Bgl2p, Ecm33p, and Als1p proteins are involved in adhesion to saliva-coated hydroxyapatite.

: is an opportunistic pathogen that causes oral candidiasis. A previous study showed that Bgl2p and Ecm33p may mediate the interaction between the yeast and saliva-coated hydroxyapatite (SHA; a model for the tooth surface). This study investigated the roles of these cell wall proteins in the adherence of to SHA beads. : and null mutants were generated from wild-type strain SC5314 by using the -flipper gene disruption method. A novel method based on labelling the yeast with Nile red, was used to investigate the adherence. : Adhesion of and null mutants to SHA beads was 76.4% and 64.8% of the wild-type strain, respectively. Interestingly, the adhesion of the double mutant (87.7%) was higher than that of both single mutants. qRT-PCR analysis indicated that the gene was over-expressed in the strain. The triple null mutant showed a significantly reduced adherence to the beads, (37.6%), compared to the wild-type  strain. : Bgl2p and Ecm33p contributed to the interaction between and SHA beads. Deletion of these genes triggered overexpression of the gene in the mutant strain, and deletion of all three genes caused a significant decrease in adhesion.