding repeats that are homologous to the D repeats of the Fnbps (44,45).…”

Section: Discussionmentioning

confidence: 99%

The Fibronectin-binding MSCRAMM FnbpA ofStaphylococcus aureus Is a Bifunctional Protein That Also Binds to Fibrinogen

Wann

Gurusiddappa

Höök

2000

Journal of Biological Chemistry

285

277

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Staphylococcus aureus is an important pathogen capable of causing a wide spectrum of diseases in humans and animals. This bacterium expresses a variety of virulence factors that participate in the process of infection. These include MSCRAMMs (microbial surface components recognizing adhesive matrix molecules) that mediate the adherence of the bacteria to host extracellular matrix components, such as collagen, fibronectin (Fn), and fibrinogen (Fg). Two Fn-binding MSCRAMMs, FnbpA and FnbpB, have been previously identified. The Fn binding activity has been localized to the ϳ40-amino acid residue D repeats in the C-terminal part of these proteins. However, no biological activity has yet been attributed to the N-terminal A regions of these proteins. These regions exhibit substantial amino acid sequence identity to the A regions of other staphylococcal MSCRAMMs, including ClfA, ClfB, and SdrG (Fbe), all of which bind Fg. This raises the question of whether the Fn-binding MSCRAMMs can also bind specifically to Fg. In this report, we show that a recombinant form of the A region of FnbpA does specifically recognize Fg. We localize the binding site in Fg for recombinant FnbpA to the ␥-chain, in particular to the C-terminal residues of this polypeptide, the site also recognized by ClfA. In addition, we demonstrate that recombinant FnbpA can compete with ClfA for binding to both immobilized and soluble Fg. By the use of surface plasmon resonance spectroscopy and fluorescence polarization, we determine the dissociation equilibrium constant for the interaction of recombinant FnbpA with intact immobilized Fg and with a synthetic C-terminal ␥-chain peptide, respectively. Finally, by overexpressing FnbpA in a mutant strain of S. aureus that lacks the expression of both ClfA and ClfB, we show that native FnbpA can mediate the interaction of S. aureus with soluble Fg.

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“…M3 protein, a membrane-anchored streptococcal surface protein (24,25), and HA capsule were identified in this study as the CIV-binding and -aggregating factors of GAS isolated from ARF patients. Cpa, the only collagen-binding protein so far described, binds Bars, 1 µm (a and d), 0.5 µm (b and e), and 0.2 µm (c).…”

Section: Discussionmentioning

confidence: 99%

Rheumatic fever–associated Streptococcus pyogenes isolates aggregate collagen

Dinkla¹,

Rohde²,

Jansen³

et al. 2003

J. Clin. Invest.

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Multiple binding of type 3 streptococcal M protein to human fibrinogen, albumin and fibronectin

Cited by 80 publications

References 38 publications

Molecular Characterization of a Novel Fibronectin-binding Protein of Streptococcus pyogenesStrains Isolated from Toxic Shock-like Syndrome Patients

Molecular Characterization of a Novel Fibronectin-binding Protein of Streptococcus pyogenesStrains Isolated from Toxic Shock-like Syndrome Patients

The Fibronectin-binding MSCRAMM FnbpA ofStaphylococcus aureus Is a Bifunctional Protein That Also Binds to Fibrinogen

Rheumatic fever–associated Streptococcus pyogenes isolates aggregate collagen

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