Recent research is providing compelling evidence for protein glycosylation being central to the survival and pathogenesis of many bacteria and thus represents an ideal target to disable them. Bacterial glycosylation systems are a largely untapped resource to counteract the continued threat posed by bacterial pathogens, either through the development of novel antimicrobials or via glycoconjugate vaccines. However, to fully realize this benefit, and in the longer term to produce recombinant human glycoproteins of considerable therapeutic value, a better understanding of the basic mechanisms and pathways of bacterial glycosylation is essential. Mass spectrometry is playing a pivotal role in providing this understanding.
This workshop talk will discuss glycomic and glycoproteomic strategies that are suited to unravelling N- and O-glycosylation pathways in both gram positive and gram negative pathogens. Examples will include glycoproteins from Clostridium difficile, Campylobacter jejuni, Streptococcus parasanguinis and Neisseria meningitidis.