Evidence map›Paper›PMID 33116178›Full record

ArticleScientific reports2020

Functional characterization of Schistosoma mansoni fucosyltransferases in Nicotiana benthamiana plants.

Kim van Noort, Dieu-Linh Nguyen, Verena Kriechbaumer, Chris Hawes, Cornelis H Hokke, Arjen Schots, Ruud H P Wilbers

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

14 citing papers in PubMed, 19 citations in OpenAlex.

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  13. β-Hexosaminidases Along the Secretory Pathway ofFrontiers in plant science · 2021
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 2 countries.

Kim van NoortLaboratory of Nematology, Plant Sciences Group, Wageningen University and Research, Droevendaalsesteeg 1, 6708 PB, Wageningen, The Netherlands.
Dieu-Linh NguyenDepartment of Parasitology, Leiden University Medical Center, Albinusdreef, 2333 ZA, Leiden, The Netherlands.
Verena KriechbaumerDepartment of Biological and Medical Sciences, Oxford Brookes University, Oxford, OX3 0BP, UK.
Chris HawesDepartment of Biological and Medical Sciences, Oxford Brookes University, Oxford, OX3 0BP, UK.
Cornelis H HokkeDepartment of Parasitology, Leiden University Medical Center, Albinusdreef, 2333 ZA, Leiden, The Netherlands.
Arjen SchotsLaboratory of Nematology, Plant Sciences Group, Wageningen University and Research, Droevendaalsesteeg 1, 6708 PB, Wageningen, The Netherlands.
Ruud H P WilbersLaboratory of Nematology, Plant Sciences Group, Wageningen University and Research, Droevendaalsesteeg 1, 6708 PB, Wageningen, The Netherlands. ruud.wilbers@wur.nl.
Wageningen University & Research · NLLeiden University Medical Center · NLOxford Brookes University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Helminth parasites secrete a wide variety of immunomodulatory proteins and lipids to dampen host immune responses. Many of these immunomodulatory compounds are modified with complex sugar structures (or glycans), which play an important role at the host-parasite interface. As an example, the human blood fluke Schistosoma mansoni produces highly fucosylated glycan structures on glycoproteins and glycolipids. Up to 20 different S. mansoni fucosyltransferase (SmFucT) genes can be found in genome databases, but thus far only one enzyme has been functionally characterized. To unravel the synthesis of highly fucosylated N-glycans by S. mansoni, we examined the ability of ten selected SmFucTs to modify N-glycans upon transient expression in Nicotiana benthamiana plants. All enzymes were localized in the plant Golgi apparatus, which allowed us to identify the SmFucTs involved in core fucosylation and the synthesis of complex antennary glycan motifs. This knowledge provides a starting point for investigations into the role of specific fucosylated glycan motifs of schistosomes in parasite-host interactions. The functionally characterized SmFucTs can also be applied to synthesize complex N-glycan structures on recombinant proteins to study their contribution to immunomodulation. Furthermore, this plant expression system will fuel the development of helminth glycoproteins for pharmaceutical applications or novel anti-helminth vaccines.

Indexed as

AnimalsAntibodies, HelminthAntigens, HelminthFucosyltransferasesGlycoproteinsGlycosylationHelminth ProteinsHost-Parasite InteractionsNicotianaParasitesPolysaccharidesSchistosoma mansoniAntibodies, HelminthAntigens, HelminthFucosyltransferasesGlycoproteinsHelminth ProteinsPolysaccharides

Identifiers

PMID33116178
PMCPMC7595089
OpenAlexW3095280334

What OpenQuestion holds

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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.