Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

MoPce1, a Cap/PR Domain Containing Effector Is Required for the Pathogenicity of Magnaporthe oryzae by Interacting with the OsDi19-5 in Rice

Huimin Bai
,
Xiaomin Chen
,
Dao Zhou
,
Jiayuan Guo
,
Ting Sun
,
Yuanhao Liu
,
Zecheng Lai
,
Dongmei Zhang
,
Wei Tang
,
Xiuxiu Li
,
Zhenhui Zhong
ORCID logo ,
Guodong Lu
,
Zonghua Wang
* ,
Huakun Zheng
* ORCID logo
Version 1 : Received: 5 November 2023 / Approved: 8 November 2023 / Online: 8 November 2023 (15:52:43 CET)

How to cite: Bai, H.; Chen, X.; Zhou, D.; Guo, J.; Sun, T.; Liu, Y.; Lai, Z.; Zhang, D.; Tang, W.; Li, X.; Zhong, Z.; Lu, G.; Wang, Z.; Zheng, H. MoPce1, a Cap/PR Domain Containing Effector Is Required for the Pathogenicity of Magnaporthe oryzae by Interacting with the OsDi19-5 in Rice. Preprints 2023, 2023110510. https://doi.org/10.20944/preprints202311.0510.v1 Bai, H.; Chen, X.; Zhou, D.; Guo, J.; Sun, T.; Liu, Y.; Lai, Z.; Zhang, D.; Tang, W.; Li, X.; Zhong, Z.; Lu, G.; Wang, Z.; Zheng, H. MoPce1, a Cap/PR Domain Containing Effector Is Required for the Pathogenicity of Magnaporthe oryzae by Interacting with the OsDi19-5 in Rice. Preprints 2023, 2023110510. https://doi.org/10.20944/preprints202311.0510.v1

Abstract

Rice blast fungus (Magnaporthe oryzae) causes massive yield losses annually worldwide. The fungus secreted bunch of effector proteins target different rice cellular compartments to facilitate its infection. However, most of intensively studied effectors are small secreted proteins with high presence/absence polymorphism in the fungus, and effectors conserved among different species were rarely investigated. In this study, we identified MoPce1, a CAP/PR domain containing protein common in different species, as an important virulence factor from a screening of 145 putative core effectors (PCE). MoPCE1 is required for pathogenicity but not the asexual development. Ectopic expression of MoPCE1sp in ZH11 background compromised the plant resistance. We also found that MoPce1 lacks the conserved cysteine residuals in CAP domain, and is BIC-localized in invasive hyphae and nuclei-localized when ectopically expressed in tobacco leaves and rice protoplasts. These results suggested that MoPce1 may bind novel ligand(s) rather than sterol. Indeed, we found that MoPce1 could interact with OsDi19-5, a transcription factor in rice. We inferred from these results that MoPce1 is required for pathogenicity by suppressing the immune response in rice, likely through the interaction with OsDi19-5.

Keywords

MoPCE1; CAP domain; effector; pathogenicity; OsDi19-5

Subject

Biology and Life Sciences, Immunology and Microbiology

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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