... understanding life in molecular detail

Welcome to the Asbury Centre Fellowship page.

The Asbury Centre provides an exciting, vibrant and progressive environment for researchers. We are passionate about our prestigious fellowships and the opportunities surrounding these with excellent career prospects in all of our research areas. Below you will find information about our current fellows, their independently funded fellowships and their work within the Astbury Centre. We actively support and encourage all of our fellows as their research is vital to the progression of the centre and the future of Structural Molecular Biology.

   Externally funded Fellows

The Astbury Centre is delighted to have the following Research Fellows as members of the Centre. We are happy to receive requestes from anyone interested in writing a fellowship, short of long term, to join the Centre. Information about fellowships, including the prestigious University of Leeds Academic Fellowships can be found here. Please contact us at l.v.gray@leeds.ac.uk.


Photo of Peter Adams

Dr Peter Adams

University Academic Fellow (January 2015 - August 2020)

Dr Peter Adams was awarded a University Academic Fellowship (Aug 2015 - Aug 2020) and recently completed a BBSRC Anniversary Future Leader Fellowship (Jan 2015 - Jan 2018), which ran concurrently, joining the Molecular and Nanoscale Physics group at the University of Leeds (School of Physics and Astronomy). His research involves understanding the organisation and biophysics of natural and re-designed photosynthetic systems. Multi-disciplinary approaches are followed, including protein biochemistry, spectroscopy, surface chemistry, nano/micro fabrication and various microscopies (TEM, AFM, fluorescence). Novel 3-D arrangements of membranes containing spinach light-harvesting proteins in defined protein compositions and arrangements are under development. These controlled model ‘light-harvesting’ membranes will act as a platform to test the factors influencing self-assembly, organisation and function in biological membranes and lead towards new bio/nano-devices.

Photo of Alexander  Borodavka

Dr Alexander Borodavka

Sir Henry Wellcome Postdoctoral Fellowship (April 2014 - March 2019)

Alex was awarded a Sir Henry Wellcome fellowship to study rotaviruses. Rotaviruses (RVs) cause an estimated 23 million outpatient visits and over 500,000 deaths annually among children under 5 years old. Rotaviruses possess segmented genomes, comprising 11 distinct double-stranded RNA molecules that are packaged into each virion. There is as yet no plausible model explaining the highly efficient mechanism of this molecular process. Understanding this fundamental biological problem will yield novel, attractive RV drug targets, as this is a virus-specific process and infectivity requires all 11 segments. I use single molecule fluorescence techniques combined with a search for high affinity RNA structural motifs involved in segment assortment using various biochemical and biophysical techniques. Ultimately the identified intersegment RNA interactions will be probed in RV-infected cells. These results will help to improve our understanding of how RVs achieve such tightly regulated genome packaging, identify potential novel antiviral targets, as well as reveal new insights into development of a helper-virus free RV reverse genetics system.

Photo of Juan Fontana

Dr Juan Fontana

University Academic Fellow (April 2016 - March 2021)

Juan was awarded a University Academic Fellowship to start his independent research group at the School of Molecular and Cellular Biology. His research is focused in understanding how enveloped viruses, like Influenza and Herpes Simplex Virus, enter the host cell. To this end he takes advantage of cryo-electron microscopy techniques, which allow visualisation of viruses at the molecular level, integrated with other approaches. This research will expand the understanding of enveloped viral fusion and will enable the discovery of new drug targets or vaccine candidates to block infection by enveloped viruses.

Photo of Elisabtta Gropelli

Dr Elisabtta Gropelli

Astbury Fellow Member, Medical Research Foundation Funding (June 2018 – May 2021)

Elisabetta’s research aims to elucidate the molecular mechanism whereby viruses initiate infection. She focuses on the Picornaviridae, a large family of human and animal pathogens, which includes poliovirus, hepatitis A virus, the human rhinoviruses and foot-and-mouth disease virus. Elisabetta investigates the fundamental and irreversible steps that picornaviruses use to deliver their genetic information (RNA) into the host-cell. This is a crucial but poorly understood mechanism that underpins viral infection and that, therefore, may be target of a potent therapeutic intervention. Elisabetta has shown that poliovirus uses a highly coordinated strategy to deliver its RNA genome into the host-cell cytoplasm. Indeed, the viral RNA is extruded from the capsid and across lipid membranes via a protective “umbilicus” formed by viral proteins and cellular lipids. Elisabetta has been awarded Medical Research Foundation funding to investigate hepatitis A virus initiation of infection using cellular and molecular biology in combination with structural biology approaches.

Photo of Glyn Hemsorth

Dr Glyn Hemsorth

BBSRC David Phillips Fellow and University Academic Fellow (September 2016 - August 2021)

Industrial biotechnology is one of the most promising approaches to reducing pollution, conserving resources and reducing the costs incurred during the manufacture of many of the chemical precursors and fuels upon which we rely. This approach aims to utilize enzymes or microorganisms to generate new bio-based products from renewable raw materials. A major challenge for research in this context is to unlock the sugars contained in plant cell walls to be utilized for biofuels and other high value chemical precursor manufacture. Research in Dr Hemsworth’s laboratory seeks to combine approaches from bioinformatics, structural biology, enzymology, and enzyme engineering to probe and exploit natural electron transport processes to activate a recently identified family of enzymes known as Lytic Polysaccharide Monooxygenases (LPMOs). These copper dependent oxidases have emerged as key players in both the natural and applied breakdown of biomass. Understanding how LPMOs are activated will, therefore, be key to optimizing the efficiency of enzymatic biomass conversion and maximizing the lifetime of the reaction mixtures used in these processes.

Photo of Vajinder Kumar

Dr Vajinder Kumar

Marie-Sklodowska Curie Individual Fellowship (April 2018 - March 2020)

Dr. Vajinder Kumar was awarded a Marie-Sklodowska Curie individual fellowship to study shiga like toxins and synthesis glycoproteins to inhibit this toxin. There are 1.7 billion cases of diarrhoeal diseases each year leading to the deaths of 760,000 children under five years old. Many of these deaths are caused by bacteria that produce protein toxins. The 2011 European outbreak of a highly virulent enterohaemorrhagic shiga toxin-producing E. coli O104:H4, demonstrated that toxigenic, multi-antibiotic-resistant bacteria pose an equal and on-going threat to both the developed and developing world. Food poisoning associated with E. coli O157:H7 and O104:H4, arises from production of a Shiga-like toxin that initially causes diarrhoea, which turns bloody after a few days and then subsequently leads to kidney failure: so called haemolytic uremic syndrome (HUS). There is no current specific treatment for HUS; only supportive care can be provided. A particular challenge with treating infections of shiga toxin-producing E. coli with antibiotics is that in some cases the bacteria respond by increasing expression of toxins doing further harm to their host. However, during an E. coli outbreak, there is a window of opportunity for each patient between initiation of diarrhoea and onset of HUS in which a drug could be administered intravenously to prevent the toxin from damaging the kidney. So, he is synthesizing some glycoprotein inhibitors and will evaluate these glycoproteins against the toxin that can stop the toxin’s action and prevent this debilitating disease.

Photo of Jamel Mankouri

Dr Jamel Mankouri

Royal Society University Research Fellow (October 2011 - October 2019)

Viruses are intracellular parasites whose pathogenicity is dependent on the interaction with susceptible cells. To persist they must change host cell physiology to avoid immune detection and utilize the host cell biochemical machinery to create an environment favourable for viral survival. Research in Dr Mankouri's laboratory focuses on understanding the interaction between clinically important human viruses with cellular ion channels. The research aims to understand how viruses modulate ion channel function and investigates the effects of restoring the function of virus-ion channel targets using pharmacological activators/inhibitors on the virus lifecycle. These studies will allow a better understanding of the host cell processes that viruses require in order to survive.

Photo of Takashi Ochi

Dr Takashi Ochi

University Academic Fellow (September 2018 to August 2023)

My research focuses on understanding the architectures of centrosomes and basal bodies. I use structure-biology techniques cryo-electron microscopy and X-ray crystallography as well as biochemistry, biophysics and cell biology to determine structures and functions of the organelles.

Photo of Nikesh Patel

Dr Nikesh Patel

Astbury Fellow Member, Medical Research Foundation Funding (May 2018 – April 2021)

Nikesh was awarded a Medical Research Foundation funding to investigate the replication of Hepatitis B Virus (HBV). It is estimated that over 2 billion people have been infected by HBV, with >350 million of these becoming chronic carriers due to the inability of their immune systems to clear the virus. HBV causes ~ 900k deaths annually worldwide, illustrating its status as an unmet medical target. The replication of the HBV genome is an obligate step in its lifecycle, but occurs within the confines of its nucleocapsid (NC). As such it is yet to be experimentally interrogated. By using single molecule techniques, Cryo-Electron Microscopy and X-Ray Footprinting, upon actively replicating HBV NC, we should gain a deeper mechanistic and structural understanding of HBV replication, potentially highlighting novel drug targets.

Photo of Akshath Uchangi  Satyaprasad

Dr Akshath Uchangi Satyaprasad

Marie-Curie Fellowship (June 2018 - June 2020)

Understanding the structural mechanisms in multivalent interactions is key to design glycoconjugates that can block viral interactions, thereby preventing infection. Despite 17 years of extensive research, the structure of two vitally important tetrameric lectins, DC-SIGN and DC-SIGNR, remain unknown. These lectins bind to virus surface multiple glycans and enhance many viral infections (e.g. HIV, HCV and Ebola). My work will address this challenge by developing a novel multimodal readout strategy (e.g. FRET, TEM and particle size analysis) using compact polyvalent glycan-quantum dots (QD) to fully exploit multivalency and QD’s unique properties. By tuning QD surface glycan structure, valency, inter-glycan spacing and flexibility, we will create a perfect spatial & orientation match to those of glycan-binding-domains (CRDs) in DC-SIGN/R, leading to greatly enhanced binding affinity. By studying QD-glycan binding with DC-SIGN/R, we will reveal key structural data (e.g. CRD orientation, distance, binding mode) in DC-SIGN/R. We will verify the binding data with native receptors on cell surfaces, correlate receptor binding affinity with virus inhibition potency, and study their immune cell-activation.

Photo of Jennifer Tomlinson

Dr Jennifer Tomlinson

Royal Society Dorothy Hodgkin Research Fellowship (January 2018 - December 2022)

Jennifer was awarded a Dorothy Hodgkin Fellowship by the Royal Society to study the role of allostery and protein dynamics in antibiotic resistance. The rise in antibiotic resistance is threatening our ability to treat bacterial infections and without action it has been predicted that antimicrobial resistance will overtake cancer as a cause of death by 2050. To try to overcome existing resistance mechanisms we need to understand them in molecular detail. Jennifer’s research makes use of NMR spectroscopy along with other biochemical and biophysical techniques to characterize the mechanisms of resistance to two clinically important antibiotics for which allostery and dynamics are important. This research will give a detailed understanding of a novel antibiotic resistance mechanism and may also identify druggable ‘hot spots’ to try to disrupt the resistance.

Photo of Megan Wright

Dr Megan Wright

University Academic Fellow (September 2016 - August 2021)

Megan was awarded a University Academic Fellowship to start her independent research group in the School of Chemistry. Her research is in the area of chemical biology, applying novel chemical tools to understand protein function and interaction with small molecules. Her work focuses on probing pathways and global cellular regulatory mechanisms in diverse systems (e.g. apoptosis, protein post-translational modification, bacterial quorum sensing) and elucidating the mode of action of cell-cell signals at the host-pathogen interface. This research employs a wide range of methods, including organic and peptide synthesis, protein biochemistry, and global and chemical quantitative mass spectrometry-based proteomics.

Photo of Qian Wu

Dr Qian Wu

University Academic Fellow (September 2018 to August 2023)

Our lab is interested in understanding the molecular mechanism of pathways involved in human DNA damage response and repair. We study DNA double-strand breaks (DSBs), which are the most toxic damages in cells. We use structural biology as the main tool to determine the architecture of large protein assemblies function at the damaged DNA ends. This will enable us to identify suitable targets to develop small molecule compounds or protein peptides that modulate the DNA damage response and repair signalling for future drug discovery and medical applications.

Photo of Elton Zeqiraj

Dr Elton Zeqiraj

Sir Henry Dale and University Academic Fellow (August 2016 - July 2021)

Elton was awarded a Sir Henry Dale Fellowship by the Wellcome Trust and the Royal Society to study how the small molecule ubiquitin governs cell signalling networks. Elton’s lab is also supported by a University Academic Fellowship from the University of Leeds. The laboratory uses structural biology, biophysics and enzymology techniques to study deubiquitinating enzymes (a.k.a. DUBs). The majority of the lab’s efforts are dedicated towards understanding how DUBs are activated allosterically and how they can be inhibited when it is beneficial to do so.