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C-type lectin Langerin is a beta-glucan receptor on human Langerhans cells that recognizes opportunistic and pathogenic fungi.

de Jong MA, Vriend LE, Theelen B, Taylor ME, Fluitsma D, Boekhout T, Geijtenbeek TB - Mol. Immunol. (2010)

Bottom Line: We have screened a large panel of fungi for recognition by human Langerin and, strikingly, we observed strong binding of Langerin to a variety of Candida and Saccharomyces species and Malassezia furfur, but very weak binding was observed to Cryptococcus gattii and Cryptococcus neoformans.Notably, Langerin is the primary fungal receptor on LCs, since the interaction of LCs with the different fungi was blocked by antibodies against Langerin.Langerin recognizes both mannose and beta-glucans present on fungal cell walls and our data demonstrate that Langerin is the major fungal pathogen receptor on human LCs that recognizes pathogenic and commensal fungi.

View Article: PubMed Central - PubMed

Affiliation: Center for Experimental and Molecular Medicine, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands.

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Titration of a selection of fungi. Yeast strains from Candida species (A and B), Cryptococcus neoformans (C), Cryptococcus gattii (D), and Saccharomyces cerevisiae (E) were coated onto ELISA plates at different concentrations. Mannan was used to determine specificity. Data are representative of at least three independent experiments. Error bars represent standard deviation of triplicates.
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fig2: Titration of a selection of fungi. Yeast strains from Candida species (A and B), Cryptococcus neoformans (C), Cryptococcus gattii (D), and Saccharomyces cerevisiae (E) were coated onto ELISA plates at different concentrations. Mannan was used to determine specificity. Data are representative of at least three independent experiments. Error bars represent standard deviation of triplicates.

Mentions: Langerin efficiently interacted with all Candida species tested, namely C. albicans, C. glabrata, C. guilliermondii, C. krusei, C. lusitaniae, and C. nivariensis, and Saccharomyces cerevisiae at a concentration of 106 and 107/ml, whereas most binding was lost at 105/ml or lower (Figs. 1D and 2A, B and E). No difference was observed between virulent and non-virulent strains of S. cerevisiae (Fig. 2E). Cryptococcus species only weakly interacted with Langerin at high concentrations which was abrogated after dilution (Fig. 2C and D). These data demonstrate that Langerin is a fungal receptor that interacts with Malassezia furfur, Saccharomyces and Candida species but not with Cryptococcus species.


C-type lectin Langerin is a beta-glucan receptor on human Langerhans cells that recognizes opportunistic and pathogenic fungi.

de Jong MA, Vriend LE, Theelen B, Taylor ME, Fluitsma D, Boekhout T, Geijtenbeek TB - Mol. Immunol. (2010)

Titration of a selection of fungi. Yeast strains from Candida species (A and B), Cryptococcus neoformans (C), Cryptococcus gattii (D), and Saccharomyces cerevisiae (E) were coated onto ELISA plates at different concentrations. Mannan was used to determine specificity. Data are representative of at least three independent experiments. Error bars represent standard deviation of triplicates.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2837148&req=5

fig2: Titration of a selection of fungi. Yeast strains from Candida species (A and B), Cryptococcus neoformans (C), Cryptococcus gattii (D), and Saccharomyces cerevisiae (E) were coated onto ELISA plates at different concentrations. Mannan was used to determine specificity. Data are representative of at least three independent experiments. Error bars represent standard deviation of triplicates.
Mentions: Langerin efficiently interacted with all Candida species tested, namely C. albicans, C. glabrata, C. guilliermondii, C. krusei, C. lusitaniae, and C. nivariensis, and Saccharomyces cerevisiae at a concentration of 106 and 107/ml, whereas most binding was lost at 105/ml or lower (Figs. 1D and 2A, B and E). No difference was observed between virulent and non-virulent strains of S. cerevisiae (Fig. 2E). Cryptococcus species only weakly interacted with Langerin at high concentrations which was abrogated after dilution (Fig. 2C and D). These data demonstrate that Langerin is a fungal receptor that interacts with Malassezia furfur, Saccharomyces and Candida species but not with Cryptococcus species.

Bottom Line: We have screened a large panel of fungi for recognition by human Langerin and, strikingly, we observed strong binding of Langerin to a variety of Candida and Saccharomyces species and Malassezia furfur, but very weak binding was observed to Cryptococcus gattii and Cryptococcus neoformans.Notably, Langerin is the primary fungal receptor on LCs, since the interaction of LCs with the different fungi was blocked by antibodies against Langerin.Langerin recognizes both mannose and beta-glucans present on fungal cell walls and our data demonstrate that Langerin is the major fungal pathogen receptor on human LCs that recognizes pathogenic and commensal fungi.

View Article: PubMed Central - PubMed

Affiliation: Center for Experimental and Molecular Medicine, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands.

Show MeSH
Related in: MedlinePlus