M. J. Banfield

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

This study characterizes the interaction between the WY domain of the P. infestans effector Pi04314 and the host PP1c phosphatase, showing how it mimics host regulatory proteins to promote infection.

This paper demonstrates how allelic compatibility in the Pik NLR pair can be exploited to engineer NLRs with expanded effector recognition specificities without causing constitutive cell death.

The paper characterizes the Piks allele of the rice immune receptor Pik, showing it does not recognize known AvrPik effectors of the rice blast fungus, suggesting a novel recognition mechanism.

This paper reveals how the blast fungus effector AVR-Pii binds to rice Exo70, modulating immune recognition through a novel Zinc-finger fold and conserved hydrophobic interface.

The paper engineers rice NLR receptors to recognize new effector variants by incorporating effector targets, enhancing disease resistance against blast fungus.

The paper shows that a key functional motif in the effector PexRD54 of Phytophthora mirabilis degenerated after a host jump, leading to reduced interaction with host ATG8 proteins.

This paper studies the evolution of a rice NLR gene pair, showing that the sensor NLR undergoes dynamic domain integration under balancing selection, while the helper NLR remains functionally conserved under purifying selection.

The paper introduces pOPIN-GG vectors enabling modular cloning for rapid protein expression with various tags, maintaining expression levels and supporting complex purification.

This paper reveals how the WRKY domain of the Arabidopsis NLR receptor RRS1 recognizes structurally distinct bacterial effectors to initiate immunity.

The paper shows that allelic specialization in rice NLR receptor pairs confers resistance to fungal strains and reveals a single amino acid polymorphism driving preferential association between matching pairs.

The paper identifies a single amino acid change in APikL2 that expands its host-target binding spectrum through altered hydrogen-bonding networks.

The paper reconstructs the evolutionary history of rice NLR receptors Pik-1 and Pik-2, showing their HMA domain evolved convergent high-affinity binding to the fungal effector AVR-PikD.

The paper identifies how multiple AVR-Pik variants bind OsHIPP19 with high affinity, revealing structural differences that enhance binding compared to Pik-1's HMA domain.

This study shows that the fungal effector AVR-Pik binds and stabilizes rice HMA proteins, co-opting their function to suppress immunity, while also triggering immunity in plants with integrated HMA domains in NLRs.

This paper identifies a single amino acid change in the Pikh allele of a rice immune receptor that extends resistance to multiple strains of the blast fungus through enhanced effector binding.

This study shows that the rice NLR pair Pikp-1/Pikp-2 activates immunity through receptor cooperation, not negative regulation, by forming complexes with the effector AVR-PikD.

This study uses structure-guided engineering to expand the effector recognition of a rice NLR receptor, showing improved binding and immune response to variant effector proteins.

This study produces and characterizes the NB-ARC domain of the tomato NLR NRC1, revealing its structural similarity to mammalian homologues and its ability to bind ADP.

This study shows that a rice NLR receptor can recognize a structurally similar effector from a different pathogen, leading to partial resistance.

The paper examines three effectors from the rice blast fungus and their corresponding rice NLR immune receptors to highlight general concepts of plant-microbe interactions and identify 12 lessons in effector and NLR biology.

The paper shows that the oomycete effector HaRxL106 induces shade avoidance and suppresses salicylic acid signaling in Arabidopsis by interacting with RCD1, a protein involved in immune responses.