Expanding our understanding of the role of microbial glycoproteomes through high-throughput mass spectrometry approaches

AbstractProtein glycosylation is increasingly recognised as an essential requirement for effective microbial infections. Within microbial pathogen ’s protein glycosylation is used for both defensive and offensive purposes; enabling pathogens to fortify themselves against the host immune response or to disarm the host’s ability to resist infection. Although microbial protein glycosylation systems have been recognised for nearly two decades only recently has the true extend of protein glycosylation within microbes begun to be appreciated. A key enabler for this conceptual shift has been the development and application of modern approaches for the characterisation of glycosylation. Over the last decade my research has focused on the dev elopment of proteomic tools to probe microbial glycosylation. By developing workflows for glycopeptide enrichment and identification we have demostrated that it is now possible to characterise the glycoproteomes of microbial species in a truely high-throughput manner. Using these high-throughput app roaches we have shown a number of bacterial species modify multiple proteins including members of the Campylobacter genus and the pathogensA. baumannii,R. solanacearum andB. cenocepacia. These studies have established that bacterial glycosylation is widespread, that glycan microheterogeneity is common place and that an extensive array of glycans are used to decorate protein compared to Eukaryotic glycosylation systems. Excitingly these approaches ...

Source: Glycoconjugate Journal - July 3, 2019 Category: Biochemistry Source Type: research