The adhesion of pathogenic bacteria to surfaces is of immense importance for health care applications.
Via a combined experimental and computational approach, we studied the initiation of contact in the
adhesion process of the pathogenic bacterium Staphylococcus aureus. AFM force spectroscopy with
single cell bacterial probes paired with Monte Carlo simulations enabled an unprecedented molecular
investigation of the contact formation. Our results reveal that bacteria attach to a surface over distances
far beyond the range of classical surface forces via stochastic binding of thermally fluctuating cell wall
proteins. Thereby, the bacteria are pulled into close contact with the surface as consecutive proteins of
different stiffnesses attach. This mechanism greatly enhances the attachment capability of S. aureus. It,
however, can be manipulated by enzymatically/chemically modifying the cell wall proteins to block their
consecutive binding. Our study furthermore reveals that fluctuations in protein density and structure are
much more relevant than the exact form of the binding potential
