Single amino acid mutations in the potato immune receptor R3a expand response to Phytophthora effectors

Autores
Segretin, Maria Eugenia; Pais, Silvia Marina; Franceschetti, Marina; Chaparro Garcia, Angela; Bos, Jorunn I. B.; Banfield, Mark J.; Kamoun, Sophien
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Both plants and animals rely on nucleotide-binding domain and leucine-rich repeat-containing proteins (NB-LRRs or NLRs) to respond to invading pathogens and activate immune responses. How plant NB-LRR proteins respond to pathogens is poorly understood. We undertook a gain-of-function random mutagenesis screen of the potato NB-LRR immune receptor R3a to study how this protein responds to the effector protein AVR3a from the oomycete pathogen Phytophthora infestans. R3a response can be extended to the stealthy AVR3aEM isoform of the effector while retaining recognition of AVR3aKI. Each one of 8 single amino acid mutations is sufficient to expand the R3a response to AVR3aEM and other AVR3a variants. These mutations occur across the R3a protein, from the N-terminus to different regions of the LRR domain. Further characterization of these R3a mutants revealed that at least one of them was sensitized, exhibiting a stronger response than the wild-type R3a protein to AVR3aKI. Remarkably, the N336Y mutation, near the R3a nucleotide-binding pocket, conferred response to the effector protein PcAVR3a4 from the vegetable pathogen Phytophthora capsici. This work contributes to understanding how NB-LRR receptor specificity can be modulated. Together with knowledge of pathogen effector diversity, this strategy can be exploited to develop synthetic immune receptors.
Fil: Segretin, Maria Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; Argentina. The Sainsbury Laboratory; Reino Unido
Fil: Pais, Silvia Marina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; Argentina. The Sainsbury Laboratory; Reino Unido
Fil: Franceschetti, Marina. John Innes Institute; Reino Unido
Fil: Chaparro Garcia, Angela. The Sainsbury Laboratory; Reino Unido
Fil: Bos, Jorunn I. B.. The Sainsbury Laboratory; Reino Unido
Fil: Banfield, Mark J.. John Innes Institute; Reino Unido
Fil: Kamoun, Sophien. The Sainsbury Laboratory; Reino Unido
Materia
R3a
Potato
Nb-Lrr
Phytophthora
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/4005
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/4005
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Single amino acid mutations in the potato immune receptor R3a expand response to Phytophthora effectorsSegretin, Maria EugeniaPais, Silvia MarinaFranceschetti, MarinaChaparro Garcia, AngelaBos, Jorunn I. B.Banfield, Mark J.Kamoun, SophienR3aPotatoNb-LrrPhytophthorahttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Both plants and animals rely on nucleotide-binding domain and leucine-rich repeat-containing proteins (NB-LRRs or NLRs) to respond to invading pathogens and activate immune responses. How plant NB-LRR proteins respond to pathogens is poorly understood. We undertook a gain-of-function random mutagenesis screen of the potato NB-LRR immune receptor R3a to study how this protein responds to the effector protein AVR3a from the oomycete pathogen Phytophthora infestans. R3a response can be extended to the stealthy AVR3aEM isoform of the effector while retaining recognition of AVR3aKI. Each one of 8 single amino acid mutations is sufficient to expand the R3a response to AVR3aEM and other AVR3a variants. These mutations occur across the R3a protein, from the N-terminus to different regions of the LRR domain. Further characterization of these R3a mutants revealed that at least one of them was sensitized, exhibiting a stronger response than the wild-type R3a protein to AVR3aKI. Remarkably, the N336Y mutation, near the R3a nucleotide-binding pocket, conferred response to the effector protein PcAVR3a4 from the vegetable pathogen Phytophthora capsici. This work contributes to understanding how NB-LRR receptor specificity can be modulated. Together with knowledge of pathogen effector diversity, this strategy can be exploited to develop synthetic immune receptors.Fil: Segretin, Maria Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; Argentina. The Sainsbury Laboratory; Reino UnidoFil: Pais, Silvia Marina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; Argentina. The Sainsbury Laboratory; Reino UnidoFil: Franceschetti, Marina. John Innes Institute; Reino UnidoFil: Chaparro Garcia, Angela. The Sainsbury Laboratory; Reino UnidoFil: Bos, Jorunn I. B.. The Sainsbury Laboratory; Reino UnidoFil: Banfield, Mark J.. John Innes Institute; Reino UnidoFil: Kamoun, Sophien. The Sainsbury Laboratory; Reino UnidoAmerican Phytopathological Society2014-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/zipapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/4005Segretin, Maria Eugenia; Pais, Silvia Marina; Franceschetti, Marina; Chaparro Garcia, Angela; Bos, Jorunn I. B.; et al.; Single amino acid mutations in the potato immune receptor R3a expand response to Phytophthora effectors; American Phytopathological Society; Molecular Plant-Microbe Interactions; 27; 7; 3-2014; 624-6370894-0282enginfo:eu-repo/semantics/altIdentifier/url/http://apsjournals.apsnet.org/doi/abs/10.1094/MPMI-02-14-0040-Rinfo:eu-repo/semantics/altIdentifier/url/http://dx.doi.org/10.1094/MPMI-02-14-0040-Rinfo:eu-repo/semantics/altIdentifier/issn/0894-0282info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:55:08Zoai:ri.conicet.gov.ar:11336/4005instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:55:08.34CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Single amino acid mutations in the potato immune receptor R3a expand response to Phytophthora effectors
title Single amino acid mutations in the potato immune receptor R3a expand response to Phytophthora effectors
spellingShingle Single amino acid mutations in the potato immune receptor R3a expand response to Phytophthora effectors
Segretin, Maria Eugenia
R3a
Potato
Nb-Lrr
Phytophthora
title_short Single amino acid mutations in the potato immune receptor R3a expand response to Phytophthora effectors
title_full Single amino acid mutations in the potato immune receptor R3a expand response to Phytophthora effectors
title_fullStr Single amino acid mutations in the potato immune receptor R3a expand response to Phytophthora effectors
title_full_unstemmed Single amino acid mutations in the potato immune receptor R3a expand response to Phytophthora effectors
title_sort Single amino acid mutations in the potato immune receptor R3a expand response to Phytophthora effectors
dc.creator.none.fl_str_mv Segretin, Maria Eugenia
Pais, Silvia Marina
Franceschetti, Marina
Chaparro Garcia, Angela
Bos, Jorunn I. B.
Banfield, Mark J.
Kamoun, Sophien
author Segretin, Maria Eugenia
author_facet Segretin, Maria Eugenia
Pais, Silvia Marina
Franceschetti, Marina
Chaparro Garcia, Angela
Bos, Jorunn I. B.
Banfield, Mark J.
Kamoun, Sophien
author_role author
author2 Pais, Silvia Marina
Franceschetti, Marina
Chaparro Garcia, Angela
Bos, Jorunn I. B.
Banfield, Mark J.
Kamoun, Sophien
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv R3a
Potato
Nb-Lrr
Phytophthora
topic R3a
Potato
Nb-Lrr
Phytophthora
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Both plants and animals rely on nucleotide-binding domain and leucine-rich repeat-containing proteins (NB-LRRs or NLRs) to respond to invading pathogens and activate immune responses. How plant NB-LRR proteins respond to pathogens is poorly understood. We undertook a gain-of-function random mutagenesis screen of the potato NB-LRR immune receptor R3a to study how this protein responds to the effector protein AVR3a from the oomycete pathogen Phytophthora infestans. R3a response can be extended to the stealthy AVR3aEM isoform of the effector while retaining recognition of AVR3aKI. Each one of 8 single amino acid mutations is sufficient to expand the R3a response to AVR3aEM and other AVR3a variants. These mutations occur across the R3a protein, from the N-terminus to different regions of the LRR domain. Further characterization of these R3a mutants revealed that at least one of them was sensitized, exhibiting a stronger response than the wild-type R3a protein to AVR3aKI. Remarkably, the N336Y mutation, near the R3a nucleotide-binding pocket, conferred response to the effector protein PcAVR3a4 from the vegetable pathogen Phytophthora capsici. This work contributes to understanding how NB-LRR receptor specificity can be modulated. Together with knowledge of pathogen effector diversity, this strategy can be exploited to develop synthetic immune receptors.
Fil: Segretin, Maria Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; Argentina. The Sainsbury Laboratory; Reino Unido
Fil: Pais, Silvia Marina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; Argentina. The Sainsbury Laboratory; Reino Unido
Fil: Franceschetti, Marina. John Innes Institute; Reino Unido
Fil: Chaparro Garcia, Angela. The Sainsbury Laboratory; Reino Unido
Fil: Bos, Jorunn I. B.. The Sainsbury Laboratory; Reino Unido
Fil: Banfield, Mark J.. John Innes Institute; Reino Unido
Fil: Kamoun, Sophien. The Sainsbury Laboratory; Reino Unido
description Both plants and animals rely on nucleotide-binding domain and leucine-rich repeat-containing proteins (NB-LRRs or NLRs) to respond to invading pathogens and activate immune responses. How plant NB-LRR proteins respond to pathogens is poorly understood. We undertook a gain-of-function random mutagenesis screen of the potato NB-LRR immune receptor R3a to study how this protein responds to the effector protein AVR3a from the oomycete pathogen Phytophthora infestans. R3a response can be extended to the stealthy AVR3aEM isoform of the effector while retaining recognition of AVR3aKI. Each one of 8 single amino acid mutations is sufficient to expand the R3a response to AVR3aEM and other AVR3a variants. These mutations occur across the R3a protein, from the N-terminus to different regions of the LRR domain. Further characterization of these R3a mutants revealed that at least one of them was sensitized, exhibiting a stronger response than the wild-type R3a protein to AVR3aKI. Remarkably, the N336Y mutation, near the R3a nucleotide-binding pocket, conferred response to the effector protein PcAVR3a4 from the vegetable pathogen Phytophthora capsici. This work contributes to understanding how NB-LRR receptor specificity can be modulated. Together with knowledge of pathogen effector diversity, this strategy can be exploited to develop synthetic immune receptors.
publishDate 2014
dc.date.none.fl_str_mv 2014-03
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/4005
Segretin, Maria Eugenia; Pais, Silvia Marina; Franceschetti, Marina; Chaparro Garcia, Angela; Bos, Jorunn I. B.; et al.; Single amino acid mutations in the potato immune receptor R3a expand response to Phytophthora effectors; American Phytopathological Society; Molecular Plant-Microbe Interactions; 27; 7; 3-2014; 624-637
0894-0282
url http://hdl.handle.net/11336/4005
identifier_str_mv Segretin, Maria Eugenia; Pais, Silvia Marina; Franceschetti, Marina; Chaparro Garcia, Angela; Bos, Jorunn I. B.; et al.; Single amino acid mutations in the potato immune receptor R3a expand response to Phytophthora effectors; American Phytopathological Society; Molecular Plant-Microbe Interactions; 27; 7; 3-2014; 624-637
0894-0282
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://apsjournals.apsnet.org/doi/abs/10.1094/MPMI-02-14-0040-R
info:eu-repo/semantics/altIdentifier/url/http://dx.doi.org/10.1094/MPMI-02-14-0040-R
info:eu-repo/semantics/altIdentifier/issn/0894-0282
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/zip
application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Phytopathological Society
publisher.none.fl_str_mv American Phytopathological Society
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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