The role of a cytosolic superoxide dismutase in barley-pathogen interactions
Online Publication Date2016-07-17
Print Publication Date2017-04
Permanent link to this recordhttp://hdl.handle.net/10754/625029
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AbstractReactive oxygen species (ROS), including superoxide (O2-HO2) and hydrogen peroxide (H2O2), are differentially produced during resistance responses to biotrophic pathogens and during susceptible responses to necrotrophic and hemi-biotrophic pathogens. Superoxide dismutase (SOD) is responsible for the catalysis of the dismutation of O2-HO2 to H2O2, regulating the redox status of plant cells. Increased SOD activity has been correlated previously with resistance in barley to the hemi-biotrophic pathogen Pyrenophora teres f. teres (Ptt, the causal agent of the net form of net blotch disease), but the role of individual isoforms of SOD has not been studied. A cytosolic CuZnSOD, HvCSD1, was isolated from barley and characterized as being expressed in tissue from different developmental stages. HvCSD1 was up-regulated during the interaction with Ptt and to a greater extent during the resistance response. Net blotch disease symptoms and fungal growth were not as pronounced in transgenic HvCSD1 knockdown lines in a susceptible background (cv. Golden Promise), when compared with wild-type plants, suggesting that cytosolic O2-HO2 contributes to the signalling required to induce a defence response to Ptt. There was no effect of HvCSD1 knockdown on infection by the hemi-biotrophic rice blast pathogen Magnaporthe oryzae or the biotrophic powdery mildew pathogen Blumeria graminis f. sp. hordei, but HvCSD1 also played a role in the regulation of lesion development by methyl viologen. Together, these results suggest that HvCSD1 could be important in the maintenance of the cytosolic redox status and in the differential regulation of responses to pathogens with different lifestyles.
CitationLightfoot DJ, Mcgrann GRD, Able AJ (2016) The role of a cytosolic superoxide dismutase in barley-pathogen interactions. Molecular Plant Pathology 18: 323–335. Available: http://dx.doi.org/10.1111/mpp.12399.
SponsorsThis work was partially funded by the Grains Research and Development Corporation (CMB0009) and the Molecular Plant Breeding Cooperative Research Centre. GRDM was supported by the Biotechnology and Biological Sciences Research Council (BBSRC) Biotic Interactions Strategic Programme grant reference BBJ004553/1. Thanks are due to Rohan Singh, Alan Little and Nigel Percy for technical assistance with the development of the knockdown lines, GFP localization and SOD activity assays, respectively. The authors have no conflicts of interest to declare.
JournalMolecular Plant Pathology