English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

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.

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