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Plant NB-LRR proteins confer robust protection against microbes and metazoan parasites by recognizing pathogen-derived avirulence (Avr) proteins that are delivered to the host cytoplasm. Microbial Avr proteins usually function as virulence factors in compatible interactions; however, little is known about the types of metazoan proteins recognized by NB-LRR proteins and their relationship with virulence. In this report, we demonstrate that the secreted protein RBP-1 from the potato cyst nematode  Globodera pallida  elicits defense responses, including cell death typical of a hypersensitive response (HR), through the NB-LRR protein Gpa2.  Gp-Rbp-1  variants from  G. pallida  populations both virulent and avirulent to  Gpa2  demonstrated a high degree of polymorphism, with positive selection detected at numerous sites. All  Gp -RBP-1 protein variants from an avirulent population were recognized by Gpa2, whereas virulent populations possessed  Gp -RBP-1 protein variants both recognized and non-recognized by Gpa2. Recognition of  Gp -RBP-1 by Gpa2 correlated to a single amino acid polymorphism at position 187 in the  Gp -RBP-1 SPRY domain.  Gp -RBP-1 expressed from Potato virus X elicited Gpa2-mediated defenses that required Ran GTPase-activating protein 2 (RanGAP2), a protein known to interact with the Gpa2 N terminus. Tethering RanGAP2 and  Gp -RBP-1 variants via fusion proteins resulted in an enhancement of Gpa2-mediated responses. However, activation of Gpa2 was still dependent on the recognition specificity conferred by amino acid 187 and the Gpa2 LRR domain. These results suggest a two-tiered process wherein RanGAP2 mediates an initial interaction with pathogen-delivered  Gp -RBP-1 proteins but where the Gpa2 LRR determines which of these interactions will be productive.

The Cyst Nematode SPRYSEC Protein RBP-1 Elicits Gpa2- and RanGAP2-Dependent Plant Cell Death