Alternative splicing of a multi-drug transporter from Pseudoperonospora cubensis generates an RXLR effector protein that elicits a rapid cell death.

Pseudoperonospora cubensis, an obligate oomycete pathogen, is the causal agent of cucurbit downy mildew, a foliar disease of global economic importance. Similar to other oomycete plant pathogens, Ps. cubensis has a suite of RXLR and RXLR-like effector proteins, which likely function as virulence or...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Elizabeth A Savory, Cheng Zou, Bishwo N Adhikari, John P Hamilton, C Robin Buell, Shin-Han Shiu, Brad Day
Formato: article
Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2012
Materias:
R
Q
Acceso en línea:https://doaj.org/article/eb0b3a8bbd3b4c43beab51e8966b1182
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:eb0b3a8bbd3b4c43beab51e8966b1182
record_format dspace
spelling oai:doaj.org-article:eb0b3a8bbd3b4c43beab51e8966b11822021-11-18T07:23:06ZAlternative splicing of a multi-drug transporter from Pseudoperonospora cubensis generates an RXLR effector protein that elicits a rapid cell death.1932-620310.1371/journal.pone.0034701https://doaj.org/article/eb0b3a8bbd3b4c43beab51e8966b11822012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22496844/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Pseudoperonospora cubensis, an obligate oomycete pathogen, is the causal agent of cucurbit downy mildew, a foliar disease of global economic importance. Similar to other oomycete plant pathogens, Ps. cubensis has a suite of RXLR and RXLR-like effector proteins, which likely function as virulence or avirulence determinants during the course of host infection. Using in silico analyses, we identified 271 candidate effector proteins within the Ps. cubensis genome with variable RXLR motifs. In extending this analysis, we present the functional characterization of one Ps. cubensis effector protein, RXLR protein 1 (PscRXLR1), and its closest Phytophthora infestans ortholog, PITG_17484, a member of the Drug/Metabolite Transporter (DMT) superfamily. To assess if such effector-non-effector pairs are common among oomycete plant pathogens, we examined the relationship(s) among putative ortholog pairs in Ps. cubensis and P. infestans. Of 271 predicted Ps. cubensis effector proteins, only 109 (41%) had a putative ortholog in P. infestans and evolutionary rate analysis of these orthologs shows that they are evolving significantly faster than most other genes. We found that PscRXLR1 was up-regulated during the early stages of infection of plants, and, moreover, that heterologous expression of PscRXLR1 in Nicotiana benthamiana elicits a rapid necrosis. More interestingly, we also demonstrate that PscRXLR1 arises as a product of alternative splicing, making this the first example of an alternative splicing event in plant pathogenic oomycetes transforming a non-effector gene to a functional effector protein. Taken together, these data suggest a role for PscRXLR1 in pathogenicity, and, in total, our data provide a basis for comparative analysis of candidate effector proteins and their non-effector orthologs as a means of understanding function and evolutionary history of pathogen effectors.Elizabeth A SavoryCheng ZouBishwo N AdhikariJohn P HamiltonC Robin BuellShin-Han ShiuBrad DayPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 4, p e34701 (2012)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Elizabeth A Savory
Cheng Zou
Bishwo N Adhikari
John P Hamilton
C Robin Buell
Shin-Han Shiu
Brad Day
Alternative splicing of a multi-drug transporter from Pseudoperonospora cubensis generates an RXLR effector protein that elicits a rapid cell death.
description Pseudoperonospora cubensis, an obligate oomycete pathogen, is the causal agent of cucurbit downy mildew, a foliar disease of global economic importance. Similar to other oomycete plant pathogens, Ps. cubensis has a suite of RXLR and RXLR-like effector proteins, which likely function as virulence or avirulence determinants during the course of host infection. Using in silico analyses, we identified 271 candidate effector proteins within the Ps. cubensis genome with variable RXLR motifs. In extending this analysis, we present the functional characterization of one Ps. cubensis effector protein, RXLR protein 1 (PscRXLR1), and its closest Phytophthora infestans ortholog, PITG_17484, a member of the Drug/Metabolite Transporter (DMT) superfamily. To assess if such effector-non-effector pairs are common among oomycete plant pathogens, we examined the relationship(s) among putative ortholog pairs in Ps. cubensis and P. infestans. Of 271 predicted Ps. cubensis effector proteins, only 109 (41%) had a putative ortholog in P. infestans and evolutionary rate analysis of these orthologs shows that they are evolving significantly faster than most other genes. We found that PscRXLR1 was up-regulated during the early stages of infection of plants, and, moreover, that heterologous expression of PscRXLR1 in Nicotiana benthamiana elicits a rapid necrosis. More interestingly, we also demonstrate that PscRXLR1 arises as a product of alternative splicing, making this the first example of an alternative splicing event in plant pathogenic oomycetes transforming a non-effector gene to a functional effector protein. Taken together, these data suggest a role for PscRXLR1 in pathogenicity, and, in total, our data provide a basis for comparative analysis of candidate effector proteins and their non-effector orthologs as a means of understanding function and evolutionary history of pathogen effectors.
format article
author Elizabeth A Savory
Cheng Zou
Bishwo N Adhikari
John P Hamilton
C Robin Buell
Shin-Han Shiu
Brad Day
author_facet Elizabeth A Savory
Cheng Zou
Bishwo N Adhikari
John P Hamilton
C Robin Buell
Shin-Han Shiu
Brad Day
author_sort Elizabeth A Savory
title Alternative splicing of a multi-drug transporter from Pseudoperonospora cubensis generates an RXLR effector protein that elicits a rapid cell death.
title_short Alternative splicing of a multi-drug transporter from Pseudoperonospora cubensis generates an RXLR effector protein that elicits a rapid cell death.
title_full Alternative splicing of a multi-drug transporter from Pseudoperonospora cubensis generates an RXLR effector protein that elicits a rapid cell death.
title_fullStr Alternative splicing of a multi-drug transporter from Pseudoperonospora cubensis generates an RXLR effector protein that elicits a rapid cell death.
title_full_unstemmed Alternative splicing of a multi-drug transporter from Pseudoperonospora cubensis generates an RXLR effector protein that elicits a rapid cell death.
title_sort alternative splicing of a multi-drug transporter from pseudoperonospora cubensis generates an rxlr effector protein that elicits a rapid cell death.
publisher Public Library of Science (PLoS)
publishDate 2012
url https://doaj.org/article/eb0b3a8bbd3b4c43beab51e8966b1182
work_keys_str_mv AT elizabethasavory alternativesplicingofamultidrugtransporterfrompseudoperonosporacubensisgeneratesanrxlreffectorproteinthatelicitsarapidcelldeath
AT chengzou alternativesplicingofamultidrugtransporterfrompseudoperonosporacubensisgeneratesanrxlreffectorproteinthatelicitsarapidcelldeath
AT bishwonadhikari alternativesplicingofamultidrugtransporterfrompseudoperonosporacubensisgeneratesanrxlreffectorproteinthatelicitsarapidcelldeath
AT johnphamilton alternativesplicingofamultidrugtransporterfrompseudoperonosporacubensisgeneratesanrxlreffectorproteinthatelicitsarapidcelldeath
AT crobinbuell alternativesplicingofamultidrugtransporterfrompseudoperonosporacubensisgeneratesanrxlreffectorproteinthatelicitsarapidcelldeath
AT shinhanshiu alternativesplicingofamultidrugtransporterfrompseudoperonosporacubensisgeneratesanrxlreffectorproteinthatelicitsarapidcelldeath
AT bradday alternativesplicingofamultidrugtransporterfrompseudoperonosporacubensisgeneratesanrxlreffectorproteinthatelicitsarapidcelldeath
_version_ 1718423570217959424