Dr Jennifer Tomlinson
- Position: Royal Society Dorothy Hodgkin Research Fellow
- Areas of expertise: NMR spectroscopy; structural biology; antibiotic resitance mechanisms; protein-protein interactions; protein dynamics
- Email: J.H.Tomlinson@leeds.ac.uk
- Phone: +44(0)113 343 0991
- Location: 6.02 Miall
I obtained my Royal Society Dorothy Hodgkin Research Fellowship at the University of Leeds in 2018. Before that I was a postdoctoral researcher at the University working in the lab of Dr Alex O'Neill (2010-2017).
I obtained my PhD at the University of Sheffield (2009) in the lab of Prof. Mike Williamson, using NMR to study the effects of pH on protein structure before undertaking a postdoctoral Wellcome Trust VIP fellowship (2009-2010) also at the University of Sheffield using NMR to study intrinsically disordered peptides.
My research is focused on the use of structural biology such as NMR spectroscopy and biophysical techniques to study protein structure and dynamics. I seek to understand the detailed molecular mechanisms of resistance to important clinical antibiotics, particularly those involving allosteric effects and protein dynamics.
The rise in antibiotic resistance is threatening our ability to treat bacterial infections and precipitating a public health crisis. The Chief Medical Officer for England has described it as a 'catastrophic threat' on a par with climate change and terrorism and it has been predicted that without action, antibiotic resistance will overtake cancer as a cause of death by 2050. The lack of new antibiotics in development means that it is important to understand the mechanisms by which bacteria are resistant to the currently available antibiotics in order to try to circumvent these mechanisms and prolong the usefulness of these important antibiotics.
Fusidic acid inhibits bacterial protein synthesis by binding to Elongation Factor G (EF-G) when it is bound to the ribosome and preventing its release. Resistance to fusidic acid is mediated by the protein FusB that binds to EF-G in these stalled complexes and promotes its release. Structural studies have identified a change in the dynamics of EF-G on FusB binding that may be important in the mechanism of resistance (https://www.nature.com/articles/srep19524). My work aims to characterize this mechanism to provide an understanding of how FusB confers antibiotic resistance.<h4>Research projects</h4> <p>Any research projects I'm currently working on will be listed below. Our list of all <a href="https://biologicalsciences.leeds.ac.uk/dir/research-projects">research projects</a> allows you to view and search the full list of projects in the faculty.</p>
- Modulation of antibiotic resistance and protein synthesis by disrupting Elongation Factor G dynamics
- PhD, University of Sheffield, NMR studies of changes in Protein G with pH
- MBiolSci (Hons) Biochemistry, University of Sheffield
<li><a href="//phd.leeds.ac.uk/project/1876-understanding-the-mechanisms-of-fusidic-acid-antimicrobial-resistance">Understanding the mechanisms of fusidic acid antimicrobial resistance</a></li>