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Department of Veterinary Medicine

Cambridge Veterinary School

Studying at Cambridge


Dr Alana Thackray

Dr Alana Thackray

Senior Research Associate in Molecular Pathology

Alana Thackray is accepting applications for PhD students.

Office Phone: +44 (0)1223 339019

Subject groups/Research projects

Infection and Immunity:

Departments and Institutes

Cambridge Neuroscience:

Research Interests

My basic research interests are concerned with molecular pathology, diagnosis and therapy of conventional and non-conventional pathogens, including viruses and prions. I am currently investigating the molecular nature of the infectious prion agent associated with transmissible spongiform encephalopathies such as scrapie of sheep, BSE of cattle and CJD of humans. I am interested in the interactions of pathogens with the immune system, in particular, peripheral prion pathogenesis and prion neuroinvasion. Analysis of the biochemical pathways associated with ovine prion formation, clearance, and neurotoxicity will be helped by the application of new tractable animal models of this condition. Use of a genetically well-defined host will allow identification of genetic modifiers of ovine prion disease pathogenesis, providing the potential for development of new diagnostic markers and therapeutic targets for prion diseases in general. The fruitfly Drosophila melanogaster has been used to model a number of human neurodegenerative diseases and a major strength of Drosophila model systems is the ability to rapidly generate transgenic flies that express heterologous proteins in a tissue-specific manner. Genetic pathways are extensively conserved between mammalian and Drosophila genomes, which allows fly models of neurodegenerative disease to identify candidate genetic modifiers of the condition in the host species. At present, we are investigating Drosophila as a new animal model of ovine scrapie in order to provide a more tractable invertebrate model of transmissible mammalian prion disease. My research work has involved the generation of novel anti-PrP monoclonal antibodies to probe the structure of PrPC and PrPSc; the generation of recombinant PrP protein for biophysical and biochemical analysis and resultant computational modelling to predict prion protein structure. In addition, my projects involve the use of novel gene knock-out and transgenic mice, cell culture, flow cytometry, immunohistochemistry, in situ hybridisation, RT-PCR, SDS-PAGE, western blotting, protein misfolding cyclic amplification (PMCA), conformational-dependent immunoassays (CDI) and more recently confocal microscopy. I am actively involved in the development and commercialisation of molecular reagents for prion research and a prion diagnostic test. I also have considerable experience in research into the pathogenesis and chemotherapy of herpes viruses both in vivo and in vitro, using prophylactic and therapeutic strategies.

Main collaborators

  • Dr Jan Felix Evers: University of Cambridge, UK
  • Dr Matthias Landgraf: University of Cambridge, UK
  • Professor Michael Klein: University of Würzburg, Germany
  • Professor Man-Sun Sy: Case Western Reserve University, Cleveland, USA
  • Dr Mark Zabel: Colorado State University, USA
  • Dr David Burke: University of Cambridge, UK
  • Dr John Spiropoulos: AHVLA, Weybridge, UK


  • Drosophila
  • Prion
  • Transmissible spongiform encephalopathies
  • Protein misfolding
  • PrP


Key Publications

Thackray AM, Di Y, Zhang C, Wolf H, Pradl L, Vorberg I, Andréoletti O & Bujdoso R. (2014). Prion-induced and spontaneous formation of transmissible toxicity in PrP transgenic Drosophila. Biochemical Journal. 463: 31-40

Yang S, Thackray AM, Hopkins L, Monie TP, Burke D & Bujdoso R. (2014). Polymorphisms at amino acid residues 141 and 154 influence conformational variation in ovine PrP. Biomedical Research International. doi: 10.1155/2014/372491. 1-14

Thackray AM, Zhang C, Arndt T & Bujdoso R. (2014). Cytosolic PrP can participate in prion-mediated toxicity. Journal of Virology. 88(14): 8129-8138

Bujdoso R & Thackray AM. (2013) The emergence of a Drosophila model to measure ovine prion infectivity. CAB Reviews: Perspectives in Agriculture, Veterinary Science, Nutrition and Natural Resources, 8.  Article ID 0058, doi: 10.1079/PAVSNNR20130058

Li W, Bell NAW, Hernández-Ainsa S, Thacker VV, Thackray AM, Bujdoso R & Keyser UF. (2013). Single protein molecule detection by glass nanopores. ACS Nano. 7(5): 4129-4134

Thackray AM, Lockey R, Beck KE, Spiropoulos J. & Bujdoso R. (2012). Evidence for co-infection of ovine prion strains in classical scrapie isolates. Journal of Comparative Pathology. doi:10.1016/j.jcpa.2012.01.009 [PubMed]

Thackray AM, Muhammad F, Zhang C, Di Y, Jahn TR, Landgraf M, Crowther DC, Evers JF. & Bujdoso R. (2012). Ovine PrP transgenic Drosophila show reduced locomotor activity and decreased survival. Biochemical Journal. doi:10.1042/BJ20112141[PubMed]

Thackray AM, Muhammad F, Zhang C, Denyer M, Spiropoulos J, Crowther DC. & Bujdoso R. (2012). Prion-induced toxicity in PrP transgenic Drosophila. Experimental & Molecular Pathology. 92:194-201.[PubMed]

Thackray AM, Hopkins L, Lockey R, Spiropoulos J. & Bujdoso R. (2012). Propagation of ovine prions from "poor" transmitter scrapie isolates in ovine PrP transgenic mice. Experimental & Molecular Pathology. 92:167-174.[PubMed]

Thackray AM, Hopkins L, Lockey R, Spiropoulos, J. & Bujdoso, R. (2011). Emergence of multiple prion strains from single isolates of ovine scrapie. Journal of General Virology. 92: 1482-1491.[PubMed]

Thackray AM, Hopkins L, Spiropoulos J. & Bujdoso R. (2008). Molecular and transmission characteristics of primary-passaged ovine scrapie isolates in conventional and ovine PrP transgenic mice. Journal of Virology. 82: 11197-11207.[PubMed]

Yang S, Thackray AM, Fitzmaurice TJ. & Bujdoso R. (2008). Copper-induced structural changes in the ovine prion protein are influenced by a polymorphism at codon 112. Biochimica et Biophysica Acta. 1784:683-692.[PubMed]

Thackray AM, Hopkins L, Klein MA. & Bujdoso R. (2007). Mouse-adapted ovine scrapie prion strains are characterized by different conformers of PrPSc. Journal of Virology. 81: 12119-12127.[PubMed]

Thackray AM, Fitzmaurice TJ, Hopkins L. & Bujdoso R. (2006). Ovine plasma prion protein levels show genotypic variation detected by C-terminal epitopes not exposed in cell-surface PrPC. Biochemical Journal. 400: 349-358.[PubMed]

Thackray AM, Ryder SJ. & Bujdoso R. (2005). Modification of blood cell PrP epitope exposure during prion disease. Biochemical Journal. 390: 563-571.[PubMed]

Thackray AM, Yang S, Wong E, Fitzmaurice T, Morgan-Warren R, & Bujdoso R. (2004). Conformational variation between allelic variants of ovine cell surface prion protein. Biochemical Journal. 381: 221-229.[PubMed]

Thackray AM, Madec J-Y, Wong E, Morgan-Warren R, Brown D, Baron T. & Bujdoso R. (2003). Detection of bovine spongiform encephalopathy, ovine scrapie prion-related protein (PrPSc) and normal PrPC by monoclonal antibodies raised to copper-refolded prion protein. Biochemical Journal. 370: 81-90.[PubMed]

Shaw MM, Gürr WK, Thackray AM, Watts PA, Littler E. & Field HJ. (2002). Temporal pattern of herpes simplex virus type 1 infection and cell death in the mouse brain stem: influence of guanosine nucleoside analogues. Journal of Virological Methods. 102: 93-102.[PubMed]

Thackray AM, Klein MA, Aguzzi A. & Bujdoso R. (2002). Chronic subclinical prion disease induced by low dose inoculum. Journal of Virology. 76: 2510-2517.[PubMed]

Thackray AM, Knight R, Haswell SJ, Bujdoso R. & Brown DR. (2002). Metal imbalance and compromised antioxidant function are early changes in prion disease. Biochemical Journal. 362: 253-258 [PubMed]