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C. albicans  binds various bacteria, including the oral commensal  Streptococcus gordonii . Published reports documented the role of  C. albicans  Als3 and  S. gordonii  SspB in this interaction, and the importance of the Als N-terminal domain (NT-Als) in  C. albicans  adhesion. Here, we demonstrate that Als1 also binds  S. gordonii . We also describe use of the NT-Als crystal structure to design mutations that precisely disrupt peptide-binding cavity (PBC) or amyloid-forming region (AFR) function in Als3.  C. albicans  displaying Als3 PBC mutant proteins showed significantly reduced binding to  S. gordonii ; mutation of the AFR did not affect the interaction. These observations present an enigma: the Als PBC binds free C termini of ligands, but the SspB C terminus is covalently linked to peptidoglycan and thus unavailable as a ligand. These observations and the predicted SspB elongated structure suggest that partial proteolysis of streptococcal cell wall proteins is necessary for recognition by Als adhesins.

A proposed mechanism for the interaction between the Candida albicans Als3 adhesin and streptococcal cell wall proteins