Research Projects

O-linked Protein glycosylation, the chemical addition of polymers of sugars referred to as glycans to residues of proteins, enables the augmentation of protein properties and is now known to be widespread in bacterial systems 5-7. Within Burkholderia species O-linked glycosylation occurs within the periplasmic space involving the transfer of a trisaccharide β-Gal-(1,3)-α-GalNAc-(1,3)-β-GalNAc to protein substrates by the oligosaccharyltransferase pglL 7 with the O-linked Glycosylation Cluster (OGC) responsible for the biosynthesis of the O-linked glycan trisaccharide 5. Across multiple Burkholderia species it has been noted that the O-linked trisaccharide can be further modified by succinylation7,8 yet the function as well as the enzyme/s responsible for succinylation are currently unknown. The goal of this study is to gain a better understanding of the origins and roles of glycan succinylation observed within the Burkholderia O-linked glycan used for protein glycosylation. Using mutagenesis as well as complementation studies the consequences and roles of potential succinyltransferases will be assessed using proteomic and phenotypic assays. By studying succinylation within B. cenocepacia, we aim to gain insight into how this glycan modification impacts the bacterial proteome and survival.

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