The role of glycan-galectin interactions in regulating B cell signalling and activation

感染时免疫系统细胞的活化伴随着细胞表面蛋白的重组。这种重组在指导细胞如何应对病原体方面起着关键作用。控制细胞表面蛋白质组织的细胞组分尚不清楚。然而，几乎每一种参与识别和清除病原体的蛋白质都通过在称为糖基化的过程中添加糖链进行修饰。半乳糖凝集素是可以结合糖基化蛋白并因此在细胞表面上产生晶格样结构的蛋白质家族，其可以控制细胞表面蛋白质的组织或区室化。此外，半乳糖凝集素涉及健康和疾病状态下的广泛生物过程。尽管这些蛋白质的重要性，这些影响的机制仍然在很大程度上未知。我的研究目标是了解半乳糖凝集素和糖基化细胞表面蛋白之间的相互作用如何调节免疫细胞活化。我的目标是应用新的和新兴的光学显微镜技术，以可视化这些相互作用如何在单分子水平上调节细胞表面蛋白的运动和聚集，以及这些相互作用如何影响免疫细胞激活。这些研究可能会在我们对免疫反应的理解方面产生根本性的进步，它是如何调节的，以及如何最有效地调节它以达到治疗目的。

The activation of cells of the immune system upon infection is accompanied by the reorganization of cell surface proteins. Such reorganization plays a key role in directing how the cell responds to the pathogen. The cellular components that control the organization of cell surface proteins are not clear. However, nearly every protein involved in the recognition and clearance of pathogens is modified by the addition of sugar chains in a process known as glycosylation. Galectins are a family of proteins that can bind to glycosylated proteins and thus create a lattice-like structure on the cell surface, which may control the organization or compartmentalization of cell surface proteins. Moreover, galectins are implicated in a wide range of biological processes in both healthy and disease states. Despite the importance of these proteins, the mechanisms that underlie these effects remain largely unknown. My research goal is to understand how the interaction between galectins and glycosylated cell surface proteins regulates immune cell activation. I aim to apply new and emerging optical microscopy techniques in order to visualize how these interactions regulate the movement and clustering of cell surface proteins at both the level of single molecules as well as how these interactions effect immune cell activation. These studies are likely to yield fundamental advances in our understanding of the immune response, how it is regulated, and how it can most effectively be modulated for therapeutic purposes.