A poplar rust effector protein associates with protein disulfide isomerase and enhances plant susceptibility


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Madina, Mst Hur, Rahman, Md Saifur, Huang, Xiaoqiang, Zhang, Yang, Zheng, Huanquan et Germain, Hugo (2020). A poplar rust effector protein associates with protein disulfide isomerase and enhances plant susceptibility. Biology, 9 (9). pp. 1-20. ISSN 2079-7737 DOI 10.3390/biology9090294

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Melampsora larici-populina (Mlp), the causal agent of Populus leaf rust, secretes an array of effectors into the host through the haustorium to gain nutrients and suppress immunity. The precise mechanisms by which these effectors promote virulence remain unclear. To address this question, we developed a transgenic Arabidopsis line expressing a candidate effector, Mlp124357. Constitutive expression of the effector increased plant susceptibility to pathogens. A GxxxG motif present in Mlp124357 is required for its subcellular localization at the vacuolar membrane of the plant cell, as replacement of the glycine residues with alanines led to the delocalization of Mlp124357 to the nucleus and cytoplasm. We used immunoprecipitation and mass spectrometry (MS) to identify Mlp124357 interaction partners. Only one of the putative interaction partners knock-out line caused delocalization of the effector, indicating that Arabidopsis protein disulfide isomerase-11 (AtPDI-11) is required for the effector localization. This interaction was further confirmed by a complementation test, a yeast-two hybrid assay and a molecular modeling experiment. Moreover, localization results and infection assays suggest that AtPDI-11 act as a helper for Mlp124357. In summary, our findings established that one of Mlp effectors resides at the vacuole surface and modulates plant susceptibility. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

Type de document: Article
Mots-clés libres: effector fungal rust GxxxG motif helper protein plant susceptibility protein disulfide isomerase
Date de dépôt: 15 mars 2021 14:31
Dernière modification: 15 mars 2021 14:31
Version du document déposé: Version officielle de l'éditeur
URI: https://depot-e.uqtr.ca/id/eprint/9509

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