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

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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.