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Nanonewton forces between Staphylococcus aureus surface protein IsdB and vitronectin
Single-molecule experiments have recently revealed that the interaction between staphylococcal surface proteins and their ligands can be extremely strong, equivalent to the strength of covalent bonds. Here, we report on the unusually high binding strength between Staphylococcus aureus iron-regulated...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
RSC
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9419033/ https://www.ncbi.nlm.nih.gov/pubmed/36133863 http://dx.doi.org/10.1039/d0na00636j |
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author | Mathelié-Guinlet, Marion Viela, Felipe Pietrocola, Giampiero Speziale, Pietro Dufrêne, Yves F. |
author_facet | Mathelié-Guinlet, Marion Viela, Felipe Pietrocola, Giampiero Speziale, Pietro Dufrêne, Yves F. |
author_sort | Mathelié-Guinlet, Marion |
collection | PubMed |
description | Single-molecule experiments have recently revealed that the interaction between staphylococcal surface proteins and their ligands can be extremely strong, equivalent to the strength of covalent bonds. Here, we report on the unusually high binding strength between Staphylococcus aureus iron-regulated surface determinant B (IsdB) and vitronectin (Vn), an essential human blood protein known to interact with bacterial pathogens. The IsdB–Vn interaction is dramatically strengthened by mechanical tension, with forces up to 2000 pN at a loading rate of 10(5) pN s(−1). In line with this, flow experiments show that IsdB-mediated bacterial adhesion to Vn is enhanced by fluid shear stress. The stress-dependent binding of IsdB to Vn is likely to play a role in promoting bacterial adhesion to human cells under fluid shear stress conditions. |
format | Online Article Text |
id | pubmed-9419033 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | RSC |
record_format | MEDLINE/PubMed |
spelling | pubmed-94190332022-09-20 Nanonewton forces between Staphylococcus aureus surface protein IsdB and vitronectin Mathelié-Guinlet, Marion Viela, Felipe Pietrocola, Giampiero Speziale, Pietro Dufrêne, Yves F. Nanoscale Adv Chemistry Single-molecule experiments have recently revealed that the interaction between staphylococcal surface proteins and their ligands can be extremely strong, equivalent to the strength of covalent bonds. Here, we report on the unusually high binding strength between Staphylococcus aureus iron-regulated surface determinant B (IsdB) and vitronectin (Vn), an essential human blood protein known to interact with bacterial pathogens. The IsdB–Vn interaction is dramatically strengthened by mechanical tension, with forces up to 2000 pN at a loading rate of 10(5) pN s(−1). In line with this, flow experiments show that IsdB-mediated bacterial adhesion to Vn is enhanced by fluid shear stress. The stress-dependent binding of IsdB to Vn is likely to play a role in promoting bacterial adhesion to human cells under fluid shear stress conditions. RSC 2020-10-30 /pmc/articles/PMC9419033/ /pubmed/36133863 http://dx.doi.org/10.1039/d0na00636j Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/ |
spellingShingle | Chemistry Mathelié-Guinlet, Marion Viela, Felipe Pietrocola, Giampiero Speziale, Pietro Dufrêne, Yves F. Nanonewton forces between Staphylococcus aureus surface protein IsdB and vitronectin |
title | Nanonewton forces between Staphylococcus aureus surface protein IsdB and vitronectin |
title_full | Nanonewton forces between Staphylococcus aureus surface protein IsdB and vitronectin |
title_fullStr | Nanonewton forces between Staphylococcus aureus surface protein IsdB and vitronectin |
title_full_unstemmed | Nanonewton forces between Staphylococcus aureus surface protein IsdB and vitronectin |
title_short | Nanonewton forces between Staphylococcus aureus surface protein IsdB and vitronectin |
title_sort | nanonewton forces between staphylococcus aureus surface protein isdb and vitronectin |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9419033/ https://www.ncbi.nlm.nih.gov/pubmed/36133863 http://dx.doi.org/10.1039/d0na00636j |
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