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Interaction of the Staphylococcus aureus Surface Protein FnBPB with Corneodesmosin Involves Two Distinct, Extremely Strong Bonds
[Image: see text] Attachment of Staphylococcus aureus to human skin corneocyte cells plays a critical role in exacerbating the severity of atopic dermatitis (AD). Pathogen-skin adhesion is mediated by bacterial cell-surface proteins called adhesins, including fibronectin-binding protein B (FnBPB). F...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9936583/ https://www.ncbi.nlm.nih.gov/pubmed/36820093 http://dx.doi.org/10.1021/acsnanoscienceau.2c00036 |
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author | Paiva, Telmo O. Viljoen, Albertus da Costa, Thaina M. Geoghegan, Joan A. Dufrêne, Yves F. |
author_facet | Paiva, Telmo O. Viljoen, Albertus da Costa, Thaina M. Geoghegan, Joan A. Dufrêne, Yves F. |
author_sort | Paiva, Telmo O. |
collection | PubMed |
description | [Image: see text] Attachment of Staphylococcus aureus to human skin corneocyte cells plays a critical role in exacerbating the severity of atopic dermatitis (AD). Pathogen-skin adhesion is mediated by bacterial cell-surface proteins called adhesins, including fibronectin-binding protein B (FnBPB). FnBPB binds to corneodesmosin (CDSN), a glycoprotein exposed on AD patient corneocytes. Using single-molecule experiments, we demonstrate that CDSN binding by FnBPB relies on a sophisticated two-site mechanism. Both sites form extremely strong bonds with binding forces of ∼1 and ∼2.5 nN albeit with faster dissociation rates than those reported for homologues of the adhesin. This previously unidentified two-binding site interaction in FnBPB illustrates its remarkable variety of adhesive functions and is of biological significance as the high strength and short bond lifetime will favor efficient skin colonization by the pathogen. |
format | Online Article Text |
id | pubmed-9936583 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-99365832023-02-18 Interaction of the Staphylococcus aureus Surface Protein FnBPB with Corneodesmosin Involves Two Distinct, Extremely Strong Bonds Paiva, Telmo O. Viljoen, Albertus da Costa, Thaina M. Geoghegan, Joan A. Dufrêne, Yves F. ACS Nanosci Au [Image: see text] Attachment of Staphylococcus aureus to human skin corneocyte cells plays a critical role in exacerbating the severity of atopic dermatitis (AD). Pathogen-skin adhesion is mediated by bacterial cell-surface proteins called adhesins, including fibronectin-binding protein B (FnBPB). FnBPB binds to corneodesmosin (CDSN), a glycoprotein exposed on AD patient corneocytes. Using single-molecule experiments, we demonstrate that CDSN binding by FnBPB relies on a sophisticated two-site mechanism. Both sites form extremely strong bonds with binding forces of ∼1 and ∼2.5 nN albeit with faster dissociation rates than those reported for homologues of the adhesin. This previously unidentified two-binding site interaction in FnBPB illustrates its remarkable variety of adhesive functions and is of biological significance as the high strength and short bond lifetime will favor efficient skin colonization by the pathogen. American Chemical Society 2022-10-18 /pmc/articles/PMC9936583/ /pubmed/36820093 http://dx.doi.org/10.1021/acsnanoscienceau.2c00036 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Paiva, Telmo O. Viljoen, Albertus da Costa, Thaina M. Geoghegan, Joan A. Dufrêne, Yves F. Interaction of the Staphylococcus aureus Surface Protein FnBPB with Corneodesmosin Involves Two Distinct, Extremely Strong Bonds |
title | Interaction
of the Staphylococcus aureus Surface
Protein FnBPB with Corneodesmosin Involves Two Distinct,
Extremely Strong Bonds |
title_full | Interaction
of the Staphylococcus aureus Surface
Protein FnBPB with Corneodesmosin Involves Two Distinct,
Extremely Strong Bonds |
title_fullStr | Interaction
of the Staphylococcus aureus Surface
Protein FnBPB with Corneodesmosin Involves Two Distinct,
Extremely Strong Bonds |
title_full_unstemmed | Interaction
of the Staphylococcus aureus Surface
Protein FnBPB with Corneodesmosin Involves Two Distinct,
Extremely Strong Bonds |
title_short | Interaction
of the Staphylococcus aureus Surface
Protein FnBPB with Corneodesmosin Involves Two Distinct,
Extremely Strong Bonds |
title_sort | interaction
of the staphylococcus aureus surface
protein fnbpb with corneodesmosin involves two distinct,
extremely strong bonds |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9936583/ https://www.ncbi.nlm.nih.gov/pubmed/36820093 http://dx.doi.org/10.1021/acsnanoscienceau.2c00036 |
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