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The Streptococcal Binding Site in the Gelatin-binding Domain of Fibronectin Is Consistent with a Non-linear Arrangement of Modules
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 fibronecti...
Autores principales: | , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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American Society for Biochemistry and Molecular Biology
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2978626/ https://www.ncbi.nlm.nih.gov/pubmed/20843804 http://dx.doi.org/10.1074/jbc.M110.156935 |
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author | Atkin, Kate E. Brentnall, Andrew S. Harris, Gemma Bingham, Richard J. Erat, Michele C. Millard, Christopher J. Schwarz-Linek, Ulrich Staunton, David Vakonakis, Ioannis Campbell, Iain D. Potts, Jennifer R. |
author_facet | Atkin, Kate E. Brentnall, Andrew S. Harris, Gemma Bingham, Richard J. Erat, Michele C. Millard, Christopher J. Schwarz-Linek, Ulrich Staunton, David Vakonakis, Ioannis Campbell, Iain D. Potts, Jennifer R. |
author_sort | Atkin, Kate E. |
collection | PubMed |
description | 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 α1 chain of type I collagen to (8)F1(9)F1 and that UR binding to (8)F1 is likely to occur through anti-parallel β-zipper formation. Thus, we propose that streptococcal proteins that contain adjacent NTD- and GBD-binding sites form a highly unusual extended tandem β-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. |
format | Text |
id | pubmed-2978626 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-29786262011-01-04 The Streptococcal Binding Site in the Gelatin-binding Domain of Fibronectin Is Consistent with a Non-linear Arrangement of Modules Atkin, Kate E. Brentnall, Andrew S. Harris, Gemma Bingham, Richard J. Erat, Michele C. Millard, Christopher J. Schwarz-Linek, Ulrich Staunton, David Vakonakis, Ioannis Campbell, Iain D. Potts, Jennifer R. J Biol Chem Glycobiology and Extracellular Matrices 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 α1 chain of type I collagen to (8)F1(9)F1 and that UR binding to (8)F1 is likely to occur through anti-parallel β-zipper formation. Thus, we propose that streptococcal proteins that contain adjacent NTD- and GBD-binding sites form a highly unusual extended tandem β-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. American Society for Biochemistry and Molecular Biology 2010-11-19 2010-09-15 /pmc/articles/PMC2978626/ /pubmed/20843804 http://dx.doi.org/10.1074/jbc.M110.156935 Text en © 2010 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version full access. Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) applies to Author Choice Articles |
spellingShingle | Glycobiology and Extracellular Matrices Atkin, Kate E. Brentnall, Andrew S. Harris, Gemma Bingham, Richard J. Erat, Michele C. Millard, Christopher J. Schwarz-Linek, Ulrich Staunton, David Vakonakis, Ioannis Campbell, Iain D. Potts, Jennifer R. The Streptococcal Binding Site in the Gelatin-binding Domain of Fibronectin Is Consistent with a Non-linear Arrangement of Modules |
title | The Streptococcal Binding Site in the Gelatin-binding Domain of Fibronectin Is Consistent with a Non-linear Arrangement of Modules |
title_full | The Streptococcal Binding Site in the Gelatin-binding Domain of Fibronectin Is Consistent with a Non-linear Arrangement of Modules |
title_fullStr | The Streptococcal Binding Site in the Gelatin-binding Domain of Fibronectin Is Consistent with a Non-linear Arrangement of Modules |
title_full_unstemmed | The Streptococcal Binding Site in the Gelatin-binding Domain of Fibronectin Is Consistent with a Non-linear Arrangement of Modules |
title_short | The Streptococcal Binding Site in the Gelatin-binding Domain of Fibronectin Is Consistent with a Non-linear Arrangement of Modules |
title_sort | streptococcal binding site in the gelatin-binding domain of fibronectin is consistent with a non-linear arrangement of modules |
topic | Glycobiology and Extracellular Matrices |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2978626/ https://www.ncbi.nlm.nih.gov/pubmed/20843804 http://dx.doi.org/10.1074/jbc.M110.156935 |
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