Extracellular plant subtilases dampen cold-shock peptide elicitor levels.

Recognizing pathogen-associated molecular patterns on the cell surface is crucial for plant immunity. The proteinaceous nature of many of these patterns suggests that secreted proteases play important roles in their formation and stability. Here we demonstrate that the apoplastic subtilase SBT5.2a inactivates the immunogenicity of cold-shock proteins (CSPs) of the bacterial plant pathogen Pseudomonas syringae by cleaving within the immunogenic csp22 epitope. Consequently, mutant plants lacking SBT5.2a activity retain higher levels of csp22, leading to enhanced immune responses and reduced pathogen growth. SBT5.2 sensitivity is influenced by sequence variation surrounding the cleavage site and probably extends to CSPs from other bacterial species. These findings suggest that variations in csp22 stability among bacterial pathogens are a crucial factor in plant-bacteria interactions and that pathogens exploit plant proteases to avoid pattern recognition.