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• W3203060319 abstract "Abstract Alternaria leaf spot in apple ( Malus x domestica ), caused by the fungal pathogen Alternaria alternata f. sp. mali (also called A. mali ), is a devastating disease resulting in substantial economic losses. We previously established that the resistance (R) protein MdRNL2, containing a coiled-coil, nucleotide-binding, and leucine-rich repeat (CC R -NB-LRR) domain, interacts with another CC R -NB-LRR protein, MdRNL6, to form a MdRNL2–MdRNL6 complex that confers resistance to A. mali . Here, to investigate the function of the MdRNL2–MdRNL6 complex, we identified two novel pathogenesis-related (PR) proteins, MdPR10-1 and MdPR10-2, that interact with MdRNL2. Yeast two-hybrid (Y2H) assays and bimolecular fluorescence complementation (BiFC) assays confirmed that MdPR10-1 and MdPR10-2 interact with MdRNL2 and MdRNL6 at the leucine-rich repeat domain. Transient expression assays demonstrated that accumulation of MdPR10-1 and MdPR10-2 enhanced the resistance of apple to four strains of A. mali that we tested: ALT1, GBYB2, BXSB5, and BXSB7. In vitro antifungal activity assays demonstrated that both the proteins contribute to Alternaria leaf spot resistance by inhibiting fungal growth. Our data provide evidence for a novel regulatory mechanism in which MdRNL2 and MdRNL6 interact with MdPR10-1 and MdPR10-2 to inhibit fungal growth, thereby contributing to Alternaria leaf spot resistance in apple. The identification of these two novel PR proteins will facilitate breeding for fungal disease resistance in apple." @default.
• W3203060319 created "2021-10-11" @default.
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• W3203060319 date "2021-10-01" @default.
• W3203060319 modified "2023-10-02" @default.
• W3203060319 title "Two pathogenesis-related proteins interact with leucine-rich repeat proteins to promote Alternaria leaf spot resistance in apple" @default.
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• W3203060319 doi "https://doi.org/10.1038/s41438-021-00654-4" @default.
• W3203060319 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8484663" @default.
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