ArticleMolecules (Basel, Switzerland)2020
Production and Use of Recombinant Profilins Amb a 8, Art v 4, Bet v 2, and Phl p 12 for Allergenic Sensitization Studies.
Article in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Common Ragweed Allergy Under Global Change Linking Invasion-Driven Aeroallergen Exposure with Molecular Sensitization and Allergic Airway Disease.Life (Basel, Switzerland) · 2026Review
- Advances in clinical examination techniques for allergic rhinitis: a review from traditional testing to precision diagnosis.Frontiers in allergy · 2026Review
- Can Physicochemical Properties Alter the Potency of Aeroallergens? Part 2 - Impact of Physicochemical Properties.Current allergy and asthma reports · 2024Review
- Profile of cross-reactivity to common pollen allergens in Northwest China based on component resolved diagnosis.Scientific reports · 2024Article
- Heterogenous Induction of Blocking Antibodies against Ragweed Allergen Molecules by Allergen Extract-Based Immunotherapy Vaccines.Vaccines · 2024Article
- Detection of Bet v 1 Homologous Proteins and Plant Profilins by Indirect ELISA.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Molecular Basis of Plant Profilins' Cross-Reactivity.Biomolecules · 2023Article
- Component-Resolved Diagnosis Based on a Recombinant Variant of Mus m 1 Lipocalin Allergen.International journal of molecular sciences · 2023Article
- pH-dependent structural diversity of profilin allergens determines thermal stability.Frontiers in allergy · 2022Article
- Crystal structure of timothy grass allergen Phl p 12.0101 reveals an unusual profilin dimer.Acta biochimica Polonica · 2021Article
- Multiplicity of carotene patterns derives from competition between phytoene desaturase diversification and biological environments.Scientific reports · 2020Article
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Authors and funding
10 authors.
Funding
Abstract
Four recombinant (r) allergens (rAmb a 8.0101, rArt v 4.0101, rBet v 2.0101, and rPhl p 12.0101) were successfully produced and used for sensitization studies. The allergens belong to the profilin family which is one of the most numerous allergen families. These four proteins represent allergens originating from pollen of weeds (rAmb a 8.0101 and rArt v 4.0101), tree (rBet v 2.0101) and grass (rPhl p 12.0101). The recombinant allergens were characterized using various biochemical and biophysical methods and tested for their ability to bind patient-derived antibodies. One hundred patients aged 2 to 50 years sensitized to pollen and plant-derived food allergens (IgE > 0.35 kU/L) were included. Sensitization to individual allergen sources and components of birch and timothy pollens was evaluated using multiparameter immunoblots. The presence of IgE to pollen-derived recombinant profilins rAmb a 8.0101, rArt v 4.0101, rBet v 2.0101, and rPhl p 12.0101 in serum was evaluated using ELISA method. The presence of IgE against pollen profilins was detected in 20 out of 100 studied patients. High correlation was seen between IgE ELISA results with individual pollen profilins. In summary, it was shown that the recombinant versions of the four allergenic profilins can be used for sensitization studies and for component-resolved allergy diagnostics.
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