High-force catch bonds between the Staphylococcus aureus surface protein SdrE and complement regulator factor H drive immune evasion

Oliveira Paiva, Telmo Manuel;Geoghegan, Joan A.;Dufrêne, Yves
(2023) Communications Biology — Vol. 6, n° 1, p. 302 (2023)

Files

s42003-023-04660-1.pdf
  • Open Access
  • Adobe PDF
  • 1.84 MB
Download

Details

Authors
Abstract
The invasive bacterial pathogen Staphylococcus aureus recruits the complement regulatory protein factor H (fH) to its surface to evade the human immune system. Here, we report the identification of an extremely high-force catch bond used by the S. aureus surface protein SdrE to efficiently capture fH under mechanical stress. We find that increasing the external force applied to the SdrE-fH complex prolongs the lifetime of the bond at an extraordinary high force, 1,400 pN, above which the bond lifetime decreases as an ordinary slip bond. This catch-bond behavior originates from a variation of the dock, lock and latch interaction, where the SdrE ligand binding domains undergo conformational changes under stress, enabling the formation of long-lived hydrogen bonds with fH. The binding mechanism dissected here represents a potential target for new therapeutics against multidrug-resistant S. aureus strains. © 2023, The Author(s).
Affiliations

Citations

  • APA
  • Chicago
  • FWB

Oliveira Paiva, T. M., Geoghegan, J. A., & Dufrêne, Y. (2023). High-force catch bonds between the Staphylococcus aureus surface protein SdrE and complement regulator factor H drive immune evasion. Communications Biology, 6(1), 302. https://doi.org/10.1038/s42003-023-04660-1 (Original work published 2023)