Fig. 2: Both CLEC2D/TLR2 heterodimers and CLEC2D homodimers have high binding affinity to fungal β-glucans. | Nature Communications

Fig. 2: Both CLEC2D/TLR2 heterodimers and CLEC2D homodimers have high binding affinity to fungal β-glucans.

From: C-type lectin receptor 2d forms homodimers and heterodimers with TLR2 to negatively regulate IRF5-mediated antifungal immunity

Fig. 2

a Flow cytometry assay of the competitive binding of C. albicans yeast cells with CLEC2D-hIgG1-Fc or hIgG1-Fc (hFc) using the indicated polysaccharides. b Representative immunofluorescent staining assay of the binding of CLEC2D-hIgG1-Fc (green) or Dectin-1-hIgG1-Fc (green) with C. albicans. Chitin was stained with Calcofluor White (50 μg/ml, blue), and β-glucan was stained with anti β-1,3-glucan antibody (red). Scar bars = 2 μm. Three times experiments were repeated independently with similar results. c ELISA assay for the binding of indicated amino acid point mutated proteins of CLEC2D-hIgG1-Fc or hIgG1-Fc (hFc) with plate-coated curdlan or α-mannan (5 μg/well). d ELISA results for the binding of diluted CLEC2D-Fc and TLR2-His homo- or heterodimers with plated-coated curdlan, α-mannan or Pam3CSK4 (1 μg/well), which were detected with anti-Fc or -His Abs, respectively. e ELISA results for the binding of CLEC2D-Fc/TLR2-His heterodimers containing the dilution of either CLEC2D-Fc (Red line) or TLR2-His (Black line) with plated-coated curdlan, α-mannan or Pam3CSK4 (1 μg/well), which were detected with anti-Fc or -His Abs, respectively. f Flow cytometry assay of the competitive binding of Dectin-1-hIgG1-Fc with the CLEC2D-Fc/TLR2-His heterodimers to C. albicans yeast cells, which was detected with anti-His Ab. Data were presented as mean ± SEM; n = 3 (d–f), n = 4 (c) biologically independent samples. Data were analyzed by unpaired two-sided Student’s t-test in (c–f). Source data are provided as a Source Data file.

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