ArticleThe Journal of biological chemistry2016
Structural, Functional, and Immunological Characterization of Profilin Panallergens Amb a 8, Art v 4, and Bet v 2.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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Who cites it
25 citing papers in PubMed, 41 citations in OpenAlex.
- Amb a 1-Specific IgE in Heart Failure: A Translational Framework for Seasonal Risk, Endotyping, and Patient-Centered Management.Journal of clinical medicine · 2026Review
- Developmental and quantitative expression profile of the six pollen allergens of mugwort (Artemisia vulgaris L.).BMC plant biology · 2025Article
- Global Ragweed Allergy: Molecular Allergens and Integrated Control Strategies.Journal of asthma and allergy · 2025Review
- Heterogenous Induction of Blocking Antibodies against Ragweed Allergen Molecules by Allergen Extract-Based Immunotherapy Vaccines.Vaccines · 2024Article
- Worldwide Heterogeneity of Food Allergy: Focus on Peach Allergy in Southern Italy.Journal of clinical medicine · 2024Review
- Article
- Molecular Basis of Plant Profilins' Cross-Reactivity.Biomolecules · 2023Article
- A native IgE in complex with profilin provides insights into allergen recognition and cross-reactivity.Communications biology · 2022Article
- Complex IgE sensitization patterns in ragweed allergic patients: Implications for diagnosis and specific immunotherapy.Clinical and translational allergy · 2022Article
- pH-dependent structural diversity of profilin allergens determines thermal stability.Frontiers in allergy · 2022Article
- How Do Pollen Allergens Sensitize?Frontiers in molecular biosciences · 2022Review
- Crystal structure of timothy grass allergen Phl p 12.0101 reveals an unusual profilin dimer.Acta biochimica Polonica · 2021Article
- Crosstalk Between the Immune System and Plant-Derived Nanovesicles: A Study of Allergen Transporting.Frontiers in bioengineering and biotechnology · 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
- Structural and computational examination of theThe Journal of biological chemistry · 2019Article
- Analysis of Pollen Allergens in Lily by Transcriptome and Proteome Data.International journal of molecular sciences · 2019Article
- Comparative structural and thermal stability studies of Cuc m 2.0101, Art v 4.0101 and other allergenic profilins.Molecular immunology · 2019Article
- Mugwort Pollen-Related Food Allergy: Lipid Transfer Protein Sensitization and Correlation With the Severity of Allergic Reactions in a Chinese Population.Allergy, asthma & immunology research · 2019Article
- Molecular patterns in the isotype-specific antibody responses to the major cedar aeroallergen Jun a 1.Molecular immunology · 2018Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Ragweed allergens affect several million people in the United States and Canada. To date, only two ragweed allergens, Amb t 5 and Amb a 11, have their structures determined and deposited to the Protein Data Bank. Here, we present structures of methylated ragweed allergen Amb a 8, Amb a 8 in the presence of poly(l-proline), and Art v 4 (mugwort allergen). Amb a 8 and Art v 4 are panallergens belonging to the profilin family of proteins. They share significant sequence and structural similarities, which results in cross-recognition by IgE antibodies. Molecular and immunological properties of Amb a 8 and Art v 4 are compared with those of Bet v 2 (birch pollen allergen) as well as with other allergenic profilins. We purified recombinant allergens that are recognized by patient IgE and are highly cross-reactive. It was determined that the analyzed allergens are relatively unstable. Structures of Amb a 8 in complex with poly(l-proline)10 or poly(l-proline)14 are the first structures of the plant profilin in complex with proline-rich peptides. Amb a 8 binds the poly(l-proline) in a mode similar to that observed in human, mouse, and P. falciparum profilin·peptide complexes. However, only some of the residues that form the peptide binding site are conserved.
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Registered trials
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