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

Abstract

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 electrospray 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.

Primary style protein expression in the self-incompatible/compatible apricot by the 2D-DIGE technique

“…This technology has furthered research of the physiological and biochemical aspects of plants exposed to biological and abiotic stress; e.g. proteomics research (Zhen et al, 2008) has been used to examine the effects of stress in Arabidopsis thaliana (Amme et al, 2006) and the compatible interaction in Pisum sativum (Amey et al, 2008). However, there is no report of research related to plant SC proteins.…”

Boron deficiency results in induction of pathogenesis-related proteins from the PR-10 family during the legume–rhizobia interaction

“…PR10 proteins, including ABR17, are induced in pea (Amey et al, 2008) and in other legumes (Broderick et al, 1997;Nyamsuren et al, 2003;Colditz et al, 2004) in response to pathogens. Nevertheless, not all PR10 proteins are induced in response to pathogens.…”

Proteomic studies of phytopathogenic fungi, oomycetes and their interactions with hosts

“…Catalogued host (pea) leaf proteins, which showed alternation in their abundance levels during a compatible interaction with P. viciae (Amey et al 2008). …”

“…Among these proteins were disease resistance response protein PI176 (PR-10 family), abscisic acid responsive protein ABR17 (PR-10 family), three photosynthetic proteins, a glycine-rich RNA binding protein and, cytosolic and chloroplastic glyceraldehyde 3-phosphate dehydrogenases. These proteins are implicated in triggering defence responses, signal transduction, protein turnover, and photosynthesis (Amey et al 2008).…”