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Defining the protein modifications associated with respiratory disease
Project details
The composition of pulmonary mucus, which is secreted to protect the airways, changes with the onset of respiratory diseases like asthma, COPD and IPF. These changes are relatively well-understood at the protein level but it is less clear how the post-translational modifications of these proteins changes with the onset of disease. We and others have shown that these post-translational modifications, particularly O-glycosylation, plays a defining role in the function of these mucosal proteins (Goddard-Borger, Nature Communications, 2020, doi:10.1038/s41467-020-16223-7). This highlights the importance of investigating how mucosal protein modifications differ in respiratory diseases.
This project will focus on the development of tools and methods to characterise the post-translational modifications of mucosal proteins. It is an excellent opportunity for those interested in protein science and/or proteomics.
About our research group
Many proteins are modified by diverse and complex glycan molecules, which modulate protein folding, trafficking, half-life and function. The Goddard-Borger Lab studies the role of these modifications, as well as the proteins that read, write and erase them, in diseases as diverse as malaria (Goddard-Borger and Boddey, Nature Communications, 2017, doi.org/10.1038/s41467-017-00571-y), COVID-19 (Williams & Goddard-Borger, Biochemical Society Transactions, 2020, doi:10.1042/BST20200505) and other respiratory diseases (Goddard-Borger, Nature Communications, 2020, doi:10.1038/s41467-020-16223-7).
We use chemical, molecular and structural biology techniques to do this, which provides students an opportunity to gain practical skills in all of these fields with a high level of support from senior researchers. We collaborate extensively and welcome individuals who want to work as part of a diverse team to achieve significant research goals.
(Goddard-Borger, Nature Communications, 2020, doi:10.1038/s41467-020-16223-7),
illustrating how post-translational modifications can define interactions between mucosal proteins.