RPS5-Mediated Disease Resistance: Fundamental Insights and Translational Applications.

Focusing on the discovery and characterization of the disease resistance protein RPS5 and its guardee PBS1, this review discusses work done in the Innes laboratory from the initial identification of the gene in 1995 to the recent deployment of the PBS1 decoy system in crops. This is done through discussion of the structure, function, and signaling environment of RPS5 and PBS1, highlighting collaborations and influential ideas along the way. RPS5, a nucleotide-binding leucine-rich repeat (NLR) protein, is activated by the proteolytic cleavage of PBS1.

Optimizing the PBS1 Decoy System to Confer Resistance to Potyvirus Infection in and Soybean.

The resistance protein RPS5 is activated by proteolytic cleavage of the protein kinase PBS1 by the effector protease AvrPphB. We have previously shown that replacing seven amino acids at the cleavage site of PBS1 with a motif cleaved by the NIa protease of turnip mosaic virus (TuMV) enables RPS5 activation upon TuMV infection. However, this engineered resistance conferred a trailing necrosis phenotype indicative of a cell-death response too slow to contain the virus.