The effector SPRYSEC-19 of Globodera rostochiensis suppresses CC-NB-LRR-mediated disease resistance in plants.
The potato cyst nematode Globodera rostochiensis invades roots of host plants where it transforms cells near the vascular cylinder into a permanent feeding site. The host cell modifications are most likely induced by a complex mixture of proteins in the stylet secretions of the nematodes. Resistance to nematodes conferred by nucleotide-binding-leucine-rich repeat (NB-LRR) proteins usually results in a programmed cell death in and around the feeding site, and is most likely triggered by the recognition of effectors in stylet secretions. However, the actual role of these secretions in the activation and suppression of effector-triggered immunity is largely unknown. Here we demonstrate that the effector SPRYSEC-19 of G. rostochiensis physically associates in planta with the LRR domain of a member of the SW5 resistance gene cluster in tomato (Lycopersicon esculentum). Unexpectedly, this interaction did not trigger defense-related programmed cell death and resistance to G. rostochiensis. By contrast, agroinfiltration assays showed that the coexpression of SPRYSEC-19 in leaves of Nicotiana benthamiana suppresses programmed cell death mediated by several coiled-coil (CC)-NB-LRR immune receptors. Furthermore, SPRYSEC-19 abrogated resistance to Potato virus X mediated by the CC-NB-LRR resistance protein Rx1, and resistance to Verticillium dahliae mediated by an unidentified resistance in potato (Solanum tuberosum). The suppression of cell death and disease resistance did not require a physical association of SPRYSEC-19 and the LRR domains of the CC-NB-LRR resistance proteins. Altogether, our data demonstrated that potato cyst nematodes secrete effectors that enable the suppression of programmed cell death and disease resistance mediated by several CC-NB-LRR proteins in plants.
Laboratory of Nematology, Wageningen University, 6700 ES Wageningen, The Netherlands.
Wiebe J
WJ
Postma
Erik J
EJ
Slootweg
Sajid
S
Rehman
Anna
A
Finkers-Tomczak
Tom O G
TO
Tytgat
Kasper
K
van Gelderen
Jose L
JL
Lozano-Torres
Jan
J
Roosien
Rikus
R
Pomp
Casper
C
van Schaik
Jaap
J
Bakker
Aska
A
Goverse
Geert
G
Smant
D000595:Amino Acid Sequence; D000818:Animals; D016923:Cell Death; D047369:Chromatin Immunoprecipitation; D003001:Cloning, Molecular; D060467:Disease Resistance; D017343:Genes, Plant; D005822:Genetic Vectors; D015801:Helminth Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D006790:Host-Parasite Interactions; D000090263:Leucine-Rich Repeat Proteins; D018551:Solanum lycopersicum / Q000235:genetics / Q000276:immunology* / Q000469:parasitology; D008969:Molecular Sequence Data; D009348:Nematoda / Q000276:immunology / Q000472:pathogenicity*; D010935:Plant Diseases / Q000276:immunology / Q000382:microbiology / Q000469:parasitology; D018515:Plant Leaves / Q000276:immunology / Q000469:parasitology; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism; D030821:Plants, Genetically Modified / Q000276:immunology / Q000469:parasitology; D017863:Potexvirus / Q000276:immunology / Q000472:pathogenicity; D025941:Protein Interaction Mapping; D011506:Proteins / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction; D011198:Solanum tuberosum / Q000276:immunology / Q000469:parasitology; D014026:Nicotiana / Q000235:genetics / Q000276:immunology / Q000469:parasitology; D014170:Transformation, Genetic; D020172:Verticillium / Q000276:immunology / Q000472:pathogenicity
D015801:Helminth Proteins; D000090263:Leucine-Rich Repeat Proteins; D010940:Plant Proteins; D011506:Proteins; C419645:Sw-5 protein, Lycopersicon esculentum