A two-domain mechanism for group A streptococcal adherence through protein F to the extracellular matrix.

Ozeri, Vered; Tovi, Aviva; Burstein, Israel; Natanson-Yaron, Shira; Caparon, Michael G.; Yamada, Kenneth M.; Akiyama, S K; Vlodavsky, Israël; Hanski, Emanuel

doi:10.1002/j.1460-2075.1996.tb00435.x

Cited by 101 publications

(181 citation statements)

References 27 publications

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“…The GBD is known to associate with segments of these bacterial proteins (32,33) raising the possibility of competition with collagen for FN binding. Such binding could have significant functional implications for tissue changes induced during bacterial colonization.…”

Section: Discussionmentioning

confidence: 99%

Identification and structural analysis of type I collagen sites in complex with fibronectin fragments

Erat¹,

Slatter

Lowe

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

136

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Collagen and fibronectin are major components of vertebrate extracellular matrices. Their association and distribution control the development and properties of diverse tissues, but thus far no structural information has been available for the complex formed. Here, we report binding of a peptide, derived from the ␣1 chain of type I collagen, to the gelatin-binding domain of human fibronectin and present the crystal structure of this peptide in complex with the 8 -9 FnI domain pair. Both gelatin-binding domain subfragments, 6 FnI 1-2 FnII 7 FnI and 8 -9 FnI, bind the same specific sequence on D-period 4 of collagen I ␣1, adjacent to the MMP-1 cleavage site. 8 -9 FnI also binds the equivalent sequence of the ␣2 chain. The collagen peptide adopts an antiparallel ␤-strand conformation, similar to structures of proteins from pathogenic bacteria bound to FnI domains. Analysis of the type I collagen sequence suggests multiple putative fibronectin-binding sites compatible with our structural model. We demonstrate, by kinetic unfolding experiments, that the triple-helical collagen state is destabilized by 8 -9 FnI. This finding suggests a role for fibronectin in collagen proteolysis and tissue remodeling.collagen destabilization ͉ extracellular matrix ͉ protein structure C ollagen is the most abundant protein in mammals, accounting for Ϸ25% of the body-protein content. It is crucial for effects as diverse as cell differentiation, cell migration, and mechanical properties of tissues. Many human diseases have their origin in mutations that affect interactions of collagen with other extracellular matrix (ECM) molecules and cell receptors (1). Type I collagen fibrils form spontaneously in vitro; in vivo, however, formation requires integrin receptors and fibronectin (FN) (2). FN is a large glycosylated protein composed of multiple copies of 3 classes of domains, FnI, FnII, and FnIII, that forms fibrils in the ECM (3). It plays a role in many important physiological processes, such as embryogenesis, wound healing, hemostasis, and thrombosis (4), and disruption of the FN gene is embryonic lethal in mice (5).The interaction of these 2 proteins has long been demonstrated in vitro by using denatured collagen (gelatin) (6, 7) and isolated collagen type I chains or chain fragments (8, 9). The collagen-binding site on FN has been localized to the 42-kDa gelatin-binding domain (GBD; for an overview of FN and collagen fragments see Fig. 1) (10, 11), and anti-GBD antibodies inhibit collagen organization in fibroblast cultures (12). Similarly, experiments in cultures have identified the collagenase/ MMP-1 (13) cleavage site in type I collagen as important for FN-mediated attachment of fibroblasts to collagen ECM (14). Peptides spanning that region (15) or MMP-1 cleavage at this site (6) inhibit attachment. However, attempts to reconstitute the FN-collagen interaction in vitro by using synthetic peptides failed to find strong, specific, interactions (8,9), and the precise sequence determinants for FN-binding to collagen remained unknown...

show abstract

Section: Discussionmentioning

confidence: 99%

Identification and structural analysis of type I collagen sites in complex with fibronectin fragments

Erat¹,

Slatter

Lowe

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

136

View full text Add to dashboard Cite

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“…1) as well as both the NTD and GBF from Fn (39). Upstream regions with differing boundaries have also been referred to as spacer (43), UFBD (44), or FUD (42).…”

Section: Discussionmentioning

confidence: 99%

“…Upstream regions with differing boundaries have also been referred to as spacer (43), UFBD (44), or FUD (42). It was suggested that UR and FnBRs independently mediate adherence of bacteria to Fn, with UR acting as the high affinity Fn-binding site (39). However, the UR construct, as defined by Ozeri et al (39), contains, according to our definition of FnBRs, an almost complete FnBR (SfbI-1) that would bind to the NTD.…”

Section: Discussionmentioning

confidence: 99%

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High Affinity Streptococcal Binding to Human Fibronectin Requires Specific Recognition of Sequential F1 Modules

Schwarz‐Linek

Pilka

Pickford

et al. 2004

Journal of Biological Chemistry

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Fibronectin (Fn) binding by the Streptococcus pyogenes protein SfbI has been shown to trigger integrindependent internalization of this pathogen by human epithelial and endothelial cells. Here, using nuclear magnetic resonance spectroscopy and isothermal titration calorimetry in a dissection approach, the basis for the specificity and high affinity of the interaction between the N-terminal domain of Fn and SfbI is revealed. Each of the five Fn type 1 modules is directly involved in the interaction and is recognized by short consecutive motifs within the repeat region of SfbI. Crucially, these motifs must be combined in the correct order to form a high affinity ligand for the N-terminal domain of Fn.

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“…Unlabeled 70K, 1 μM, completely blocked formation of linear arrays of FITC-70K, indicating specificity of array formation. FUD, a recombinant piece of protein F1 of S. pyogenes with strong affinity for 70K Ozeri et al, 1996) and a known inhibitor of FN assembly , also blocked linear array formation by FITC-70K. Neither a recombinant piece of FN encompassing repeats III7 through 10 and containing the integrin-binding region of FN, tested at 1μM, nor 1.5mM GRGDSP peptide decreased formation of linear arrays.…”

Section: K Binds To Cells In Linear Arrays In the Absence Of Intact Fnmentioning

confidence: 94%

The N-terminal 70-kDa fragment of fibronectin binds to cell surface fibronectin assembly sites in the absence of intact fibronectin

2006

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Binding of the N-terminal 70-kDa (70K) fragment of fibronectin to fibroblasts blocks assembly of intact fibronectin and is an accurate indicator of the ability of various agents to enhance or inhibit fibronectin assembly. Such binding is widely thought to be to already assembled fibronectin. We evaluated this hypothesis with fibronectin-null mouse fibroblasts plated on laminin-1 in the absence of intact fibronectin. As a proteolytic fragment or recombinant protein, 70K bound fibronectin-null cells specifically in linear arrays that extended outwards from the periphery of spread cells. At early time points, these arrays were similar to those formed by intact fibronectin. 70K arrays formed within 5min following ligand addition at concentrations as low as 5nM, indicating rapid and high affinity binding. Bound 70K was extractable with Triton X-100 or deoxycholate but became insoluble when cross-linked with a membrane-impermeable agent into large SDS-stable complexes. Intact fibronectin, in contrast, became progressively non-extractable in the absence of cross-linking. The detergent-resistant arrays of cross-linked 70K localized to tips of cellular extensions and partially overlapped with α 6 and β 1 integrin subunits at the base of the extensions. α 5 did not localize with 70K arrays, but became progressively co-localized with assemblies of intact fibronectin over time. These results support a model in which the 70-kDa region of fibronectin binds to linearly arrayed cell surface molecules of adherent cells to initiate assembly, display of the arrays is controlled by the integrin that mediates adhesion, and fibronectin-binding integrins promote fibronectinfibronectin interactions during progression of assembly.

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A two-domain mechanism for group A streptococcal adherence through protein F to the extracellular matrix.

Cited by 101 publications

References 27 publications

Identification and structural analysis of type I collagen sites in complex with fibronectin fragments

Identification and structural analysis of type I collagen sites in complex with fibronectin fragments

High Affinity Streptococcal Binding to Human Fibronectin Requires Specific Recognition of Sequential F1 Modules

The N-terminal 70-kDa fragment of fibronectin binds to cell surface fibronectin assembly sites in the absence of intact fibronectin

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