Mauricio P. Contreras

This study shows how a plant pathogen effector blocks the stepwise assembly of a helper NLR resistosome by stabilizing an intermediate state.

The paper identifies conserved sensor-helper NLR interfaces in the NRC immune receptor network and validates their role in immune activation through structural and functional studies.

The paper introduces SNI, a framework to identify atypical protein assemblies, and applies it to NLRs, finding an undecameric assembly in NRC7 orthologs.

The paper shows that the rice NLR pair Pik-1 and Pik-2 forms a hetero-oligomeric complex at the plasma membrane in the resting state before effector activation.

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.

The paper shows that NRC3 evolved to resist suppression by a nematode effector, revealing a new type of gene-for-gene interaction between pathogens and host immune receptors.

The paper analyzes NLR evolution in lettuce and related species, finding that sensor NLRs evolve faster than helper NLRs and that sensor diversification is linked to helper dependency.

This study determines the structure of sensor-activated NbNRC2 using cryo-EM, revealing a hexameric resistosome and highlighting structural changes during NLR activation.

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.