ArticleThe World Allergy Organization journal2020
Proteomic identification of allergenic proteins in red oak (
Article in The World Allergy Organization journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Safety evaluation of the food enzyme non-reducing end α-l-arabinofuranosidase from the non-genetically modifiedEFSA journal. European Food Safety Authority · 2025Article
- Fructose biphosphate aldolase: A new cassava allergen.The World Allergy Organization journal · 2023Article
- Perspectives of Proteomics in Respiratory Allergic Diseases.International journal of molecular sciences · 2023Review
- Biochemical and clinical studies of putative allergens to assess what distinguishes them from other non-allergenic proteins in the same family.Transgenic research · 2022Article
- Identification of Allergenic Proteins in Velvet Mesquite (Life (Basel, Switzerland) · 2022Article
- Safety evaluation of the food enzyme non-reducing end α-l-arabinofuranosidase from the genetically modifiedEFSA journal. European Food Safety Authority · 2022Article
- Review
- Allergenicity assessment ofHeliyon · 2021Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundRed oak pollen is an important cause of allergic respiratory disease and it is widely distributed in North America and central Europe. To date, however, red oak pollen allergens have not been identified. Here, we describe the allergenic protein profile from red oak pollen.
methodsTotal proteins were extracted from red oak pollen using a modified phenolic extraction method, and, subsequently, proteins were separated by two-dimensional gel electrophoresis (2DE) for both total protein stain (Coomassie Blue) and immunoblotting. A pool of 8 sera from red oak sensitive patients was used to analyze blotted proteins. Protein spots were analyzed by Mass Spectrometry.
resultsElectrophoretic pattern of total soluble proteins showed higher intensity bands in the regions of 26-40 and 47-52 kDa. Two dimensional immunoblots using pool sera from patients revealed four allergenic proteins spots with molecular masses in the range from 50 to 55 kDa. Mass spectrometry analysis identified 8 proteins including Enolase 1 and Enolase 1 chloroplastic, Xylose isomerase (X1 isoform), mitochondrial Aldehyde dehydrogenase, UTP-Glusose-1-phosphate uridylyltransferase, Betaxylosidase/alpha-l-arabinofuranosidase and alpha- and beta subunits of ATP synthase.
conclusionsThis study has identified for first time 8 IgE binding proteins from red oak pollen. These findings will pave the way towards the development of new diagnostic and therapeutic modalities for red oak allergy.
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