Glycoproteins are ubiquitous biomolecules involved in many biological processes ranging from immune recognition to cancer development. In eukaryotes, glycosylation is known to impart novel biological and physical roles to proteins that can be grouped into two general categories, providing labels for cell-cell communication, and assisting in protein stabilization. Until recently it was thought that protein glycosylation was rare in prokaryotic systems. However, far from being a peculiarity of a few bacterial species, it is becoming increasingly clear that virtually all plant, animal and human bacterial pathogens have at least one protein glycosylation system.
Much of glycobiology research seeks to understand how glycans on cell surfaces engage with glycan-binding proteins to mediate adhesive and signalling events. Such recognition is central to cell-cell communication including interactions between pathogens, parasites and their hosts, between cells of the immune system, and between the commensal microbial community and the gastrointestinal tract.
My laboratory specialises in the development and exploitation of high sensitivity mass spectrometry for characterising biomedically important glycans. In partnership with collaborators worldwide, we aim to determine the biological functions which follow from the intimate molecular interactions of glycans and their lectin partners. This talk will describe applications of high sensitivity glycomic and glycoproteomic strategies to glycobiology research relevant to microbiology, including glycoimmunology and infection.