Single-Molecule Analysis Demonstrates Stress-Enhanced Binding between Staphylococcus aureus Surface Protein IsdB and Host Cell Integrins

Mathelie-Guinlet, Marion;Viela Bovio, Felipe;Alfeo, Mariangela Jessica;Pietrocola, Giampiero;Dufrêne, Yves;et.al.
(2020) Nano Letters : a journal dedicated to nanoscience and nanotechnology — Vol. 20, n° 12, p. 8919-8925 (2020)

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Authors
  • Mathelie-Guinlet, Marionorcid-logoUCLouvain
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  • Viela Bovio, Felipeorcid-logoUCLouvain
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  • Alfeo, Mariangela Jessica
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  • Pietrocola, Giampieroorcid-logo
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  • Dufrêne, YvesUCLouvain
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Abstract
Binding of Staphylococcus aureus surface proteins to endothelial cell integrins plays essential roles in host cell adhesion and invasion, eventually leading to life-threatening diseases. The staphylococcal protein IsdB binds to β3-containing integrins through a mechanism that has never been thoroughly investigated. Here, we identify and characterize at the nanoscale a previously undescribed stress-dependent adhesion between IsdB and integrin αVβ3. The strength of single IsdB-αVβ3 interactions is moderate (∼100 pN) under low stress, but it increases dramatically under high stress (∼1000-2000 pN) to exceed the forces traditionally reported for the binding between integrins and Arg-Gly-Asp (RGD) sequences. We suggest a mechanism where high mechanical stress induces conformational changes in the integrin from a low-affinity, weak binding state to a high-affinity, strong binding state. This single-molecule study highlights that direct adhesin-integrin interactions represent potential targets to fight staphylococcal infections.
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Mathelie-Guinlet, M., Viela Bovio, F., Alfeo, M. J., Pietrocola, G., Speziale, P., & Dufrêne, Y. (2020). Single-Molecule Analysis Demonstrates Stress-Enhanced Binding between Staphylococcus aureus Surface Protein IsdB and Host Cell Integrins. Nano Letters : a journal dedicated to nanoscience and nanotechnology, 20(12), 8919-8925. https://doi.org/10.1021/acs.nanolett.0c04015 (Original work published 2020)