The study reports the bioengineering of a rice nucleotide-binding, leucine-rich repeat (NLR) immune receptor, Pik-1, to respond to a conserved family of effectors from the blast fungus *Magnaporthe oryzae*. By replacing the integrated heavy metal-associated (HMA) domain of Pik-1 with the HMA domain of the rice protein OsHIPP43, the researchers transformed the receptor's response profile from recognizing the rice blast effector AVR-Pik to recognizing the host-determining factor Pw12. The crystal structure of the Pw12/OsHIPP43 complex revealed a robust interface that is challenging to disrupt by mutagenesis, suggesting durable and broad resistance to blast isolates carrying PWL effectors. This approach highlights the potential of using host targets as effector recognition modules in NLRs, providing a promising strategy for generating novel disease resistance traits in plants.The study reports the bioengineering of a rice nucleotide-binding, leucine-rich repeat (NLR) immune receptor, Pik-1, to respond to a conserved family of effectors from the blast fungus *Magnaporthe oryzae*. By replacing the integrated heavy metal-associated (HMA) domain of Pik-1 with the HMA domain of the rice protein OsHIPP43, the researchers transformed the receptor's response profile from recognizing the rice blast effector AVR-Pik to recognizing the host-determining factor Pw12. The crystal structure of the Pw12/OsHIPP43 complex revealed a robust interface that is challenging to disrupt by mutagenesis, suggesting durable and broad resistance to blast isolates carrying PWL effectors. This approach highlights the potential of using host targets as effector recognition modules in NLRs, providing a promising strategy for generating novel disease resistance traits in plants.