Mark James Banfield

This study identifies Tie1, a fungal effector that targets OsTLP7 to suppress plant immunity by altering its localization and transcriptional activity.

This study investigates the oligomerization and activation mechanism of the RPS4-RRS1 immune receptor complex in Arabidopsis, showing that effector recognition triggers conformational changes that enable NADase activity.

The paper identifies ChEC108 as a fungal effector that targets plasmodesmata in Arabidopsis, binds HIPP6, and induces plasmodesmal closure to restrict fungal spread.

This study shows how engineered tandem kinase immune receptors in plants can recognize different fungal effectors, expanding their disease resistance capabilities.

This study identifies a novel wheat immune receptor pair, R3NLR and R3AK, where R3AK executes cell death through its 4-helical bundle domain, revealing a non-canonical NLR/MLKL resistance mechanism.

This paper designs de novo integrated domains using AI tools to enable plant NLR receptors to recognize non-cognate pathogen effectors, demonstrating functional immune responses and structural fidelity.

The paper shows a plant immune receptor evolved to mimic a pathogen's target, enabling it to recognize and respond to a virulence effector.

This study engineers a barley NLR receptor to enhance resistance against rice and wheat blast pathogens by improving its interaction with effector molecules.

This paper identifies an effector from Phytophthora infestans that bridges NbTOL9a to an activated NLR to suppress immunity, revealing a novel structural and functional mechanism.

This study identifies Pwl2 as a virulence factor in the rice blast fungus that suppresses host immunity by altering the localization of HIPP43.

The paper determines the solution structure and dynamics of AVR3a11, confirming its core WY domain fold and highlighting conformational flexibility in the N-terminal helix.

This study shows how the helper NLR NRC2 converts from a homodimer to a higher-order oligomer upon activation by the sensor NLR Rx, revealing the molecular mechanism of plant immune activation.

The paper shows that the rice NLR-ID receptor Pii2 indirectly recognizes the fungal effector AVR-Pii by dissociating Pii2 from host Exo70 proteins, revealing a novel mechanism of pathogen recognition.

The paper bioengineers a plant NLR receptor to recognize a conserved fungal effector, resulting in durable resistance against blast fungus isolates.

The paper identifies a functionally diverse family of Zinc-finger fold effectors in Magnaporthe oryzae, showing functional specialization across host species.