Post-translational modifications (PTMs) are modifications to amino acids on a protein following translation, which can vastly increase the functionality of a single gene product. Examples of PTMs include phosphorylation or glycosylation, involving addition of a phosphate or carbohydrate group(s), respectively. PTMs play an important role in a range of important cellular functions, enabling cells to respond to internal and external events through dynamic control of protein function. Viruses are obligate intracellular parasites that utilize host cell machinery to replicate. They hijack host cell PTM machinery and PTMs have been widely shown to influence virus-host interplay through proviral and antiviral mechanisms.
This PhD project aims to investigate the role of understudied PTMs derived from cellular metabolic pathways during infection of clinically important respiratory viruses e.g., RSV, Influenza and SARS-CoV-2.
One such PTM is O-GlcNAcylation, which is different to most other types of glycosylation, as it involves just a single O-linked N-acetylglucosamine (O-GlcNAc) sugar that can be transiently added or removed from cytoplasmic, nuclear and mitochondrial proteins. The GlcNAc moiety is derived from the cellular hexosamine biosynthesis pathway, which is interconnected to glycolysis and glucose metabolism, and therefore the modification likely plays a role in nutrient sensing. O-GlcNAcylation has been linked to a multitude of cellular functions including innate immunity, which is an important cellular host defence response to viral infections. Therefore, this PhD project will investigate the link between O-GlcNAcylation, immunometabolism and respiratory virus infection. O-GlcNAcylation is understudied compared to other PTMs, especially in virus infection, and therefore this area is open for new and exciting discoveries.
During this PhD, the candidate will receive truly interdisciplinary training in four key disciplines: virology, cell biology, molecular biology and biochemistry. The candidate will work with a range of respiratory viruses and learn skills in cell culture (including primary cells), microscopy, gene manipulation techniques, and use of chemical biology tools.
The project is collaborative, supervised by Dr Catherine Adamson and Dr Tracey Gloster. Dr Adamson has extensive experience in virology and Dr Gloster a biochemist who specialises in glycobiology including O-GlcNAcylation. Both supervisors are members of the Biomedical Sciences Research Complex (BSRC) at the University of St Andrews. The BSRC offers a state-of-the art research environment, including world-class mass spectrometry/proteomics facilities, virus containment labs, and microscopy suite, in recently renovated labs, housing groups with common interests in biomedical and infectious disease research.
We strongly encourage informal enquiries by email: csa21@st-andrews.ac.uk and tmg@st-andrews.ac.uk.
HOW TO APPLY
Application instructions can be found on the EASTBIO website- How to Apply | EastBio Doctoral Training Partnership | Biology
1) Download and complete the Equality, Diversity and Inclusion survey.
2) Download and complete the EASTBIO Application Form.
3) Please complete an application on our online portal: How to apply - Study at St Andrews - University of St Andrews
4) Select the course ‘PhD with internship’
5) Your online application must include the following documents:
- Completed EASTBIO application form
- Academic Qualifications
- English Language Qualification (if applicable)
- 2 References: this must be completed on the EASTBIO Reference Form, also found on the EASTBIO website.
Please download the EASTBIO reference form and send it to your referees. They can either upload it directly to the portal using the automated email they will receive, or they can email it to Rachel at pgrecbiology@st-andrews.ac.uk
CONTACT
Queries on the project can be directed to the project supervisor.
Queries on the application process can be directed to Rachel Horn at pgrecbiology@st-andrews.ac.uk
UKRI eligibility guidance: Terms and Conditions: View Website International/EU: View Website