Abstract
During pathogenesis, effector proteins are secreted from the pathogen to the host plant to provide virulence activity for invasion of the host. However, once the host plant recognizes one of the delivered effectors, effector-triggered immunity activates a robust immune and hypersensitive response (HR). In planta, the effector AvrRps4 is processed into the N-terminus (AvrRps4(N) ) and the C-terminus (AvrRps4(C) ). AvrRps4(C) is sufficient to trigger HR in turnip and activate AtRRS1/AtRPS4-mediated immunity in Arabidopsis; on the other hand, AvrRps4(N) induces HR in lettuce. Furthermore, AvrRps4(N) -mediated HR requires a conserved arginine at position 112 (R112), which is also important for full-length AvrRps4 (AvrRps4(F) ) processing. Here, we show that effector processing and effector recognition in lettuce are uncoupled for the AvrRps4 family. In addition, we compared effector recognition by lettuce of AvrRps4 and its homologues, HopK1 and XopO. Interestingly, unlike for AvrRps4 and HopK1, mutation of the conserved R111 in XopO by itself was insufficient to abolish recognition. The combination of amino acid substitutions arginine 111 to leucine with glutamate 114 to lysine abolished the XopO-mediated HR, suggesting that AvrRps4 family members have distinct structural requirements for perception by lettuce. Together, our results provide an insight into the processing and recognition of AvrRps4 and its homologues.