Dataset Information

The streptococcal binding site in the gelatin-binding domain of fibronectin is consistent with a non-linear arrangement of modules.

ABSTRACT: Fibronectin-binding proteins (FnBPs) of Staphylococcus aureus and Streptococcus pyogenes mediate invasion of human endothelial and epithelial cells in a process likely to aid the persistence and/or dissemination of infection. In addition to binding sites for the N-terminal domain (NTD) of fibronectin (Fn), a number of streptococcal FnBPs also contain an upstream region (UR) that is closely associated with an NTD-binding region; UR binds to the adjacent gelatin-binding domain (GBD) of Fn. Previously, UR was shown to be required for efficient streptococcal invasion of epithelial cells. Here we show, using a Streptococcus zooepidemicus FnBP, that the UR-binding site in GBD resides largely in the (8)F1(9)F1 module pair. We also show that UR inhibits binding of a peptide from the ?1 chain of type I collagen to (8)F1(9)F1 and that UR binding to (8)F1 is likely to occur through anti-parallel ?-zipper formation. Thus, we propose that streptococcal proteins that contain adjacent NTD- and GBD-binding sites form a highly unusual extended tandem ?-zipper that spans the two domains and mediates high affinity binding to Fn through a large intermolecular interface. The proximity of the UR- and NTD-binding sequences in streptococcal FnBPs is consistent with a non-linear arrangement of modules in the tertiary structure of the GBD of Fn.

SUBMITTER: Atkin KE

PROVIDER: S-EPMC2978626 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature

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The streptococcal binding site in the gelatin-binding domain of fibronectin is consistent with a non-linear arrangement of modules.

Atkin Kate E KE Brentnall Andrew S AS Harris Gemma G Bingham Richard J RJ Erat Michele C MC Millard Christopher J CJ Schwarz-Linek Ulrich U Staunton David D Vakonakis Ioannis I Campbell Iain D ID Potts Jennifer R JR

The Journal of biological chemistry 20100915 47

Fibronectin-binding proteins (FnBPs) of Staphylococcus aureus and Streptococcus pyogenes mediate invasion of human endothelial and epithelial cells in a process likely to aid the persistence and/or dissemination of infection. In addition to binding sites for the N-terminal domain (NTD) of fibronectin (Fn), a number of streptococcal FnBPs also contain an upstream region (UR) that is closely associated with an NTD-binding region; UR binds to the adjacent gelatin-binding domain (GBD) of Fn. Previou ...[more]

PMID: 20843804

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Dataset Information

The streptococcal binding site in the gelatin-binding domain of fibronectin is consistent with a non-linear arrangement of modules.

Publications

The streptococcal binding site in the gelatin-binding domain of fibronectin is consistent with a non-linear arrangement of modules.

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