Research Projects

Within the pathogen Acinetobacter baumannii multiple proteins are known to be O-linked glycosylated yet the functional significance of these events are unclear. To date glycoproteomics studies have revealed similar proteins are targeted for glycosylation between A. baumannii strains and that glycosylation preferentially occurs on serine residues. While this suggest similar glycoproteomes between strains we now know the glycan used for O-linked glycosylation is hypervariable due to being derived from the capsule loci, also known as the K-loci. This hypervariability results in the glycans used for protein glycosylation varying between strains raising the question if these different glycans have functional impacts on the proteome/glycoproteome. Within this project K-loci1 in strains of interest will be targeted for mutagenesis using a novel I-SecI approach2 to make capsule/glycosylation negative strains. Using a recombineering based cloning approach 3,4different k loci will be cloned on plasmids allowing the restoration, as well as exchange, of different capsules enabling us to assess the impact of different glycans on the glycoproteome/proteome. Proteome changes due to different glycans will be assessed using proteomic as well as phenotypic analysis with our goal to test the role of specific glycans in modulating the functions in A. baumannii. Combined this work will provide new insight into how glycosylation shapes A. baumanniibiology.

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