Evidence map›Paper›PMID 28960341›Full record

ArticleAllergy2018

Distinct epitope structures of defensin-like proteins linked to proline-rich regions give rise to differences in their allergenic activity.

I Pablos, S Eichhorn, Y Machado, P Briza, A Neunkirchner, B Jahn-Schmid, S Wildner, W T Soh, C Ebner, J-W Park and 5 more

Open access · hybridAbstract read
In one paragraph

Article in Allergy, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  4. Review
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  6. Article
  7. Review
  8. Article
  9. Article
  10. Relationship between serum inhibitory activity for IgE and efficacy of Artemisia pollen subcutaneous immunotherapy for allergic rhinitis: a preliminary self-controlled study.Allergy, asthma, and clinical immunology : official journal of the Canadian Society of Allergy and Clinical Immunology · 2020
    Article
  11. Article
  12. Review
  13. Article
  14. Similar Allergenicity to DifferentMedicina (Kaunas, Lithuania) · 2019
    Article
  15. Article
  16. Article
  17. Article
  18. Anaphylactic reaction in patient allergic to mango.Allergy, asthma, and clinical immunology : official journal of the Canadian Society of Allergy and Clinical Immunology · 2018
    Article
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

15 authors at 5 institutions in 4 countries.

I PablosDivision of Allergy and Immunology, Department of Molecular Biology, University of Salzburg, Salzburg, Austria.
S EichhornDivision of Allergy and Immunology, Department of Molecular Biology, University of Salzburg, Salzburg, Austria.
Y MachadoDivision of Allergy and Immunology, Department of Molecular Biology, University of Salzburg, Salzburg, Austria.
P BrizaDivision of Allergy and Immunology, Department of Molecular Biology, University of Salzburg, Salzburg, Austria.
A NeunkirchnerCenter for Pathophysiology, Infectiology and Immunology, Institute of Immunology, Medical University of Vienna, Vienna, Austria.
B Jahn-SchmidDepartment of Pathophysiology and Allergy Research, Medical University of Vienna, Vienna, Austria.ORCID 0000-0002-7979-6667
S WildnerDivision of Allergy and Immunology, Department of Molecular Biology, University of Salzburg, Salzburg, Austria.
W T SohDivision of Allergy and Immunology, Department of Molecular Biology, University of Salzburg, Salzburg, Austria.ORCID 0000-0003-0082-7983
C EbnerAllergy Clinic Reumannplatz, Vienna, Austria.
J-W ParkDepartment of Internal Medicine and Institute of Allergy, Yonsei University College of Medicine, Seoul, Korea.ORCID 0000-0003-0249-8749
W F PicklCenter for Pathophysiology, Infectiology and Immunology, Institute of Immunology, Medical University of Vienna, Vienna, Austria.ORCID 0000-0003-0430-4952
N AroraAllergy and Immunology Section, CSIR-Institute of Genomic and Integrative Biology, Delhi, India.ORCID 0000-0001-5115-1034
S ViethsDivision of Allergology, Paul-Ehrlich-Institut, Langen, Germany.
F FerreiraDivision of Allergy and Immunology, Department of Molecular Biology, University of Salzburg, Salzburg, Austria.ORCID 0000-0003-0989-2335
G GadermaierDivision of Allergy and Immunology, Department of Molecular Biology, University of Salzburg, Salzburg, Austria.ORCID 0000-0002-4886-417X
University of Salzburg · ATMedical University of Vienna · ATInstitute of Genomics and Integrative Biology · INPaul Ehrlich Institut · DEYonsei University · KR

Funding

Austrian Science Fund FWF I 1152
6 · The paper itself

Abstract

backgroundArt v 1, Amb a 4, and Par h 1 are allergenic defensin-polyproline-linked proteins present in mugwort, ragweed, and feverfew pollen, respectively. We aimed to investigate the physicochemical and immunological features underlying the different allergenic capacities of those allergens.

methodsRecombinant defensin-polyproline-linked proteins were expressed in E. coli and physicochemically characterized in detail regarding identity, secondary structure, and aggregation status. Allergenic activity was assessed by mediator releases assay, serum IgE reactivity, and IgE inhibition ELISA using sera of patients from Austria, Canada, and Korea. Endolysosomal protein degradation and T-cell cross-reactivity were studied in vitro.

resultsDespite variations in the proline-rich region, similar secondary structure elements were observed in the defensin-like domains. Seventy-four percent and 52% of the Austrian and Canadian patients reacted to all three allergens, while Korean patients were almost exclusively sensitized to Art v 1. This was reflected by IgE inhibition assays demonstrating high cross-reactivity for Austrian, medium for Canadian, and low for Korean sera. In a subgroup of patients, IgE reactivity toward structurally altered Amb a 4 and Par h 1 was not changed suggesting involvement of linear epitopes. Immunologically relevant endolysosomal stability of the defensin-like domain was limited to Art v 1 and no T-cell cross-reactivity with Art v 1

conclusionsDespite structural similarity, different IgE-binding profiles and proteolytic processing impacted the allergenic capacity of defensin-polyproline-linked molecules. Based on the fact that Amb a 4 demonstrated distinct IgE-binding epitopes, we suggest inclusion in molecule-based allergy diagnosis.

Indexed as

AllergensAmbrosiaArtemisiaAustriaCanadaDefensinsEnzyme-Linked Immunosorbent AssayEpitopesHumansHypersensitivityPlant ProteinsPollenProlineRepublic of KoreaAllergensDefensinsEpitopesPlant ProteinsProlineallergens and epitopesAmb a 4Art v 1defensin-like allergenweed pollen allergy

Identifiers

PMID28960341
PMCPMC5771466
OpenAlexW2760388238

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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.