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bioRxiv · 10.1101/2022.08.17.504349

The effector recognition by synthetic sensor NLR receptors requires the concerted action of multiple interfaces within and outside the integrated domain

Zhang, X.·Liu, Y.·Yuan, G.·Wang, D.·Zhu, T.·Wu, X.·Ma, M.·Guo, L.·Guo, H.·Bhadauria, V.·Liu, J.·Peng, Y.-L.
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Abstract

Plant sensor nucleotide-binding leucine-rich repeat (NLR) receptors detect pathogen effectors through their integrated domains (IDs). The 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 RGA5HMA5 that confers complete resistance in transgenic rice plants to the M. oryzae strains expressing the noncorresponding effector AVR-PikD. RGA5HMA5 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, the 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 noncorresponding effectors and activate helper NLR-mediated resistance, and has implications in structure-guided designing of sensor NLRs.

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Zhang, X., Liu, Y., Yuan, G., Wang, D., Zhu, T., Wu, X., Ma, M., Guo, L., Guo, H., Bhadauria, V., Liu, J., Peng, Y.-L.. 2022-08-18. The effector recognition by synthetic sensor NLR receptors requires the concerted action of multiple interfaces within and outside the integrated domain. https://doi.org/10.1101/2022.08.17.504349

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