Evidence map›Paper›PMID 28771001›Full record

ArticleJournal of agricultural and food chemistry2017

Abrogation of Immunogenic Properties of Gliadin Peptides through Transamidation by Microbial Transglutaminase Is Acyl-Acceptor Dependent.

Lin Zhou, Yvonne M C Kooy-Winkelaar, Robert A Cordfunke, Irina Dragan, Allan Thompson, Jan Wouter Drijfhout, Peter A van Veelen, Hongbing Chen, Frits Koning

Open access · hybridAbstract read
In one paragraph

Article in Journal of agricultural and food chemistry, 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
2.0field-weighted citation impact, top 14% 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, 31 citations in OpenAlex.

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  7. Characterization ofFoods (Basel, Switzerland) · 2021
    Article
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  13. Mechanisms by which gut microorganisms influence food sensitivities.Nature reviews. Gastroenterology & hepatology · 2019
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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

9 authors at 2 institutions in 2 countries.

Lin ZhouState Key Laboratory of Food Science and Technology, Nanchang University , Nanchang 330047, China.ORCID http://orcid.org/0000-0003-4900-7556
Yvonne M C Kooy-WinkelaarDepartment of Immunohematology and Blood Transfusion, Leiden University Medical Center , Leiden 2333 ZA, The Netherlands.
Robert A CordfunkeDepartment of Immunohematology and Blood Transfusion, Leiden University Medical Center , Leiden 2333 ZA, The Netherlands.
Irina DraganCenter for Proteomics & Metabolomics, Leiden University Medical Center , Leiden 2333 ZA, The Netherlands.
Allan ThompsonDepartment of Immunohematology and Blood Transfusion, Leiden University Medical Center , Leiden 2333 ZA, The Netherlands.
Jan Wouter DrijfhoutDepartment of Immunohematology and Blood Transfusion, Leiden University Medical Center , Leiden 2333 ZA, The Netherlands.
Peter A van VeelenCenter for Proteomics & Metabolomics, Leiden University Medical Center , Leiden 2333 ZA, The Netherlands.
Hongbing ChenState Key Laboratory of Food Science and Technology, Nanchang University , Nanchang 330047, China.
Frits KoningDepartment of Immunohematology and Blood Transfusion, Leiden University Medical Center , Leiden 2333 ZA, The Netherlands.
Leiden University Medical Center · NLNanchang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Wheat gluten confers superior baking quality to wheat based products but elicits a pro-inflammatory immune response in patients with celiac disease. Transamidation of gluten by microbial transglutaminase (mTG) and tissue transglutaminase (tTG) reduces the immunogenicity of gluten; however, little information is available on the minimal modification sufficient to eliminate gliadin immunogenicity nor has the effectiveness of transamidation been studied with T-cell clones from patients. Here we demonstrate that mTG can efficiently couple three different acyl-acceptor molecules, l-lysine, glycine ethyl ester, and hydroxylamine, to gliadin peptides and protein. While all three acyl-acceptor molecules were cross-linked to the same Q-residues, not all modifications were equally effective in silencing T-cell reactivity. Finally, we observed that tTG can partially reverse the mTG-catalyzed transamidation by its isopeptidase activity. These results set the stage to determine the impact of these modifications on the baking quality of gluten proteins and in vivo immunogenicity of such food products.

Indexed as

Bacterial ProteinsBiocatalysisGliadinGlutensHumansMolecular StructureStreptomycesT-LymphocytesTranexamic AcidTransglutaminasesBacterial ProteinsGliadinGlutensTranexamic AcidTransglutaminasesacyl-acceptor moleculegliadinimmunogenic propertiesmicrobial transglutaminasetransamidation

Identifiers

PMID28771001
PMCPMC5579586
OpenAlexW2743060350

What OpenQuestion holds

Textmetadata
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.