Evidence map›Paper›PMID 15138181›Full record

ArticleClinical and diagnostic laboratory immunology2004

Use of a synthetic peptide epitope of Asp f 1, a major allergen or antigen of Aspergillus fumigatus, for improved immunodiagnosis of allergic bronchopulmonary aspergillosis.

Taruna Madan, Priyanka Priyadarsiny, Mudit Vaid, Neel Kamal, Ashok Shah, Wahajul Haq, Seturam Bandacharya Katti, P Usha Sarma

Open access · diamondAbstract read
In one paragraph

Article in Clinical and diagnostic laboratory immunology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.4field-weighted citation impact, top 22% 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

9 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Aspergilli-aflatoxins: health threat.Indian journal of clinical biochemistry : IJCB · 2017
    Article
  3. Review
  4. Allergic aspergillosis of the respiratory tract.European respiratory review : an official journal of the European Respiratory Society · 2014
    Review
  5. Fascinating potential of aspergilli.Indian journal of clinical biochemistry : IJCB · 2010
    Article
  6. Article
  7. Review
  8. Article
  9. 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

8 authors at 3 institutions in 1 country.

Taruna MadanMolecular Biochemistry and Diagnostics, Institute of Genomics and Integrative Biology, Mall Rd., Delhi, India. u_sarma@hotmail.com
Priyanka Priyadarsiny
Mudit Vaid
Neel Kamal
Ashok Shah
Wahajul Haq
Seturam Bandacharya Katti
P Usha Sarma
Institute of Genomics and Integrative Biology · INCentral Drug Research Institute · INUniversity of Delhi · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Allergic bronchopulmonary aspergillosis (ABPA) is an immunologically complex allergic disorder caused by the fungal pathogen Aspergillus fumigatus. Elevated levels of total immunoglobulin E (IgE), specific IgE, and IgG antibodies in sera are important immunodiagnostic criteria for ABPA. International reference standards or standardized immunodiagnostic assays are not available due to a lack of well-defined diagnostic antigens. The present study was carried out to identify and evaluate the immunodiagnostic relevance of synthetic epitopic peptides of Asp f 1, a major allergen, antigen, or cytotoxin of A. fumigatus. Five overlapping peptides were synthesized from the N terminus of Asp f 1, one of the potential immunodominant regions predicted by algorithmic programs. The 11-amino-acid synthetic peptide (P1) significantly inhibited both IgG binding (89.10% +/- 4.45%) and IgE binding (77.32% +/- 3.38%) of the standardized diagnostic antigen (SDA) (a well-defined pool of diagnostically relevant allergens and antigens of A. fumigatus). With a panel of sera of ABPA patients, allergic patients with skin test negativity to A. fumigatus, and healthy individuals, P1 showed a higher diagnostic efficiency than SDA (specific IgG, 100%; specific IgE, 98.3%). The diagnostic efficiency of P1 could be attributed to the presence of homologous epitopes in various immunodominant allergens or antigens of A. fumigatus. The ability of P1 to induce histamine release from sensitized mast cells and a Th2 type of cytokine profile in peripheral blood mononuclear cells of ABPA patients suggests its potential for use in intradermal testing. P1 could be further explored for development of a standardized, specific, and sensitive immunodiagnostic test for aspergillosis.

Indexed as

EpitopesOligopeptidesAllergensAmino Acid SequenceAntibodies, MonoclonalAntibody SpecificityAntigensAntigens, PlantAspergillosis, Allergic BronchopulmonaryBasophilsBinding, CompetitiveBlotting, WesternCell ProliferationEnzyme-Linked Immunosorbent AssayFungal ProteinsHistamine ReleaseAllergensAntibodies, MonoclonalAntigensAntigens, PlantASPF1 protein, Aspergillus fumigatusEpitopesFungal ProteinsImmunoglobulin EImmunoglobulin GInterferon-gammaInterleukinsOligopeptides

Identifiers

PMID15138181
PMCPMC404572
OpenAlexW2163115178

What OpenQuestion holds

Textmetadata
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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.