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Candida cell wall epitopes and virulence-associated proteins encompass a broad array of structural and functional molecules essential for the pathogenicity of Candida species, most notably Candida albicans. The fungal cell wall is a dynamic, multilayered structure consisting of an inner core of chitin and beta-glucans, and an outer layer of mannosylated proteins (mannoproteins) [8, 11]. These components are critical for maintaining cell integrity, mediating adhesion to host tissues (e.g., Als3, Hwp1), and facilitating invasion through the secretion of hydrolases like secreted aspartyl proteases (Saps) [4, 10]. Because these molecules are absent in humans and are surface-exposed, they serve as primary targets for the host immune system and therapeutic interventions [2, 6]. Current treatments include echinocandins, which inhibit beta-glucan synthesis, while emerging strategies focus on vaccines (e.g., NDV-3A) and monoclonal antibodies designed to neutralize virulence factors or enhance opsonization [1, 3, 7]. Targeting these epitopes is particularly relevant for addressing multidrug-resistant pathogens like Candida auris, where traditional antifungals may fail [2, 12].
Inhibition of beta-1,3-glucan synthase; Inhibition of Gwt1 protein (GPI-anchor synthesis); Neutralization of virulence factors; Opsonization and enhancement of phagocytosis; Inhibition of secreted aspartyl proteases
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