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The synthetic NLR RGA5HMA5 requires multiple interfaces within and outside the integrated domain for effector recognition
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The synthetic NLR RGA5HMA5 requires multiple interfaces within and outside the integrated domain for effector recognition
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Journal Article
The synthetic NLR RGA5HMA5 requires multiple interfaces within and outside the integrated domain for effector recognition
2024
Overview
Some plant sensor nucleotide-binding leucine-rich repeat (NLR) receptors detect pathogen effectors through their integrated domains (IDs). Rice RGA5 sensor NLR recognizes its corresponding effectors AVR-Pia and AVR1-CO39 from the blast fungus
Magnaporthe oryzae
through direct binding to its heavy metal-associated (HMA) ID to trigger the RGA4 helper NLR-dependent resistance in rice. Here, we report a mutant of RGA5 named RGA5
HMA5
that confers complete resistance in transgenic rice plants to the
M. oryzae
strains expressing the noncorresponding effector AVR-PikD. RGA5
HMA5
carries three engineered interfaces, two of which lie in the HMA ID and the other in the C-terminal Lys-rich stretch tailing the ID. However, RGA5 variants having one or two of the three interfaces, including replacing all the Lys residues with Glu residues in the Lys-rich stretch, failed to activate RGA4-dependent cell death of rice protoplasts. Altogether, this work demonstrates that sensor NLRs require a concerted action of multiple surfaces within and outside the IDs to both recognize effectors and activate helper NLR-mediated resistance, and has implications in structure-guided designing of sensor NLRs.
An engineered sensor NLR RGA5
HMA5
carrying multiple resurfaced interfaces was generated to confer complete resistance to the rice blast fungus strains expressing the non-corresponding effector AVR-PikD, paving a way to broaden the resistance spectra of NLRs.
