Evidence map›Paper›PMID 32099050›Full record

ArticleScientific reports2020

Antigenic cross-reactivity between Schistosoma mansoni and allergenic invertebrates putatively due to shared glycanic epitopes.

Marwa H El-Faham, Fatou Gai, Joseph E Igetei, Sarah Richter, Franco H Falcone, Gabi Schramm, Michael J Doenhoff

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 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
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  4. Observational
  5. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 4 countries.

Marwa H El-Faham *School of Life Sciences, University Park, University of Nottingham, Nottinghamshire, NG7 2RD, UK.
Fatou Gai *School of Pharmacy, Division of Molecular Therapeutics and Formulation, University of Nottingham, Nottingham, NG7 2RD, UK. paxfg3@nottingham.ac.uk.
Joseph E IgeteiSchool of Life Sciences, University Park, University of Nottingham, Nottinghamshire, NG7 2RD, UK.
Sarah RichterSchool of Life Sciences, University Park, University of Nottingham, Nottinghamshire, NG7 2RD, UK.
Franco H FalconeSchool of Pharmacy, Division of Molecular Therapeutics and Formulation, University of Nottingham, Nottingham, NG7 2RD, UK.
Gabi SchrammExperimental Pneumology, Research Center Borstel, Airway Research Center North, Member of the German Center for Lung Research (DZL), Parkallee 22, D-23845, Borstel, Germany.
Michael J DoenhoffSchool of Life Sciences, University Park, University of Nottingham, Nottinghamshire, NG7 2RD, UK.
University of Nottingham · GBAlexandria University · EGGerman Center for Lung Research · DEUniversity of Hohenheim · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Previous studies have shown that rabbit IgG antibodies against Schistosoma mansoni egg antigens (SmSEA) cross-react with allergens in natural rubber latex, peanuts and grass and tree pollens. Here we describe antigenic molecules that cross-react with rabbit anti-S. mansoni IgG antibodies in extracts of the house dust mite (HDM) Dermatophagoides farinae, the Australian cockroach (ACR) Periplaneta australasiae and in the venom of the honey bee Apis mellifera (HBV). Tandem mass spectrometry identified the cross-reactive allergens as Der f 15 in HDM, two homologues of the Periplaneta americana cockroach allergen Cr-PI/Per a 3 in ACR and two isoforms of the allergen Api m 1 (phospholipase A2: PLA2) in HBV. Cross-reactive rabbit anti-SmSEA IgG antibodies eluted from the three invertebrate allergens reacted with S. mansoni egg antigens and variably with schistosome cercarial and worm antigens. Treatment of the electroblotted allergens with sodium metaperiodate abrogated most of the cross-reactivity of the rabbit anti-SmSEA antibodies, suggesting it was due to cross-reactive carbohydrate determinants (CCDs). Furthermore, analyses of the allergens' amino acid sequences indicated that they had potential for both N- and O-linked glycosylation. A potential role for the CCDs shared by the schistosome and invertebrates in inducing an allergy-protective effect, as proposed by the hygiene hypothesis, is discussed.

Indexed as

AllergensAmino Acid SequenceAnimalsAntigens, DermatophagoidesBeesBee VenomsCockroachesCross ReactionsEpitopesGlycosylationHumansPolysaccharidesPyroglyphidaeRabbitsSchistosoma mansoniTandem Mass SpectrometryAllergensAntigens, DermatophagoidesBee VenomsEpitopesPolysaccharides

Identifiers

PMID32099050
PMCPMC7042331
OpenAlexW3008349641

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.