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Candida albicans surface adhesins and cell wall antigens are a diverse group of glycoproteins and polysaccharides that form the outermost layer of the fungal cell, serving as the primary interface with the host environment [6, 9]. These components, which include the agglutinin-like sequence (Als) proteins, hyphal wall protein 1 (Hwp1), and structural polysaccharides such as beta-glucans and mannans, are essential for the fungus's ability to adhere to host tissues, form resilient biofilms, and transition between yeast and hyphal forms [1, 13]. Because of their critical role in virulence and their accessibility on the cell surface, they are prime targets for the development of novel antifungal therapies, including vaccines like NDV-3A and monoclonal antibodies designed to neutralize adhesion or opsonize the fungus for immune clearance [10, 12]. Additionally, existing antifungal classes like echinocandins exert their effects by disrupting the synthesis of these cell wall components, specifically inhibiting beta-1,3-glucan synthase [3, 7]. The dynamic nature of the cell wall allows C. albicans to adapt to host defenses, making these surface molecules central to both the pathogenesis of invasive candidiasis and the development of targeted immunotherapies [13, 14].
Drugs targeting these components work by inhibiting the synthesis of structural polysaccharides (e.g., beta-1,3-glucan synthase inhibition), neutralizing surface adhesins to prevent host colonization, or opsonizing the fungal cells to enhance phagocytic clearance by the host immune system.
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