Dynamics of the interaction between a fibronectin molecule and a living bacterium under mechanical force.
Fibronectin (Fn) is an important mediator of bacterial invasions and of persistent infections like that of Staphylococcus epidermis. Similar to many other types of cell-protein adhesion, the binding between Fn and S. epidermidis takes place under physiological shear rates. We investigated the dynamics of the interaction between individual living S. epidermidis cells and single Fn molecules under mechanical force by using the scanning force microscope. The mechanical strength of this interaction and the binding site in the Fn molecule were determined. The energy landscape of the binding/unbinding process was mapped, and the force spectrum and the association and dissociation rate constants of the binding pair were measured. The interaction between S. epidermidis cells and Fn molecules is compared with those of two other protein/ligand pairs known to mediate different dynamic states of adhesion of cells under a hydrodynamic flow: the firm adhesion mediated by biotin/avidin interactions, and the rolling adhesion, mediated by L-selectin/P-selectin glycoprotein ligand-1 interactions. The inner barrier in the energy landscape of the Fn case characterizes a high-energy binding mode that can sustain larger deformations and for significantly longer times than the correspondent high-strength L-selectin/P-selectin glycoprotein ligand-1 binding mode. The association kinetics of the former interaction is much slower to settle than the latter. On this basis, the observations made at the macroscopic scale by other authors of a strong lability of the bacterial adhesions mediated by Fn under high turbulent flow are rationalized at the molecular level.
Bustanji
Yasser
Y
Dipartimento di Biochimica, Università degli Studi di Bologna, Via Irnerio 48, 40126 Bologna, Italy.
Arciola
Carla Renata
CR
Conti
Matteo
M
Mandello
Enrico
E
Montanaro
Lucio
L
Samorí
Bruno
B
D001360:Avidin / Q000737:chemistry; D001422:Bacterial Adhesion; D055592:Biophysical Phenomena; D001703:Biophysics; D001710:Biotin / Q000737:chemistry; D002448:Cell Adhesion; D005353:Fibronectins / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D018625:Microscopy, Atomic Force; D011485:Protein Binding; D013211:Staphylococcus aureus / Q000378:metabolism; D013212:Staphylococcus epidermidis / Q000378:metabolism*; D013997:Time Factors; D014867:Water
D005353:Fibronectins; D014867:Water; D001360:Avidin; D001710:Biotin