Proteomic analysis of a compatible interaction between Pisum sativum (pea) and the downy mildew pathogen Peronospora viciae

Amey, R., Schleicher, T., Slinn, J., Lewis, M., Macdonald, H., Neill, S. and Spencer-Phillips, P. T. (2008) Proteomic analysis of a compatible interaction between Pisum sativum (pea) and the downy mildew pathogen Peronospora viciae. In: Lebeda, A., Spencer-Phillips, P. T. and Cooke, B., eds. (2008) The Downy Mildews - Genetics, Molecular Biology and Control. Springer Netherlands, pp. 41-55. ISBN 978-1-4020-8972-5 Available from:

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A proteomic approach was used to identify host proteins altering in abundance during Peronospora viciae infection of a susceptible cultivar of pea (Pisum sativum cv. Livioletta). Proteins were extracted from fully developed pea leaflets at 4 days post-inoculation, before visible symptoms were apparent. Cytoplasmic proteins and membrane- and nucleic acid-associated proteins from infected and control leaves were examined using two-dimensional difference gel electrophoresis. The majority of proteins had a similar abundance in control and infected leaves; however, several proteins were altered in abundance and twelve were found to have increased significantly in the latter. These proteins were selected for either matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry or electro-spray ionisation quadrupole time-of-flight tandem mass spectrometry analysis following trypsin digestion, with sequence identity being assigned to eight of the proteins. These included the ABR17 stress-response protein, the pathogen-induced PI176 protein, three photosynthetic proteins, a glycine-rich RNA binding protein and two glyceraldehyde 3-phosphate dehydrogenases (cytosolic and chloroplastic) which can be induced by a range of abiotic and biotic stresses in many plant species. The possible roles of these proteins in the response of the pea plant during P. viciae infection are discussed. This study represents the first proteomic analysis of downy mildew infection of pea leaves, and provides the basis for further work to elucidate molecular mechanisms of compatibility in P. viciae infections.

Item Type:Book Section
Uncontrolled Keywords:electrophoresis, DIGE, MALDI-TOF, mass spectrometry, oomycete, protein
Faculty/Department:Faculty of Health and Applied Sciences > Department of Applied Sciences
ID Code:7104
Deposited By: H. Hammond
Deposited On:21 Jul 2010 08:16
Last Modified:15 Nov 2016 20:58

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