Force-clamp spectroscopy identifies a catch bond mechanism in a Gram-positive pathogen
(2020) Nature Communications — Vol. 11, n° 1, p. 1 (2020)
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- Authors
Mathelie-Guinlet, Marion 
Viela Bovio, Felipe Pietrocola, Giampiero
- 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.
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Citations
Mathelie-Guinlet, M., Viela Bovio, F., Pietrocola, G., Speziale, P., Alsteens, D., & Dufrêne, Y. (2020). Force-clamp spectroscopy identifies a catch bond mechanism in a Gram-positive pathogen. Nature Communications, 11(1), 1. https://doi.org/10.1038/s41467-020-19216-8 (Original work published 2020)