Dynamic Force Spectroscopy of the BabA–Lewis b Binding
Résumé
The binding strength of the adhesin–receptor complex BabA-ABO/Lewis b has been analyzed by means of Dynamic Force Spectroscopy. High‑resolution measurements of rupture forces were performed on single bacterial cells, expressing the high affinity binding BabA adhesin, by use of a force measuring optical tweezers. The resulting force spectra revealed the mechanical properties of a single BabA‑Leb bond. It was found that the bond is dominated by one single energy barrier and that it is a slip‑bond. The bond length and thermal off–rate were assessed to 0.86±0.07 nm and 0.015±0.006 s, respectively.
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