Kevin Gough
Lecturer in Molecular Biochemistry, Faculty of Medicine & Health Sciences
Contact
Biography
Kevin Gough graduated with a BSc (Hons) in Biochemistry from the University of Wales, Aberystwyth (1992). He then obtained a PhD in Biochemistry from Aberystwyth, graduating in 1996. His post-doctoral employment includes three years as a research associate at The University of Leicester before becoming a Research Scientist with ADAS. Within 8 years at ADAS, his roles progressed through Senior Research Scientist to Principal Research Scientist and Leader of the ADAS Biotechnology Group. Kevin joined the School of Veterinary Medicine and Science in 2007.
Expertise Summary
Kevin Gough is a lecturer in Molecular Biochemistry within the SVMS.
He has acted as an independent scientific expert on appraisal panels for both the Defra TSE Review 2007 and for the Food Standards Agency TSE Research Programme Review 2007.
He has over ten years experience of research in Molecular Biology and Biochemistry. Techniques include: prion diagnostics, recombinant antibody production, protein purification, monoclonal antibody production, diagnostic PCR and Q-PCR, enzyme kinetics and immunoassay development, plant transformation and plant and mammalian tissue culture methods. He also has extensive experience of project and staff management, contract management, bid preparation, results dissemination, business development and commercialisation.
Research Summary
In recent years my research has included studying and developing diagnostics for two significant zoonoses: E. coli O157:H7 and BSE, as well as ovine scrapie, a disease with significant animal health… read more
Selected Publications
MADDISON B.M, BAKER C.A, TERRY L.A, BELLWORTHY S.J and THORNE L, REES H.C. AND GOUGH K.C., 2010. Environmental Sources of Scrapie Prions Journal of Virology. 84, 11560-1562 MADDISON, B.C, REES, H.C, BAKER, C.A, TAEMA, M, BELLWORTHY, S.J, THORNE, L and TERRY, L.A. AND GOUGH, K.C., 2010. Prions are secreted into the oral cavity in sheep with preclinical scrapie Journal of Infectious Diseases. 201, 1672-1676 MADDISON, B.C, BAKER, C.A, REES, H,C, TERRY, L.A, THORNE, L, BELLWORTHY, S.J, WHITELAM G.C and AND GOUGH, K.C., 2009. Prions are secreted in milk from clinically normal scrapie-exposed sheep Journal of Virology. 83, 8293-8296 OWEN, J.P., REES, H.C., MADDISON, B.C., TERRY, L.A., THORNE, L., JACKMAN, R., WHITELAM, G.C. and GOUGH, K.C., 2007. Molecular profiling of ovine prion diseases by using thermolysin-resistant PrP<sup>Sc</sup> and endogenous C2 PrP fragments Journal of Virology. 81(19), 10532-10539
Current Research
In recent years my research has included studying and developing diagnostics for two significant zoonoses: E. coli O157:H7 and BSE, as well as ovine scrapie, a disease with significant animal health and welfare implications.
Prion Diseases. Prion diseases or transmissible spongiform encephalopathies (TSEs) are fatal neurological disorders that are marked by long incubation periods (3-6 years in cattle, up to 30 years in humans). The onset of clinical signs of disease becomes evident only during the last months before death. TSEs have been described in a number of mammalian species and include scrapie in sheep and goats, bovine spongiform encephalopathy (BSE) in cattle, chronic wasting disease in deer and elk and Creutzfeldt-Jakob disease (CJD) in humans. According to the protein only hypothesis, the infectious agent of these diseases is formed by the misfolding of the cellular conformation of the prion protein (PrPC) into a protease-resistant conformation (PrPSc). The cellular prion protein is an apparently benign membrane-bound glycoprotein whose main function remains enigmatic. These diseases are of particular interest for several reasons: They are irreversible and invariably fatal; there is compelling evidence that the BSE agent has crossed the species barrier and is the causal agent of vCJD in humans; the causal agent appears to be novel, an infectious misfolded version of a host protein which encodes transmissible strain characteristics in the absence of any detectable nucleic acid; scrapie is endemic within the UK sheep flock; and, novel scrapie and BSE strains have been identified in recent years and may present new risks to animal and human health. There remain considerable challenges in the diagnoses and understanding of animal TSEs which I am actively investigating. These include elucidation of the routes of scrapie transmission and the environmental fate of the TSE agent, the strain typing of ruminant TSEs to study emerging strains, and the pre-mortem diagnosis of TSE diseases. To date, findings have included experimental evidence of PrPC in milk indicating a potential source of PrPSc transmission, reporting the first description of the disease-associated C2 fragment of PrP within a natural scrapie host, the development of a rapid molecular strain typing assay for ovine TSEs that can readily distinguish ovine scrapie from ovine BSE, and the utilisation of novel ligands for the removal and concentration of scrapie PrPSc from biological matrices.
E. coli O157:H7. We have developed recombinant antibodies that bind to virulence factors of E. coli O157 and are capable of preventing the bacteria's interaction with its host cell. Such virulence factors are vital to the infection of human hosts and are implicit in the carriage of the bacteria within the gut of asymptomatic ruminants, the proposed major reservoir of E. coli 0157 with respect to human health. Our immunoreagents provide novel tools to study these virulence factors and may also provide novel therapeutics for the passive immunization of humans and animals.
Ligand-display technology. For over ten years I have had an active interest in ligand display systems and particularly the display of recombinant antibody fragments and peptides on filamentous bacteriophage. Peptide phage-display libraries have proved useful for mapping epitopes of monoclonal antibodies, and the isolation of ligands that bind specifically to a range of target molecules including proteins and DNA. This technology also allows the isolation of peptides capable of disrupting specific protein-protein interactions. In the form of antibody phage-display libraries this technology is a powerful in vitro technique that allows the selection of antibodies with defined properties from vast libraries of binders. This allows the isolation of antibodies with exquisite selectivity between closely related molecules, and by removing the need for immunization it allows the production of antibodies against toxic or non-antigenic molecules. To date, I have applied protein-display technology to isolate ligands against a wide range of molecular targets from human mast cell surfaces, through prion proteins to plant viruses. This technique will continue to be one of the methodologies applied in my research to improve diagnostics and develop novel therapeutics against veterinary pathogens and zoonoses. Furthermore, advances are being made in display systems for recombinant MHC-peptide complexes; such techniques may be extremely useful in elucidating pathogen stimulation of cellular immunity.