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High-force catch bonds between the <i>Staphylococcus aureus</i> surface protein SdrE and complement regulator factor H drive immune evasion
Authors
Yves F Dufrêne
Joan A Geoghegan
Telmo O Paiva
Publication date
1 January 2023
Publisher
'Springer Science and Business Media LLC'
Doi
Cite
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)
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Last time updated on 19/07/2023