ArticleMolecular immunology2019
Comparative structural and thermal stability studies of Cuc m 2.0101, Art v 4.0101 and other allergenic profilins.
Article in Molecular immunology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 30 citations in OpenAlex.
- Review
- Update on hazelnut allergy: Allergen characterization, epidemiology, food processing technique and detecting strategy.Comprehensive reviews in food science and food safety · 2025Review
- A systematic review of allergen cross-reactivity: Translating basic concepts into clinical relevance.The journal of allergy and clinical immunology. Global · 2024Review
- Detection of Bet v 1 Homologous Proteins and Plant Profilins by Indirect ELISA.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Article
- Food Allergens of Plant Origin.Foods (Basel, Switzerland) · 2023Review
- Molecular Basis of Plant Profilins' Cross-Reactivity.Biomolecules · 2023Article
- Crystal structure of timothy grass allergen Phl p 12.0101 reveals an unusual profilin dimer.Acta biochimica Polonica · 2021Article
- Production and Use of Recombinant Profilins Amb a 8, Art v 4, Bet v 2, and Phl p 12 for Allergenic Sensitization Studies.Molecules (Basel, Switzerland) · 2020Article
- Molecular approach to a patient's tailored diagnosis of the oral allergy syndrome.Clinical and translational allergy · 2020Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Worldwide, more than one-third of the population suffers from allergies. A significant fraction of officially registered allergens originate from the profilin family of proteins. Profilins are small ubiquitous proteins which are found in plants, viruses and various eukaryotes including mammals. Although they are primarily regarded as minor allergens, profilins are important players in immunoglobulin E (IgE) cross-reactivity. However, in some populations profilins are recognized by IgE from at least 50% of patients allergic to a given allergen source. Cuc m 2.0101 is recognized by IgE in more than 80% of muskmelon-allergic patients. The recombinant isoallergen Cuc m 2.0101 was produced in significant quantities and its X-ray crystal structure was determined. In addition, a new Art v 4.0101 (mugwort profilin) structure was determined. The profilins Cuc m 2.0101 and Art v 4.0101 were compared in terms of their structure and thermal stability. Furthermore, structural similarities and IgE cross-reactivity between profilins from different sources are discussed to explain the molecular basis of various clinical syndromes involving this group of allergens. Special emphasis is placed on discussion of profilins' quaternary structures and their relation to biological function, as well as to protein allergenicity. Moreover, a potential impact of protein purification protocols on the structure of profilins is highlighted.
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Registered trials
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