On the surface of fungal cells under shear stress, amyloid-like cross-β bonds cluster adhesins to make high avidity adhesive patches. The cross-b bonding is essential for formation of robust biofilms that remain intact under liquid flow. Confocal microscopy and atomic force microscopy (AFM) demonstrate the cross-β patches on the surface of individual cells in cis. Single cell AFM demonstrates that cross-β bonds also form cell-to-cell bonds in trans. The bonds form in three steps: First shear stress unfolds pseudo-stable protein domains in the adhesins, exposing cross-b core sequences. Second, multiple adhesin molecules on the cell surface cluster in cis through interactions of cross-bcore sequences. Third, the clustered adhesins interact in trans to form amyloid-like adhesive bonds between the cells. Both types of cross-b bonding are inhibited by anti-amyloid treatments or mutation of the cross-b core sequences. The clustering depends on the presence of long unstructured glycoprotein stalks in the C-terminal regions of the adhesins. The stalks allow the N-terminal regions to access large areas of the cell surface, allowing cross-b interactions with nearby adhesin molecules. Such cross-b bonding is abundant in pathological fungal abscesses, and similar cross-b interactions are predicted in most fungal adhesins.