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The Candida albicans agglutinin-like sequence 3 protein (Als3) is a cell surface glycoprotein essential for the initial attachment of Candida albicans to human and microbial cells and for the formation and architecture of biofilms[1][3][6]. Als3 harbors an N-terminal domain responsible for peptide binding, a region with amyloid-forming potential that promotes aggregation, and a C-terminal GPI anchor for cell wall attachment[6]. Als3 is one of the most prominent adhesins and virulence factors in Candida pathogenesis: its deletion drastically reduces fungal adhesion and biofilm resilience[3][6]. Biofilm-localized Als3 also modulates antifungal resistance, as strains lacking Als3 show increased susceptibility to common antifungals including fluconazole, miconazole, and amphotericin B[1]. Mutations affecting the peptide-binding cavity in Als3 abolish its adhesive properties but do not affect protein expression levels or immunodetection[3][6]. Als3’s role as a major mediator of pathogenicity makes it a potential target for the development of antifungal therapies and vaccines[3][6].
Inhibition of biofilm structure and adhesion (by deletion or blocking of Als3, sensitizing biofilms to antifungals). Increased antifungal susceptibility via disruption of Als3 function. Possible vaccine target for blocking adhesion to host cells.
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