Role of O-linked glycosylation system across the Burkholderia genus
Protein glycosylation, the chemical addition of sugars to proteins, is an important but poorly understood aspect of bacterial physiology. Within the Burkholderia genus, we have discovered a highly conserved O-linked glycosylation system. The conservation of this system across pathogenic and non-pathogenic species suggests that glycosylation plays a far more fundamental role in the physiology of Bukholderia than previously thought. The goal of this project is to understand the role and diversity of glycosylation in Bukholderia. By studying glycosylation within Burkholderia we aim to gain a fundamental understanding of this biological process and how it contributes to bacterial survival.
Development of novel proteomic tools to explore Burkholderia glycosylation dependent pathogenesis
Bacterial protein glycosylation, once thought to be a rare event, has now been shown to be widespread. To date multiple general glycosylation systems have been identified yet the precise role in bacterial physiology are still unknown. A common theme is the requirement of glycosylation for persistence/virulence in mammalian hosts. Within this project we aim to explore the role of glycosylation in Burkholderia spp virulence in the mammalian host. By coupling recent innovations in metabolic labeling, redox probes and mass spectrometry workflows we seek to explore how glycosylation influence intracellular survival to increase our understanding of the molecular pathogenesis of Burkholderia.
Dr Nichollas Scott
(03) 8344 6724 | email@example.com
- Laboratory Head
- Immunology, Bacterial and Parasitic Infections, Emerging Infections
- Discovery Research
- Department of Microbiology and Immunology (DMI)
- Lab Group(s):
- Scott group
Dr Nichollas Scott's work focuses on the identification and characterisation of microbial enzymes which chemically link carbohydrates to proteins. Through the addition of carbohydrates to proteins, a process known as protein glycosylation, microbes are able to radically alter the function of proteins. Within a range of infections protein glycosylation is used for both defensive and offensive processes; enabling pathogens to fortify themselves against the host immune response or to disarm the host’s ability to resist infection. By better understanding these systems, the goal of my research aims to develop approaches to target these enzymes for antimicrobial strategies. To achieve this, my work focuses on developing new methodologies to monitor glycosylation, characterising the proteins which are modified by these enzymes and understanding the role of microbial glycosylation systems during pathogenesis.