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The fungus  Leptosphaeria maculans  ( L. maculans ) is the causal agent of blackleg disease of canola/oilseed rape ( Brassica napus ) worldwide. We previously reported cloning of the  B. napus  blackleg resistance gene,  LepR3 , which encodes a receptor-like protein. LepR3 triggers localized cell death upon recognition of its cognate Avr protein, AvrLm1. Here, we exploited the  Nicotiana benthamiana  model plant to investigate the recognition mechanism of AvrLm1 by LepR3. Co-expression of the  LepR3/AvrLm1  gene pair in  N. benthamiana  resulted in development of a hypersensitive response (HR). However, a truncated  AvrLm1  lacking its indigenous signal peptide was compromised in its ability to induce  LepR3 -mediated HR, indicating that AvrLm1 is perceived by LepR3 extracellularly. Structure-function analysis of the AvrLm1 protein revealed that the C-terminal region of AvrLm1 was required for  LepR3 -mediated HR in  N. benthamiana  and for resistance to  L. maculans  in  B. napus . LepR3 was shown to be physically interacting with the  B. napus  receptor like kinase, SOBIR1 (BnSOBIR1). Silencing of  NbSOBIR1  or  NbSERK3 (BAK1)  compromised LepR3-AvrLm1-dependent HR in  N. benthamiana , suggesting that  LepR3 -mediated resistance to  L. maculans  in  B. napus  requires  SOBIR1  and  BAK1/SERK3 . Using this model system, we determined that BnSOBIR1 and SERK3/BAK1 are essential partners in the LepR3 signaling complex and were able to define the AvrLm1 effector domain.

The receptor-like kinase SOBIR1 interacts with Brassica napus LepR3 and is required for Leptosphaeria maculans AvrLm1-triggered immunity