Identification of a region of human fibrinogen interacting with staphylococcal clumping factor

Hawiger, Jacek; Timmons, Sheila; Strong, Donna D.; Cottrell, Barbara A.; Riley, Marcia; Doolittle, Russell F.

doi:10.1021/bi00535a047

Cited by 132 publications

(92 citation statements)

References 30 publications

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“…An apparent equilibrium dissociation constant (Kd) of 0.51 k0.19 pM for the interaction of the S. uureus Clf33 with immobilized fibrinogen was determined using this technique. This is in the same range as the Kc, values obtained for the interaction between the S. a w e u s collagen-binding MSCRAMM and its ligand 128, 381, but significantly greater than the Kd determined for the interaction between fibronectin and corresponding recombinant staphylococcal and streptococcal MSCRAMM [28, 381. A K,, of 9.9 nM was previously determined for the binding of soluble fibrinogen to S. u u~e u s Newman cells [22], which seems to differ significantly from the value now determined for the CIfA-ligand interaction. However, it should be kept in mind that Newman expresses several fibrinogen-binding proteins that could bind fibrinogen simultaneously and each fibrinogen molecule is a dimer and has the potential to bind two copies of each bacterial fibrinogen-binding molecule.…”

Section: Discussioncontrasting

confidence: 67%

“…Previous studies of fibrinogen binding to S. aureus cells have focused on the clumping of S. aureus strain Newman cells in solutions of fibrinogen [22,231. By analyzing the binding of soluble 1251-labeled human fibrinogen to Newman cells, it was estimated that 2130 molecules of the protein bound/cell with a dissociation constant (Kd) of 9.9 nM [22].…”

mentioning

confidence: 99%

“…By analyzing the binding of soluble 1251-labeled human fibrinogen to Newman cells, it was estimated that 2130 molecules of the protein bound/cell with a dissociation constant (Kd) of 9.9 nM [22]. In addition, a binding site in fibrinogen for Newman cells was localized to the C-terminus of the y chain [22,231. A 15-amino acid synthetic peptide, corresponding to the C-terminal 15 residues of the y chain, inhibited fibrinogen-dependent clumping of bacteria.…”

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confidence: 99%

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Characterization of the Interaction Between the Staphylococcus Aureus Clumping Factor (ClfA) and Fibrinogen

McDevitt¹,

Nanavaty²,

House-Pompeo³

et al. 1997

European Journal of Biochemistry

201

168

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The ability of Staphylococcus aureus to adhere to adsorbed fibrinogen and fibrin is believed to be an important step in the initiation of bioinaterial and wound-associated infections. In this study, we show that the binding site in fibrinogen for the recently identified S. aureus fibrinogen-binding protein clumping factor (ClfA) is within the C-terminus of the fibrinogen y chain. S. aureus Newman cells expressing ClfA adhered to microtitre wells coated with recombinant fibrinogen purified from BHK cells, but did not adhere to wells coated with a purified recombinant fibrinogen variant where the 4 C-terminal residues of the y chain were replaced by 20 unrelated residues. In addition, a synthetic peptide corresponding to the 17 C-terminal amino acids of the fibrinogen y chain effectively inhibited adherence of ClfA-expressing cells to fibrinogen. In western ligand blots, a recombinant truncated ClfA protein called Clf33 (residues 221 -550) recognized intact recombinant fibrinogen y chains, but failed to recognize recombinant fibrinogen y chains where the 4 C-terminal amino acids were altered by deletion or substitution. Previous studies have shown that the C-terminal domain of fibrinogen y chains contains a binding site for the integrin . We now show that Clf33 inhibits ADPinduced, fibrinogen-dependent platelet aggregation in a concentration-dependent manner and inhibits adhesion of platelets to immobilized fibrinogen under fluid shear stress, indicating that the binding sites for the platelet integrin and the staphylococcal adhesin overlap. The interaction between Clf33 and fibrinogen was further characterized using the BIAcore biosensor. When soluble Clf33 was allowed to bind to immobilized fibrinogen, a Kd of 0.51 t-0.19 pM was experimentally determined using equilibrium binding data. It was also shown that the synthetic C-terminal y-chain peptide effectively inhibited this interaction.

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Section: Discussioncontrasting

confidence: 67%

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confidence: 99%

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confidence: 99%

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Characterization of the Interaction Between the Staphylococcus Aureus Clumping Factor (ClfA) and Fibrinogen

McDevitt¹,

Nanavaty²,

House-Pompeo³

et al. 1997

European Journal of Biochemistry

201

168

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“…Fig. 3 shows that Clf bound to the ␥-chains, as shown before (17,18), whereas Efb bound to the ␣-chain.…”

Section: Comparison Of Binding Characteristics Of Clf and Efb-thementioning

confidence: 55%

Multiple Binding Sites in the Interaction between an Extracellular Fibrinogen-binding Protein from Staphylococcus aureus and Fibrinogen

Palma¹,

Wade²,

Flock³

et al. 1998

Journal of Biological Chemistry

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“…The binding of bacteria to adhesive extracellular matrix proteins such as ®brinogen (Hawiger et al, 1982), ®bronectin (Kuusela, 1978), vitronectin (Chhatawal et al, 1987) and the collagens (Speziale et al, 1986) has emerged as an important mechanism of hosttissue adherence. Few bacterial MSCRAMMS (microbial surface components recognizing adhesive matrix molecules) have been isolated and characterized.…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary X-ray analysis of B-domain fragments of a Staphylococcus aureus collagen-binding protein

Deivanayagam

Rich

Danthuluri

et al. 1999

Acta Crystallogr D Biol Cryst

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Identification of a region of human fibrinogen interacting with staphylococcal clumping factor

Cited by 132 publications

References 30 publications

Characterization of the Interaction Between the Staphylococcus Aureus Clumping Factor (ClfA) and Fibrinogen

Characterization of the Interaction Between the Staphylococcus Aureus Clumping Factor (ClfA) and Fibrinogen

Multiple Binding Sites in the Interaction between an Extracellular Fibrinogen-binding Protein from Staphylococcus aureus and Fibrinogen

Crystallization and preliminary X-ray analysis of B-domain fragments of a Staphylococcus aureus collagen-binding protein

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