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The Globodera pallida Effector GpPDI1 Is a Functional Thioredoxin and Triggers Defense-Related Cell Death Independent of Its Enzymatic Activity.

Identifieur interne : 000035 ( Main/Exploration ); précédent : 000034; suivant : 000036

The Globodera pallida Effector GpPDI1 Is a Functional Thioredoxin and Triggers Defense-Related Cell Death Independent of Its Enzymatic Activity.

Auteurs : Rachel Gross [États-Unis] ; Shan Zhang [États-Unis, République populaire de Chine] ; Lihui Wei [République populaire de Chine] ; Allan Caplan [États-Unis] ; Joseph Kuhl [États-Unis] ; Louise-Marie Dandurand [États-Unis] ; Xiaofang Wang [République populaire de Chine] ; Fangming Xiao [États-Unis]

Source :

RBID : pubmed:32484388

Descripteurs français

English descriptors

Abstract

The plant-parasitic nematode Globodera pallida is an obligate biotroph that only reproduces on select species in the Solanum family. The establishment of the feeding site, the syncytium, involves secretion of effectors into the plant cell to combat the plant defense response and facilitate transformation of root cells into the syncytium. Despite the important predicted roles of effectors in the plant-pathogen interactions, the functionality of G. pallida effectors is largely unknown. In this study, we identified and characterized a G. pallida effector protein disulfide isomerase (GpPDI1). GpPDI1 contains two thioredoxin domains that function together to reduce disulfide bonds, as manifested by the nullification of enzymatic activity when either domain is absent. The transcript of GpPDI1 is localized in the dorsal gland of the nematode during the J2 stage. In addition, GpPDI1 can trigger defense-related cell death in Nicotiana benthamiana and tomato (Solanum lycopersicum) leaf tissue and localizes in the plant host cell's cytoplasm and nucleus when transiently expressed in plant cells. Significantly, the ability of elicitation of cell death is not dependent on the enzymatic activity of GpPDI1 or correlated with the subcellular distribution of GpPDI1, suggesting that a nondisulfide reducing function or structural feature of GpPDI1 is responsible for the recognition by the host immune system to elicit cell death.

DOI: 10.1094/PHYTO-02-20-0038-R
PubMed: 32484388


Affiliations:


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Le document en format XML

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<term>Thioredoxins (MeSH)</term>
<term>Tobacco (MeSH)</term>
<term>Tylenchoidea (MeSH)</term>
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<div type="abstract" xml:lang="en">The plant-parasitic nematode
<i>Globodera pallida</i>
is an obligate biotroph that only reproduces on select species in the
<i>Solanum</i>
family. The establishment of the feeding site, the syncytium, involves secretion of effectors into the plant cell to combat the plant defense response and facilitate transformation of root cells into the syncytium. Despite the important predicted roles of effectors in the plant-pathogen interactions, the functionality of
<i>G. pallida</i>
effectors is largely unknown. In this study, we identified and characterized a
<i>G. pallida</i>
effector protein disulfide isomerase (GpPDI1). GpPDI1 contains two thioredoxin domains that function together to reduce disulfide bonds, as manifested by the nullification of enzymatic activity when either domain is absent. The transcript of
<i>GpPDI1</i>
is localized in the dorsal gland of the nematode during the J2 stage. In addition, GpPDI1 can trigger defense-related cell death in
<i>Nicotiana benthamiana</i>
and tomato (
<i>Solanum lycopersicum</i>
) leaf tissue and localizes in the plant host cell's cytoplasm and nucleus when transiently expressed in plant cells. Significantly, the ability of elicitation of cell death is not dependent on the enzymatic activity of GpPDI1 or correlated with the subcellular distribution of GpPDI1, suggesting that a nondisulfide reducing function or structural feature of GpPDI1 is responsible for the recognition by the host immune system to elicit cell death.</div>
</front>
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<i>Globodera pallida</i>
Effector GpPDI1 Is a Functional Thioredoxin and Triggers Defense-Related Cell Death Independent of Its Enzymatic Activity.</ArticleTitle>
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<Abstract>
<AbstractText>The plant-parasitic nematode
<i>Globodera pallida</i>
is an obligate biotroph that only reproduces on select species in the
<i>Solanum</i>
family. The establishment of the feeding site, the syncytium, involves secretion of effectors into the plant cell to combat the plant defense response and facilitate transformation of root cells into the syncytium. Despite the important predicted roles of effectors in the plant-pathogen interactions, the functionality of
<i>G. pallida</i>
effectors is largely unknown. In this study, we identified and characterized a
<i>G. pallida</i>
effector protein disulfide isomerase (GpPDI1). GpPDI1 contains two thioredoxin domains that function together to reduce disulfide bonds, as manifested by the nullification of enzymatic activity when either domain is absent. The transcript of
<i>GpPDI1</i>
is localized in the dorsal gland of the nematode during the J2 stage. In addition, GpPDI1 can trigger defense-related cell death in
<i>Nicotiana benthamiana</i>
and tomato (
<i>Solanum lycopersicum</i>
) leaf tissue and localizes in the plant host cell's cytoplasm and nucleus when transiently expressed in plant cells. Significantly, the ability of elicitation of cell death is not dependent on the enzymatic activity of GpPDI1 or correlated with the subcellular distribution of GpPDI1, suggesting that a nondisulfide reducing function or structural feature of GpPDI1 is responsible for the recognition by the host immune system to elicit cell death.</AbstractText>
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<AffiliationInfo>
<Affiliation>Northwest A&F University, College of Horticulture, Yangling, Shaanxi 712100, China.</Affiliation>
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<Affiliation>Department of Entomology, Plant Pathology and Nematology, University of Idaho, Moscow, ID 83843, U.S.A.</Affiliation>
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<Affiliation>Northwest A&F University, College of Horticulture, Yangling, Shaanxi 712100, China.</Affiliation>
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<ForeName>Fangming</ForeName>
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<AffiliationInfo>
<Affiliation>Department of Plant Sciences, University of Idaho, Moscow, ID 83843, U.S.A.</Affiliation>
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<DescriptorName UI="D014026" MajorTopicYN="N">Tobacco</DescriptorName>
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<name sortKey="Caplan, Allan" sort="Caplan, Allan" uniqKey="Caplan A" first="Allan" last="Caplan">Allan Caplan</name>
<name sortKey="Dandurand, Louise Marie" sort="Dandurand, Louise Marie" uniqKey="Dandurand L" first="Louise-Marie" last="Dandurand">Louise-Marie Dandurand</name>
<name sortKey="Kuhl, Joseph" sort="Kuhl, Joseph" uniqKey="Kuhl J" first="Joseph" last="Kuhl">Joseph Kuhl</name>
<name sortKey="Xiao, Fangming" sort="Xiao, Fangming" uniqKey="Xiao F" first="Fangming" last="Xiao">Fangming Xiao</name>
<name sortKey="Zhang, Shan" sort="Zhang, Shan" uniqKey="Zhang S" first="Shan" last="Zhang">Shan Zhang</name>
</country>
<country name="République populaire de Chine">
<noRegion>
<name sortKey="Zhang, Shan" sort="Zhang, Shan" uniqKey="Zhang S" first="Shan" last="Zhang">Shan Zhang</name>
</noRegion>
<name sortKey="Wang, Xiaofang" sort="Wang, Xiaofang" uniqKey="Wang X" first="Xiaofang" last="Wang">Xiaofang Wang</name>
<name sortKey="Wei, Lihui" sort="Wei, Lihui" uniqKey="Wei L" first="Lihui" last="Wei">Lihui Wei</name>
</country>
</tree>
</affiliations>
</record>

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