The Cyst Nematode SPRYSEC Protein RBP-1 Elicits Gpa2- and RanGAP2-Dependent Plant Cell Death
| Autor: | Peter Moffett, Alexandra Blanchard, Melanie A. Sacco, Marianne J. Jaubert, Geert Smant, Aska Goverse, Kamila Koropacka, Eric Grenier |
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| Přispěvatelé: | Boyce Thompson Institute [Ithaca], Laboratory of Nematology, Wageningen University and Research [Wageningen] (WUR), Biologie des organismes et des populations appliquées à la protection des plantes (BIO3P), Institut National de la Recherche Agronomique (INRA)-Université de Rennes (UR)-AGROCAMPUS OUEST, Département de biologie [Sherbrooke] (UdeS), Faculté des sciences [Sherbrooke] (UdeS), Université de Sherbrooke (UdeS)-Université de Sherbrooke (UdeS), AGROCAMPUS OUEST, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National de la Recherche Agronomique (INRA) |
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
0106 biological sciences
GTPase-activating protein [SDV]Life Sciences [q-bio] 01 natural sciences pomme de terre Biology (General) Globodera pallida nb-lrr protein avirulence genes Peptide sequence nématode Plant Proteins Genetics globodera-pallida 0303 health sciences education.field_of_study Cell Death biology EPS-2 GTPase-Activating Proteins Helminth Proteins gène de résistance Potato virus X protéine sequence alignment rich repeat protein potato Research Article Plant Biology/Plant-Biotic Interactions Hypersensitive response endocrine system globodera pallida QH301-705.5 Recombinant Fusion Proteins Molecular Sequence Data Immunology Population Virulence Molecular Biology/Molecular Evolution Microbiology 03 medical and health sciences Virology Tobacco Hypersensitivity Animals Amino Acid Sequence Tylenchoidea Selection Genetic education virus-resistance Laboratorium voor Nematologie Molecular Biology 030304 developmental biology downy mildew éliciteur fungi RC581-607 biology.organism_classification Fusion protein Plant Leaves Potexvirus arabidopsis solanum tuberosum Amino Acid Substitution Parasitology Laboratory of Nematology Immunologic diseases. Allergy disease resistance genes 010606 plant biology & botany |
| Zdroj: | PLoS Pathogens 5 (2009) 8 PLoS Pathogens PLoS Pathogens, 2009, 5 (8), pp.e1000564. ⟨10.1371/journal.ppat.1000564⟩ PLoS Pathogens, Vol 5, Iss 8, p e1000564 (2009) PLoS Pathogens, 5(8) PLoS Pathogens, Public Library of Science, 2009, 5 (8), pp.e1000564. ⟨10.1371/journal.ppat.1000564⟩ Plos Pathogens 8 (5), e1000564. (2009) |
| ISSN: | 1553-7366 1553-7374 |
| DOI: | 10.1371/journal.ppat.1000564⟩ |
| Popis: | 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. Author Summary Biotrophic plant pathogens produce effector proteins that are delivered to the host cytoplasm where they alter defense responses and metabolism to favor pathogen colonization. In turn, plants have evolved intra-cellular proteins to recognize pathogen effector proteins, known as NB-LRR proteins, which are similar in structure to animal NOD-LRR immune receptors. While effector proteins recognized by NB-LRR proteins have been identified from many organisms, the identification of such proteins from metazoan plant parasites has presented unique challenges due to the lack of genetically tractable model species. The potato Gpa2 protein confers resistance to some isolates of the potato pale cyst nematode, Globodera pallida. In this report, we show that Gpa2 recognizes certain variants of the G. pallida protein, Gp-RBP-1, which is highly polymorphic both within and between populations. This recognition in turn induces defense responses, including a form of programmed cell death characteristic of plant immune receptor activation. Moreover, we show that a Gpa2-interacting protein, RanGAP2, is required for Gpa2 function and that activation of Gpa2 is enhanced when Gp-RBP-1 is artificially tethered to RanGAP2. Thus, our findings suggest that RanGAP2 acts as a recognition co-factor for Gpa2, and have important implications for our understanding of the mechanisms and evolution of pathogen recognition by NB-LRR proteins. |
| Databáze: | OpenAIRE |
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