Fibronectin structure and assembly

Potts, Jennifer R.; Campbell, Iain D.

doi:10.1016/0955-0674(94)90090-6

Cited by 205 publications

(172 citation statements)

References 61 publications

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“…On the host cell, the ®bronectin-binding integrin, a 5 b 1 , a cellular adhesion receptor, functions as a phagocytic receptor. The major binding site for S. aureus has been localized to the N-terminal fragment of ®bronectin (Potts and Campbell, 1994), whereas the RGD motif, which is important for the binding of integrins such as integrin a 5 b 1 , is found on a central part of the molecule (Potts and Campbell, 1994). Fibronectin is thus able to act as a bridging molecule by simultaneously binding the bacterial and the mammalian receptors (Fig.…”

Section: Discussionmentioning

confidence: 99%

Fibronectin-binding protein acts as Staphylococcus aureus invasin via fibronectin bridging to integrin alpha5beta1

Sinha¹,

François²,

Nüße³

et al. 1999

Cell Microbiol

507

563

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SummaryThe ability of Staphylococcus aureus to invade mammalian cells may explain its capacity to colonize mucosa and to persist in tissues after bacteraemia. To date, the underlying molecular mechanisms of cellular invasion by S. aureus are unknown, despite its high prevalence and dif®culties in treatment. Here, we show cellular invasion as a novel function for an S. aureus adhesin, previously implicated solely in attachment. S. aureus, but not S. epidermidis, invaded epithelial 293 cells in a temperature-and F-actindependent manner. Formaldehyde-®xed and live bacteria were equally invasive, suggesting that no active bacterial process was involved. All clinical S. aureus isolates analysed, but only a subset of laboratory strains, were invasive. Fibronectin-binding proteins (FnBPs) acted as S. aureus invasins, because: (i) FnBP deletion mutants of invasive laboratory strains lost invasiveness; (ii) expression of FnBPs in noninvasive strains conferred invasiveness; and (iii) the soluble isolated ®bronectin-binding domain of FnBP (D1±D4) completely blocked invasion. Integrin a 5 b 1 served as host cell receptor, which interacted with staphylococcal FnBPs through cellular or soluble ®bronectin. FnBP-de®cient mutants lost invasiveness for epithelial cells, endothelial cells and ®broblasts. Thus, ®bronectin-dependent bridging between S. aureus FnBPs and host cell integrin a 5 b 1 is a conserved mechanism for S. aureus invasion of human cells. This may prove useful in developing new therapeutic and vaccine strategies for S. aureus infections.

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Section: Discussionmentioning

confidence: 99%

Fibronectin-binding protein acts as Staphylococcus aureus invasin via fibronectin bridging to integrin alpha5beta1

Sinha¹,

François²,

Nüße³

et al. 1999

Cell Microbiol

507

563

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“…Heparin-The N-terminal HBD1 consists of five type I (FN1) homologous repeats that form two distinct regions, the N-terminal FN1(1-3) region containing the binding site for heparin and the FN1(4 -5) region that includes the binding site for fibrin (25) (Fig. 1D).…”

Section: Cd157 Binding To Fn Is Prevented Bymentioning

confidence: 99%

Binding of CD157 Protein to Fibronectin Regulates Cell Adhesion and Spreading

Morone¹,

Augeri²,

Cuccioloni

et al. 2014

Journal of Biological Chemistry

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Background: Surface CD157 modulates leukocyte and ovarian cancer cell adhesion and migration through the interaction with an unknown ligand. Results: CD157 binds heparin-binding domains of numerous extracellular matrix proteins with high affinity. Conclusion:The interaction of CD157 with extracellular matrix proteins is instrumental in the regulation of cell adhesion. Significance: These findings provide valuable insights into the biological mechanism responsible for the nonenzymatic functions of CD157.

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“…Fn has a mosaic structure and is composed of independently folded Fn type 1, type 2 and type 3 (F1, F2, and F3) modules (22) (Fig. 1C).…”

mentioning

confidence: 99%

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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Fibronectin structure and assembly

Cited by 205 publications

References 61 publications

Fibronectin-binding protein acts as Staphylococcus aureus invasin via fibronectin bridging to integrin alpha5beta1

Fibronectin-binding protein acts as Staphylococcus aureus invasin via fibronectin bridging to integrin alpha5beta1

Binding of CD157 Protein to Fibronectin Regulates Cell Adhesion and Spreading

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

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