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<div>Genetic-based disease resistance is the most effective and environmentally sustainable approach to protecting crops from disease. Although significant progress has been made with respect to understanding the mechanistic basis of plant-pathogen interactions, a remaining challenge is to expand the recognition specificity of plant resistance (<i>R</i>) proteins to confer entirely new specificities. We recently reported a novel approach for expanding the recognition specificity of an <i>Arabidopsis R </i>protein by generating ‘decoy’ proteins that function as substrates for pathogen proteases. This strategy is based on the observation that modifying the protease cleavage site within <i>Arabidopsis</i> PBS1, a substrate of the AvrPphB cysteine protease, expands the recognition specificity of the <i>Arabidopsis</i> RPS5 immune response pathway. Thus, the specificity of RPS5 can be changed simply by altering the protease cleavage sequence within PBS1. We are now using this technology to engineer resistance in soybean (<i>Glycine max</i>) to <i>Soybean Mosaic Virus</i> (SMV) based on the recognition of the viral protease by a PBS1 ‘decoy’ protein. Soybean encodes three co-orthologs of PBS1, and all three can be cleaved by AvrPphB. Furthermore, we show soybean recognizes AvrPphB, thus soybean likely contains an <i>R</i> protein that detects PBS1 cleavage. We hypothesize that we will be able to engineer resistance to SMV by introducing a cleavage site recognized by the SMV protease into a soybean PBS1 ortholog.</div>