by Denkstrom
All storiesResearchers Engineer Wheat Immune Receptors to Resist Fungal Blast

Researchers Engineer Wheat Immune Receptors to Resist Fungal Blast

Researchers at the John Innes Centre and Kobe University have engineered plant immune receptor domains in the laboratory to bind effector proteins PBY2 and PWT7 from the blast fungus Magnaporthe oryzae. According to the John Innes Centre, this could enable broader disease resistance, though protection of whole cereal plants has not yet been demonstrated.

Researchers at the John Innes Centre in Norwich and Kobe University in Japan, led by Professor Mark Banfield with first author Dr. Daniel Yu, worked on the study. The study appeared in Science Advances, with the John Innes Centre releasing results on September 23, 2026. The John Innes Centre describes the experiments as a proof-of-concept in the laboratory. Protection for growing plants has not yet been demonstrated.

One Fungus Threatening Wheat, Barley, and Rice

Magnaporthe oryzae ranks among the world's most harmful cereal pathogens. Different strains cause rice blast in Asia and wheat blast, which struck Brazil in the 1980s and has since spread to Bangladesh and Zambia. According to the John Innes Centre, the disease destroys rice each year equivalent to feeding 60 million people. Because the pathogen quickly overcomes single resistance genes, researchers seek defense mechanisms harder to break.

plant-research

The examined receptors carry a decoy domain that mimics a protein attacked by the fungus. If the pathogen injects an effector protein to disable this domain, the receptor triggers a defense response. The barley receptor Rmo2 binds the effector PBY2, and the wheat receptor Rwt7 binds PWT7 from a different fungal strain. Using X-ray crystallography, researchers deliberately modified the binding surface of Rmo2 following the pattern of Rwt7. The resulting domain, Rmo2 HMA+, retained its tight nanomolar binding to PBY2 and additionally bound the second effector PWT7 with nanomolar affinity. Conversely, the modified Rwt7 domain gained binding to PBY2. In isolated wheat cells without a cell wall, so-called protoplasts, the dual-specificity receptor was tested as proof-of-concept.

From Cell Test to Field Is Still a Long Road

The dual-specific receptor has been demonstrated only in isolated cells in the laboratory dish, not in a growing plant in a greenhouse or field. According to the John Innes Centre, the next step is to transfer results from these substitute tests to greenhouse plants. The in-house platform for wheat genome editing and transformation should support these experiments. Before a commercially viable variety could be developed, additional years of breeding or genetic engineering would be needed, followed by approval and field trial procedures that vary from country to country.

Why TKP and NLR Receptors Together Could Offer More Durable Protection

Dr. Yu and Professor Banfield regard the finding as evidence that these receptors are more programmable than previously thought, opening the possibility of combining resistance traits deliberately rather than waiting for them to emerge naturally through breeding. The researchers' long-term goal is to combine such modified tandem kinase proteins with a second class of resistance genes, the NLR genes, in a single variety. A cereal plant with multiple independent, well-characterized recognition systems would be harder for the fungus to overcome with a single mutation than a variety relying on one resistance gene. Many resistant varieties have failed within just a few growing seasons in the past. The urgency is greatest for South Asia: wheat blast is considered an emerging threat there because the disease spread from South America to Bangladesh in 2016, and many wheat varieties grown there resemble those that have proven susceptible elsewhere.