β-1,3-Glucan recognition by <i>Acanthamoeba castellanii</i> as a putative mechanism of amoeba-fungal interactions.

ABSTRACT: In this study, we conducted an in-depth analysis to characterize potential Acanthamoeba castellanii (Ac) proteins capable of recognizing fungal β-1,3-glucans. Ac specifically anchors curdlan or laminarin, indicating the presence of surface β-1,3-glucan-binding molecules. Using optical tweezers, strong adhesion of laminarin- or curdlan-coated beads to Ac was observed, highlighting their adhesive properties compared to controls (characteristic time τ of 46.9 and 43.9 s, respectively). Furthermore, Histoplasma capsulatum (Hc) G217B, possessing a β-1,3-glucan outer layer, showed significant adhesion to Ac compared to a Hc G186 strain with an α-1,3-glucan outer layer (τ of 5.3 s vs τ 83.6 s). The addition of soluble β-1,3-glucan substantia

SUBMITTER: Ferreira MdS 

PROVIDER: S-EPMC10880599 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature