An HMA-like integrated domain in the wheat tandem kinase WTK4 recognises an RNase-like pathogen effector

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Abstract

Proteins with a tandem kinase structure have recently emerged as new players in race-specific resistance in cereal crops. However, the molecular understanding of these novel immune receptors’ resistance mechanisms is limited by the lack of knowledge about the pathogen effectors that they recognise. In this work, we identify AvrWTK4, the wheat powdery mildew RNase-like effector recognised by the wheat tandem kinase immune receptor WTK4, through a combination of bi-parental genetic mapping and mutagenesis. We demonstrate that mutations in the AvrWTK4 gene or a reduction of its expression lead to virulence on WTK4 . Transfection of AvrWTK4 specifically induced cell death in WTK4 -containing Aegilops tauschii protoplasts. The avirulent AvrWTK4 variant interacts more strongly than the virulent variant with the N-terminal heavy metal-associated (HMA)-like domain of WTK4. These findings further highlight that integrated domains in tandem kinase proteins serve as decoys for pathogen effectors, which could be leveraged to design novel recognition specificities.
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Abstract

Proteins with a tandem kinase structure have recently emerged as new players in race-specific resistance in cereal crops. However, the molecular understanding of these novel immune receptors’ resistance mechanisms is limited by the lack of knowledge about the pathogen effectors that they recognise. In this work, we identify AvrWTK4, the wheat powdery mildew RNase-like effector recognised by the wheat tandem kinase immune receptor WTK4, through a combination of bi-parental genetic mapping and mutagenesis. We demonstrate that mutations in the AvrWTK4 gene or a reduction of its expression lead to virulence on WTK4. Transfection of AvrWTK4 specifically induced cell death in WTK4-containing Aegilops tauschii protoplasts. The avirulent AvrWTK4 variant interacts more strongly than the virulent variant with the N-terminal heavy metal-associated (HMA)-like domain of WTK4. These findings further highlight that integrated domains in tandem kinase proteins serve as decoys for pathogen effectors, which could be leveraged to design novel recognition specificities. Competing Interest Statement The authors have declared no competing interest. Footnotes

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requests should be addressed to Javier Sánchez-Martín or Zoe Bernasconi (zoe.bernasconi{at}botinst.uzh.ch).

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last seen: 2026-05-20T01:45:00.602351+00:00