Cargo uptake and release of the human lectin receptor Langerin

人类凝集素受体 Langerin 的货物摄取和释放

• 批准号: 388821358
• 负责人: Professor Dr. Christoph Rademacher
• 金额: --
• 依托单位: Research group Clinical Pharmacy and Diagnostics
• 依托单位国家: 德国
• 项目类别: Research Grants
• 财政年份: 2017
• 资助国家: 德国
• 起止时间: 2016-12-31 至 2020-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/388821358?language=en
• 关键词: Cargo; uptake; release; human; lectin

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.

C型凝集素是先天免疫系统的重要受体。细胞表面暴露的CTL内化糖基化抗原并启动其内体路由，从而导致有效加工。因此，这些凝集素受体决定了抗原的命运，并因此决定了引发的免疫应答。配体识别、摄取和内体释放之间的这种相互作用是如何起作用的还不完全清楚。我们选择Langerin作为我们的模型受体来研究受体结构和免疫细胞生物学之间的关系。我们以前的数据揭示了一个交流氨基酸的变构网络，它调节pH值和钙亲和力，因此使我们能够操纵细胞系统。关于Langerin介导的抗原摄取和加工存在一些相互矛盾的报告。有了我们的工具，我们不仅可以剖析所报道的强背景依赖性受体生物学的分子基础，而且同时描绘C型凝集素介导的免疫的一般特征。