Force-clamp spectroscopy identifies a catch bond mechanism in a Gram-positive pathogen

Marion Mathelié-Guinlet, Felipe Viela, Giampiero Pietrocola, Pietro Speziale, David Alsteens () and Yves F. Dufrêne ()
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Marion Mathelié-Guinlet: UCLouvain
Felipe Viela: UCLouvain
Giampiero Pietrocola: Unit of Biochemistry, University of Pavia
Pietro Speziale: Unit of Biochemistry, University of Pavia
David Alsteens: UCLouvain
Yves F. Dufrêne: UCLouvain

Nature Communications, 2020, vol. 11, issue 1, 1-8

Abstract: Abstract Physical forces have profound effects on cellular behavior, physiology, and disease. Perhaps the most intruiguing and fascinating example is the formation of catch-bonds that strengthen cellular adhesion under shear stresses. Today mannose-binding by the Escherichia coli FimH adhesin remains one of the rare microbial catch-bond thoroughly characterized at the molecular level. Here we provide a quantitative demonstration of a catch-bond in living Gram-positive pathogens using force-clamp spectroscopy. We show that the dock, lock, and latch interaction between staphylococcal surface protein SpsD and fibrinogen is strong, and exhibits an unusual catch-slip transition. The bond lifetime first grows with force, but ultimately decreases to behave as a slip bond beyond a critical force (~1 nN) that is orders of magnitude higher than for previously investigated complexes. This catch-bond, never reported for a staphylococcal adhesin, provides the pathogen with a mechanism to tightly control its adhesive function during colonization and infection.

Date: 2020
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DOI: 10.1038/s41467-020-19216-8

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