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<p>Plant viruses cause substantial damage to crops worldwide, yet conventional breeding for virus resistance remains challenging due to the inherent trade-offs between plant growth and defense. In a recent study, Yang et al. have presented a novel breeding paradigm that effectively overcomes the trade-off. The authors first demonstrate that strigolactone (SL) signaling promotes antiviral RNA interference (RNAi) by activating the transcription of <i>RNA-dependent RNA polymerase 1</i> (<i>RDR1</i>) and <i>RDR6</i>, thereby enhancing RNAi amplification. In response, the rice grassy stunt virus P3 protein directly targets the SL receptor D14, subverting the SL-RNAi antiviral module. Structural analysis of the P3-D14 complex revealed that the aspartic acid residue at the position 102 of D14 is essential for P3 binding but dispensable for SL perception. Using cytosine base editing, the authors rationally introduced a D102N substitution that abolishes the P3-D14 interaction while maintaining normal SL signaling. The resulting mutant plants exhibited robust virus resistance without growth defects. This work establishes a new paradigm for the precision breeding of crop varieties that concurrently achieve disease resistance and high yield.</p>

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Breaking the growth-defense trade-off: engineering viral-host interfaces for antiviral crop breeding

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年3月20日

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  • Ying Wang,
  • Xian-Bing Wang

摘要

Plant viruses cause substantial damage to crops worldwide, yet conventional breeding for virus resistance remains challenging due to the inherent trade-offs between plant growth and defense. In a recent study, Yang et al. have presented a novel breeding paradigm that effectively overcomes the trade-off. The authors first demonstrate that strigolactone (SL) signaling promotes antiviral RNA interference (RNAi) by activating the transcription of RNA-dependent RNA polymerase 1 (RDR1) and RDR6, thereby enhancing RNAi amplification. In response, the rice grassy stunt virus P3 protein directly targets the SL receptor D14, subverting the SL-RNAi antiviral module. Structural analysis of the P3-D14 complex revealed that the aspartic acid residue at the position 102 of D14 is essential for P3 binding but dispensable for SL perception. Using cytosine base editing, the authors rationally introduced a D102N substitution that abolishes the P3-D14 interaction while maintaining normal SL signaling. The resulting mutant plants exhibited robust virus resistance without growth defects. This work establishes a new paradigm for the precision breeding of crop varieties that concurrently achieve disease resistance and high yield.