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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...

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Autores principales: 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.
Formato: Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2010
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.
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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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