Edinburgh Research Explorer

Dr Rona Barron

UoE Honorary staff

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Education/Academic qualification

1992Doctor of Philosophy (PhD), University of Edinburgh
Identification and characterisation of a putative serine proteinase from Mycobacterium avium subsp paratuberculosis
1987Bachelor of Science, University of Edinburgh


Dr Barron is a neurobiologist with over 20 years experience in the study of Transmissible Spongiform Encephalopathies (TSEs, or Prion diseases). She completed a BSc in Bacteriology at the University of Edinburgh, and a PhD at the Moredun Research Institute in Edinburgh, characterising a serine proteinase expressed by Mycobacterium avium subsp paratuberculosis. Dr Barron then joined the Institute for Animal Health Neuropathogenesis Unit (NPU) in Edinburgh as a postdoctoral research scientist, and continued at this institution as a Senior Postdoctoral Scientist and Group Leader.  In 2007, the NPU was transferred to the Roslin Institute and The University of Edinburgh, where Dr Barron now holds the post of Reader, and runs a research group examining the nature of the TSE infectious agent, and the role of protein misfolding in neurodegenerative disease.

Dr Barron is a member of Centre for Clinical Brain Sciences, Centre for Dementia Prevention, AR-UK Scotland Network, Scottish Dementia Research Consortium, Society for General Microbiology, British Neuroscience Association, American Society for Microbiology.

Research Interests

Abnormal protein accumulation in neurotoxicity and infection in TSEs and other neurodegenerative diseases.

 The Barron Group performs a programme of research which aims to study the role of protein misfolding in neurodegenerative disease. In particular, the group focus on the relationship between abnormal PrP and the TSE infectious agent. Although the incidence of BSE and vCJD is declining in the UK, concern still exists surrounding subclinical disease in the population, and the associated risk of human-to-human transmission of disease via surgery and blood transfusion. Additionally, new atypical forms of ruminant TSE continue to be identified, and the associated risk of transmission to humans from these agents is still largely unknown. The Barron Group have particular interest in the relationship between abnormal prion protein (PrP) and TSE infectivity, and which specific abnormal PrP conformers may be infectious, neurotoxic or even protective. The group utilises biochemical, transcriptomic and proteomic technologies to examine in vivo and in vitro models of TSE and protein aggregation. The group has received funding from BBSRC, MRC, Defra and FSA.



Nature of the TSE agent. Although misfolded PrP is thought to be the sole component of the TSE infectious agent, the true relationship between abnormally folded forms of PrP and TSE infectivity are still unknown. The Barron Group are examining murine models in which the presence of abnormal PrP and TSE infectivity do not correlate to examine this relationship in more detail and determine whether a specific misfolded conformer may be associated with infectivity, rather than all misfolded aggregated form of the protein. Misfolded PrP can exist as oligomers, protofibrils and amyloid fibrils. Synthetic prions have also been created in vitro by several groups following fibrillisation of recombinant PrP, however these transmit with low efficiency suggesting that not all of the refolded PrP is infectious and a specific refolded conformer or aggregation state is required for disease transmission. Indeed recombinant PrP amyloid fibrils produced in Roslin can seed PrP amyloid accumulation in a transgenic model containing the P101L mutation in PrP, but do not cause TSE or generate TSE infectivity.


Protein misfolding and neurodegeneration. Using in vitro primary neuronal cell culture and whole brain organotypic slice culture the Barron Group are examining how cells respond to challenge with oligomeric or amyloid forms of misfolded protein. We have optimised methods for primary cell culture production and perform detailed analyses of cells using the newly acquired IMARIS software. Whole BOSCs have been maintained in culture for 8 months and fully characterised. We now aim to determine whether amyloid plaques can be seeded in these slices, or if the whole brain network and 3D support is required to sustain plaque production. 


TSE Zoonosis. Sheep scrapie has been present in the environment for several hundred years without a co-current incidence of human TSE disease. It was therefore thought that ruminant TSEs were of little risk to humans. However following the outbreak of bovine spongiform encephalopathy (BSE) in the UK, a new variant of a human TSE (vCJD) was identified. The same TSE strain was responsible for BSE and vCJD, indicating that transmission from cattle to humans (zoonosis) had likely occurred. Using transgenic mice expressing human forms of the prion protein (PrP) we have been modelling the possible risk to humans from other ruminant TSEs. While sheep scrapie (both classical and atypical) did not transmit disease to these mice, BSE infection of sheep did produce an agent that transmitted more efficiently to human PrP transgenic mice than cattle BSE. These data highlight the possible risk to public health if BSE were to enter the sheep population. We continue to monitor new and emerging agents (such as chronic wasting disease in European deer) and assess the risk posed to humans.


Current Research Interests

  • The nature of the TSE infectious agent

  • The relationship between misfolded protein and neurodegeneration

  • PrP amyloid formation and seeding; prion disease or proteinopathy?

  • The role of stress in neurodegeneration

  • Zoonotic transmission of TSE disease

My research in a nutshell

The Barron Group’s research is based around prion diseases, specifically ones such as bovine spongiform encephalopathy (BSE, or Mad Cow Disease). A prion disease is a specific type of disorder in which a protein in the brain (PrP) misfolds and aggregates, and gets deposited in the brain, destroying the brain cells. Or at least that is the hypothesis. There is no a bacterium or virus which is known to cause the misfolding of the protein, which begs the question, exactly what does? It is this question we hope to answer. 

Prion diseases are neurodegenerative diseases. These diseases are invariably fatal and there is no current cure or preventative treatment. Once clinical signs of disease begin to show, death in inevitable. Prion diseases such as BSE have been controlled, not eradicated. Incidence of BSE has declined in the UK, but a handful of cases are still being identified. New atypical forms of BSE and scrapie have been identified over the last decade. Chronic wasting disease (CWD) is a prion disease of deer. This has previously been restricted to North America, but cases have recently been identified in Europe. While these diseases remain in the environment, risks to human and animal health remain.

In our research to identify the cause of disease, we use a technique which involves injecting prion infected brain tissue into the brain of normal or genetically engineered mice. This causes the mouse to become infected and samples can be taken and screened for signs of disease. Brain tissue is taken and examined for specific forms of the prion protein (PrP) which are known to be associated with disease. Normally in prion infected mice a specific misfolded form of PrP can be identified by separation on gels or in slices of brain. This protein is a marker of disease and thought to be the infectious agent. However, samples taken from unusual models of prion disease in the Barron Lab showed little or no evidence of this abnormal form of the prion protein, even though the mice had clinical signs of prion disease. Because diagnostic tests rely on being able to detect abnormal PrP, can these tests always be relied upon? We aim to use these unusual models to identify what is causing disease in these animals, and identify better biomarkers of infection.





This Group is part of the STN and Neuroprion




Research students


Declan King. Part time PhD 2012-2018 (Primary Supervisor. 2nd Supervisor Paul Skehel)

Claire Latta. BBSRC DTP PhD 2016-2020 (2nd supervisor. Primary Supervisor Barry McColl)

Lorena Sordo. Mexican Government PhD Scholarship 2017-2020. (2nd Supervisor. Primary Supervisor Danielle Gunn-Moore)



Collaborative Activity

Tom Wishart, The Roslin Institute, University of Edinburgh. Seeding protein aggregation in whole brain organotypic slice culture. LiCor based imaging and quantitation of protein in tissue sections.

Barry McColl, The Roslin Institute, University of Edinburgh. Role of TREM2 in response to amyloid insult.

Paul Skehel, University of Edinburgh. The response of primary neuronal and glial cultures to protein misfolding and amyloid accumulation/clearance.

Pedro Piccardo, The Roslin Institute, University of Edinburgh. Amyloid seeding and neurodegeneration. Role of Tau in TSE disease.

Andy Gill, The Roslin Institute, University of Edinburgh. Defining prion protein misfolding pathways. In vitro production of recPrP conformers.

Victoria Lawson, University of Melbourne, Australia. PMCA amplification of PrPSc and Infectivity from 101LL/GSS mice.

Bruce Chesebro, RML, Montana, USA. Protein aggregation in PrP-GPI anchorless Tg mice

Byron Caughey, RML, Montana, USA. Analysis of unusual TSE models by QuIC.

Glenn Telling, Colorado State University, Colorado, USA. Amyloid seeding and neurodegeneration

Highlighted research activities & awards

  1. Asian Pacific Prion symposium

    Activity: Participating in or organising an event typesParticipation in conference

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