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

感染时免疫系统细胞的激活伴随着细胞表面蛋白的重组。这种重组在指导细胞如何对病原体作出反应方面起着关键作用。控制细胞表面蛋白组织的细胞成分尚不清楚。然而，几乎所有参与病原体识别和清除的蛋白质都是通过糖基化过程中添加糖链来修饰的。半乳糖凝集素是一类可以与糖基化蛋白结合，从而在细胞表面形成晶格状结构的蛋白，这种结构可以控制细胞表面蛋白的组织或区隔化。此外，在健康和疾病状态下，凝集素涉及广泛的生物过程。尽管这些蛋白质很重要，但这些作用背后的机制在很大程度上仍然未知。我的研究目标是了解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的激活。我的目标是应用新的和新兴的光学显微镜技术，以便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质的运动和聚集，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取得根本性的进展，它是如何被调节的，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.