Evidence map›Paper›PMID 29051538›Full record

ArticleScientific reports2017

Identification and characterization of a putative protein disulfide isomerase (HsPDI) as an alleged effector of Heterodera schachtii.

Samer S Habash, Miroslaw Sobczak, Shahid Siddique, Boris Voigt, Abdelnaser Elashry, Florian M W Grundler

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
8.6field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
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  7. The Plant Sesquiterpene Nootkatone Efficiently ReducesInternational journal of molecular sciences · 2020
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Samer S HabashRheinische Friedrich-Wilhelms-University of Bonn, INRES - Molecular Phytomedicine, Karlrobert-Kreiten-Straße 13, D-53115, Bonn, Germany.
Miroslaw SobczakDepartment of Botany, Warsaw University of Life Sciences (SGGW), Nowoursynowska 159, PL-02787, Warsaw, Poland.
Shahid SiddiqueRheinische Friedrich-Wilhelms-University of Bonn, INRES - Molecular Phytomedicine, Karlrobert-Kreiten-Straße 13, D-53115, Bonn, Germany.
Boris VoigtRheinische Friedrich-Wilhelms-University of Bonn, Department of Plant Cell Biology, Institute of Cellular and Molecular Botany, Kirschallee 1, D-53115, Bonn, Germany.
Abdelnaser ElashryRheinische Friedrich-Wilhelms-University of Bonn, INRES - Molecular Phytomedicine, Karlrobert-Kreiten-Straße 13, D-53115, Bonn, Germany.
Florian M W GrundlerRheinische Friedrich-Wilhelms-University of Bonn, INRES - Molecular Phytomedicine, Karlrobert-Kreiten-Straße 13, D-53115, Bonn, Germany. grundler@uni-bonn.de.
University of Bonn · DEWarsaw University of Life Sciences · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The plant-parasitic nematode Heterodera schachtii is an obligate biotroph that induces syncytial feeding sites in roots of its hosts. Nematodes produce effectors that are secreted into the host and facilitate infection process. Here we identified H. schachtii protein disulphide isomerase (HsPDI) as a putative effector that interferes with the host's redox status. In situ hybridization showed that HsPdi is specifically localized within esophageal glands of pre-parasitic second stage juveniles (J2). HsPdi is up-regulated in the early parasitic J2s. Silencing of HsPdi by RNA interference in the J2s hampers their development and leads to structural malfunctions in associated feeding sites induced in Arabidopsis roots. Expression of HsPDI in Arabidopsis increases plant's susceptibility towards H. schachtii. HsPdi expression is up-regulated in the presence of exogenous H

Indexed as

Amino Acid SequenceAnimalsArabidopsisFemaleGiant CellsHelminth ProteinsHost-Parasite InteractionsHydrogen PeroxideMalePlant RootsPlants, Genetically ModifiedProtein Disulfide-IsomerasesReactive Oxygen SpeciesRNA, Double-StrandedRNA InterferenceTylenchoideaHelminth ProteinsHydrogen PeroxideProtein Disulfide-IsomerasesReactive Oxygen SpeciesRNA, Double-Stranded

Identifiers

PMID29051538
PMCPMC5648851
OpenAlexW2761941263

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.