Evidence map›Paper›PMID 33444331›Full record

ArticlePloS one2021

Xyloglucan endotransglycosylase/hydrolase increases tightly-bound xyloglucan and chain number but decreases chain length contributing to the defense response that Glycine max has to Heterodera glycines.

Prakash M Niraula, Xuefeng Zhang, Dragica Jeremic, Katherine S Lawrence, Vincent P Klink

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
5.1field-weighted citation impact, top 5% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Structure and growth of plant cell walls.Nature reviews. Molecular cell biology · 2024
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Frontiers in plant science · 2022
    Article
  14. Article
  15. Review
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

5 authors at 3 institutions in 1 country.

Prakash M NiraulaDepartment of Biological Sciences, Mississippi State University, Starkville, Mississippi State, United States of America.
Xuefeng ZhangDepartment of Sustainable Bioproducts, Mississippi State University, Starkville, Mississippi State, United States of America.ORCID 0000-0003-1654-3969
Dragica JeremicDepartment of Sustainable Bioproducts, Mississippi State University, Starkville, Mississippi State, United States of America.
Katherine S LawrenceDepartment of Entomology and Plant Pathology, Auburn University, Auburn, Alabama, United States of America.
Vincent P KlinkDepartment of Biological Sciences, Mississippi State University, Starkville, Mississippi State, United States of America.ORCID 0000-0002-7167-4032
Mississippi State University · USAuburn University · USNaval Research Laboratory Information Technology Division

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Glycine max xyloglucan endotransglycosylase/hydrolase (EC 2.4.1.207), GmXTH43, has been identified through RNA sequencing of RNA isolated through laser microdissection of Heterodera glycines-parasitized root cells (syncytia) undergoing the process of defense. Experiments reveal that genetically increasing XTH43 transcript abundance in the H. glycines-susceptible genotype G. max[Williams 82/PI 518671] decreases parasitism. Experiments presented here show decreasing XTH43 transcript abundance through RNA interference (RNAi) in the H. glycines-resistant G. max[Peking/PI 548402] increases susceptibility, but it is unclear what role XTH43 performs. The experiments presented here show XTH43 overexpression decreases the relative length of xyloglucan (XyG) chains, however, there is an increase in the amount of those shorter chains. In contrast, XTH43 RNAi increases XyG chain length. The experiments show that XTH43 has the capability to function, when increased in its expression, to limit XyG chain extension. This outcome would likely impair the ability of the cell wall to expand. Consequently, XTH43 could provide an enzymatically-driven capability to the cell that would allow it to limit the ability of parasitic nematodes like H. glycines to develop a feeding structure that, otherwise, would facilitate parasitism. The experiments presented here provide experimentally-based proof that XTHs can function in ways that could be viewed as being able to limit the expansion of the cell wall.

Indexed as

AnimalsChromatography, GelFemaleGenotypeGlucansGlycine maxGlycosyltransferasesHost-Parasite InteractionsMolecular WeightPlant ProteinsPlant RootsPlants, Genetically ModifiedPrincipal Component AnalysisRNA InterferenceRNA, Small InterferingTylenchidaGlucansGlycosyltransferasesPlant ProteinsRNA, Small InterferingXylansxyloglucanxyloglucan endotransglycosylase

Identifiers

PMID33444331
PMCPMC7808671
OpenAlexW3120806367

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.