Dual specificity of Langerin to sulfated and mannosylated glycans via a single C-type carbohydrate recognition domain.

ABSTRACT: Langerin is categorized as a C-type lectin selectively expressed in Langerhans cells, playing roles in the first line of defense against pathogens and in Birbeck granule formation. Although these functions are thought to be exerted through glycan-binding activity of the C-type carbohydrate recognition domain, sugar-binding properties of Langerin have not been fully elucidated in relation to its biological functions. Here, we investigated the glycan-binding specificity of Langerin using comprehensive glycoconjugate microarray, quantitative frontal affinity chromatography, and conventional cell biological analyses. Langerin showed outstanding affinity to galactose-6-sulfated oligosaccharides, including keratan sulfate, while it preserved binding activity to mannose, as a common feature of th

SUBMITTER: Tateno H 

PROVIDER: S-EPMC2825434 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature