Endo‐1,4‐beta‐xylanase 1 (MoXYL1) secreted by Magnaporthe oryzae triggers defense responses and induces cell death in rice

Author:

Lee Gi Hyun1,Min Cheol Woo1,Yoo Ju Soon1,Jang Jeong Woo1,Yoon Jinmi2,Cho Lae‐Hyeon1,Wang Yiming3,Jeon Jong‐Seong4,Gupta Ravi5,Kim Sun Tae1ORCID

Affiliation:

1. Department of Plant Bioscience, Life and Industry Convergence Research Institute Pusan National University Miryang South Korea

2. Department of Biological Sciences and Bioengineering Inha University/Industry‐Academia Interactive R&E Center for Bioprocess Innovation, Inha University Incheon South Korea

3. Key Laboratory of Integrated Management of Crop Disease and Pests, Ministry of Education, Department of Plant Pathology Nanjing Agricultural University Nanjing China

4. Graduate School of Green‐Bio Science and Crop Biotech Institute Kyung Hee University Yongin Korea

5. College of General Education Kookmin University Seoul South Korea

Abstract

AbstractThe rice blast fungus Magnaporthe oryzae devastates cultivated rice (Oryza sativa L.), causing extensive crop losses. Despite being a major pathogen, information on this pathosystem, especially on the proteins associated with fungal pathogenicity and host defense response, is relatively scarce. Utilizing liquid chromatography‐mass spectrometry (LC–MS/MS), we identified 123 in planta‐secreted M. oryzae proteins in rice leaves and screened for their cell death‐inducing activity. Biochemical characterization of these M. oryzae proteins revealed an endo‐1,4‐beta‐xylanase (MoXYL1), which induces cell death in Nicotiana benthamiana leaves and H2O2 accumulation in rice suspension‐cultured cells. Transgenic rice plants (PDUF26::MoXYL1) expressing MoXYL1 driven by rice DOMAIN OF UNKNOWN FUNCTION PROTEIN 26 (DUF26) promoter enhanced expression of pathogen‐responsive and hormone‐related genes, and resistance to the M. oryzae and Cochliobolus miyabeanus. Data‐independent acquisition (DIA) MS‐based proteomics of wild‐type and PDUF26::MoXYL1 rice revealed 1,833 significantly modulated rice proteins upon M. oryzae infection. Among these, 219 proteins showed a significant increased abundance exclusively in PDUF26::MoXYL1 transgenic rice, while 410 proteins showed increased abundance in both wild‐type and PDUF26::MoXYL1. Notably, xylanase inhibitor proteins, pathogenesis‐related proteins, and other proteins associated with jasmonic acid biosynthesis exhibited increased abundance in response to M. oryzae. Based on these results, we proposed a putative signaling network induced by MoXYL1 and M. oryzae. In summary, our findings highlight the crucial role of MoXYL1 in inducing rice defense and in potentially enhancing rice disease resistance against fungal pathogens.

Funder

National Research Foundation

Publisher

Wiley

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