Evidence map›Paper›PMID 9784519›Full record

ArticleInfection and immunity1998

Immunological characterization of Asp f 2, a major allergen from Aspergillus fumigatus associated with allergic bronchopulmonary aspergillosis.

B Banerjee, P A Greenberger, J N Fink, V P Kurup

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

32 citing papers in PubMed, 108 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Fungi-A Component of the Oral Microbiome Involved in Periodontal Diseases.Advances in experimental medicine and biology · 2022
    Article
  6. Article
  7. At the metal-metabolite interface inMicrobiology (Reading, England) · 2021
    Article
  8. Review
  9. Article
  10. Article
  11. Zinc at the Host-Fungus Interface: How to Uptake the Metal?Journal of fungi (Basel, Switzerland) · 2020
    Review
  12. Article
  13. TheMolecular & cellular proteomics : MCP · 2020
    Article
  14. Enolase FromFrontiers in immunology · 2019
    Article
  15. Article
  16. Aspf2 FromFrontiers in immunology · 2018
    Article
  17. Article
  18. Article
  19. Review
  20. 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

4 authors at 2 institutions in 1 country.

B BanerjeeDepartment of Medicine, Division of Allergy-Immunology, The Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA.
P A Greenberger
J N Fink
V P Kurup
Medical College of Wisconsin · USNorthwestern University · US

Funding

ASPERGILLUS ALLERGENS AND ALLERGIC ASPERGILLOSISR01AI042349 · NIAID · MEDICAL COLLEGE OF WISCONSIN · PI KURUP, VISWANATH P · 1998 to 2000
$200k
NIAID NIH HHS AI 42349
6 · The paper itself

Abstract

The 37-kDa recombinant protein Asp f 2, encoding an allergen of Aspergillus fumigatus, was expressed in a prokaryotic expression system and immunologically evaluated for its functional and structural properties. The open reading frame for a 310-amino-acid-long protein was shown to encode a signal peptide of 31 amino acids. A native 37-kDa culture filtrate protein and a 55-kDa mycelial glycoprotein (gp55) exhibited complete N-terminal sequence homology to Asp f 2. A GenBank search for homologous proteins revealed 60 and 44% sequence homologies to the cytosolic protein ASPND1 from Aspergillus nidulans and fibrinogen binding protein from Candida albicans, respectively. The glycosylation sites and cysteine molecules are conserved in all the three proteins. The extracellular matrix protein laminin showed a dose-dependent interaction with Asp f 2. This protein, expressed as a major cell-associated protein within 24 h of in vitro fungal culture, comprises 20 to 40% of total fungal protein. Furthermore, both native and recombinant Asp f 2 exhibited specific immunoglobulin (IgE) binding with allergic bronchopulmonary aspergillosis (ABPA) and cystic fibrosis-ABPA patients, whereas A. fumigatus-sensitized allergic asthma and normal control subjects failed to show IgE binding with Asp f 2. These results indicate that Asp f 2 is a major allergen of A. fumigatus exhibiting IgE antibody binding with sera from patients with ABPA. The antigen should be explored further for its potential role in the differential diagnosis of A. fumigatus-associated allergic diseases.

Indexed as

AllergensAmino Acid SequenceAntibody SpecificityAntigens, FungalAspergillosis, Allergic BronchopulmonaryAspergillus fumigatusBase SequenceCell WallEpitopesFungal ProteinsImmunoglobulin ELamininMolecular Sequence DataProtein BindingProtein ConformationRecombinant Proteinsallergen Asp f 2, Aspergillus fumigatusAllergensAntigens, FungalEpitopesFungal ProteinsImmunoglobulin ELamininRecombinant Proteins

Identifiers

PMID9784519
PMCPMC108645
OpenAlexW1749084180

What OpenQuestion holds

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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.