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Brian Reavy

Staff picture: Brian Reavy
Cell and Molecular Sciences
Brian.Reavy@hutton.ac.uk
+44 (0)844 928 5428 (*)

The James Hutton Institute
Invergowrie
Dundee DD2 5DA
Scotland UK

Current research interests 

  • Identification and characterisation of plant caspase-like proteases induced by plant pathogens in crop plants.
  • Programmed cell death (PCD) is a process that acts to limit pathogen infection of plants by the death of infected cells. In addition PCD can regulate the growth and development of plants as well as their response to abiotic stresses. Caspases (cysteinyl aspartate-specific proteinases) have a critical role in PCD in animal cells. Work at The James Hutton Institute has identified plant proteins with caspase-like protease activity which are a functional analogue of the animal caspases. Our work aims to identify and characterise caspase activities in crop plants (potato and barley) and understand the function of this activity in the response to pathogen attack in these plants.
  • Improvement of plant transformation technologies.
  • This work aims to utilise the knowledge we have gained from fundamental work on plant responses to pathogens to improve gene transfer and plant regeneration technologies.

Past research 

  • BSc in Molecular Biology University of Glasgow.
  • DPhil University of Oxford. My thesis studied molecular events occuring in the replication of RNA-containing viruses of insects.
  • Post-doctoral research fellow at the Animal Virus Research Institute (now Institute for Animal Health), Pirbright, Surrey studying how to use genetic recombination in foot-and-mouth disease virus to improve production of vaccine strains of the virus.
  • Research Scientist at Beecham pharmaceuticals working on the development of novel recombinant fibrinolytic proteins.
  • Research Scientist at SCRI – during my time at the Institute I have worked on development of transgenic plants resistant to virus infection; the mechanisms of virus-vector interactions with potato leafroll virus/aphids and potato mop-top virus/Spongospora subterranea; assembly of virus ribonuclear particles and virions; molecular mechanisms of gene silencing suppression by plant virus genes.

Bibliography 

  • Reavy, B., Bagirova S., Chichkova N. V., Fedoseeva S. V., Kim S. H., Vartapetian A. B. and Taliansky M. E. 2007. Caspase-resistant VirD2 protein provides enhanced gene delivery and expression in plants. Plant Cell Reports (in press).
  • Reavy, B., Dawson, S., Canto, T. and MacFarlane, S.A. 2004. Heterologous expression of plant virus genes that suppress post-transcriptional gene silencing results in suppression of RNA interference in Drosophila cells. BMC Biotechnology 4, 18.
  • Jones, J. Reavy, B. Smant, G. and Prior A. 2004. Glutathione peroxidases of the potato cyst nematode Globodera rostochiensis. Gene 324, 47-54.
  • Liu, H., Reavy, B., Swanson, M. and MacFarlane, S.A. 2002. Functional replacement of the tobacco rattle virus cysteine-rich protein by pathogenicity proteins from unrelated plant viruses. Virology 298, 232-239.
  • Reavy, B. and Mayo, M.A. 2002. Persistent transmission of luteoviruses by aphids. Advances in Botanical Research 36, 21-46.
  • Racman, D., McGeachy, K., Reavy, B., Štrukelj, B., Zel, J. and Barker, H. 2001. Strong resistance to potato tuber necrotic ringspot disease in potato induced by transformation with coat protein gene sequences from an NTN isolate of Potato virus Y. Annals of Applied Biology 139, 269-275.
  • Mayo, M.A. and Reavy, B. 2000. Sequiviruses. In Encyclopaedia of Plant Pathology. Edited by O.C. Maloy and T.D. Murray, John Wiley and Sons. pp 899-900.
  • Gildow, F.E., Reavy, B., Mayo, M.A., Duncan, G.H., Woodford, J.A.T., Lamb, J.W. and Hay, R.T. 2000. Aphid cell ultrastructure associated with acquisition and transmission by Myzus persicae of Potato leafroll virus-like particles lacking P5 readthrough protein. Phytopathology 90, 1153-1161.
  • Reavy, B., Ziegler, A., Diplexcito, J., Macintosh, S.M., Torrance, L. and Mayo, M. 2000. Expression of functional recombinant antibody molecules in insect cell expression systems. Protein Expression and Purification 18, 221-228.

  • Email: info@hutton.ac.uk
  • Phone: +44 (0)844 928 5428
  • Craigiebuckler Aberdeen AB15 8QH Scotland
  • Invergowrie Dundee DD2 5DA Scotland
A Scottish charitable company limited by guarantee. Registered in Scotland No SC374831.
Registered office: The James Hutton Institute, Invergowrie Dundee DD2 5DA. Charity No SCO41796

Printed from /staff/brian-reavy on 21/09/14 11:10:29 PM

The James Hutton Research Institute is the result of the merger in April 2011 of MLURI and SCRI. This merger formed a new powerhouse for research into food, land use, and climate change.