期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 285, 期 47, 页码 36977-36983出版社
ELSEVIER
DOI: 10.1074/jbc.M110.156935
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资金
- BBSRC
- British Heart Foundation
- FP7 Marie Curie Fellowship
- Wellcome Trust
- Biotechnology and Biological Sciences Research Council [BB/D010608/1] Funding Source: researchfish
- British Heart Foundation [FS/09/023/27460, FS/07/034/22969] Funding Source: researchfish
- BBSRC [BB/D010608/1] Funding Source: UKRI
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 alpha 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 beta-zipper formation. Thus, we propose that streptococcal proteins that contain adjacent NTD- and GBD-binding sites form a highly unusual extended tandem beta-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.
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