Cargo uptake and release of the human lectin receptor Langerin

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C-type lectins are important receptors of the innate immune system. Cell surface exposed CTLs internalize glycosylated antigens and initiate their endosomal routing leading to efficient processing. Hence, these lectin receptors determine the fate of the antigen and consequently dictate the elicited immune response. How this interplay between ligand recognition, uptake and endosomal release works is not completely understood. We chose Langerin as our model receptor to study the relation between receptor architecture and immune cell biology. Our previous data unraveled an allosteric network of communicating amino acids, which modulate the pH and calcium affinity and therefore enable us to manipulate the cellular system. Several contradictory reports exist on the Langerin-mediated antigen uptake and processing. With our tools in hand we cannot only dissect the molecular basis for the strong context dependent receptor biology reported, but at the same time delineate general hallmarks for C-type lectin mediated immunity.