ArticleProtein science : a publication of the Protein Society2008
Solution structure of the C-terminal domain of Ole e 9, a major allergen of olive pollen.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed.
- Safety evaluation of the food enzyme endo-1,3(4)-β-glucanase from the non-genetically modifiedEFSA journal. European Food Safety Authority · 2024Article
- Safety evaluation of the food enzyme endo-1,3(4)-β-glucanase from the non-genetically modifiedEFSA journal. European Food Safety Authority · 2023Article
- Properties of a family 56 carbohydrate-binding module and its role in the recognition and hydrolysis of β-1,3-glucan.The Journal of biological chemistry · 2017Article
- Structural studies of novel glycoconjugates from polymerized allergens (allergoids) and mannans as allergy vaccines.Glycoconjugate journal · 2016Article
- Molecular Interactions of β-(1→3)-Glucans with Their Receptors.Molecules (Basel, Switzerland) · 2015Review
- An Enzymatically Active β-1,3-Glucanase from Ash Pollen with Allergenic Properties: A Particular Member in the Oleaceae Family.PloS one · 2015Article
- Allergen ligands in the initiation of allergic sensitization.Current allergy and asthma reports · 2014Article
- Structure of allergens and structure based epitope predictions.Methods (San Diego, Calif.) · 2014Review
- Current overview of allergens of plant pathogenesis related protein families.TheScientificWorldJournal · 2014Review
- Identification of critical amino acids in an immunodominant IgE epitope of Pen c 13, a major allergen from Penicillium citrinum.PloS one · 2012Article
- Molecular mechanisms of yeast cell wall glucan remodeling.The Journal of biological chemistry · 2009Article
- An Arabidopsis GPI-anchor plasmodesmal neck protein with callose binding activity and potential to regulate cell-to-cell trafficking.The Plant cell · 2009Article
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8 authors.
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Abstract
Ole e 9 is an olive pollen allergen belonging to group 2 of pathogenesis-related proteins. The protein is composed of two immunological independent domains: an N-terminal domain (NtD) with 1,3-beta-glucanase activity, and a C-terminal domain (CtD) that binds 1,3-beta-glucans. We have determined the three-dimensional structure of CtD-Ole e 9 (101 amino acids), which consists of two parallel alpha-helices forming an angle of approximately 55 degrees , a small antiparallel beta-sheet with two short strands, and a 3-10 helix turn, all connected by long coil segments, resembling a novel type of folding among allergens. Two regions surrounded by aromatic residues (F49, Y60, F96, Y91 and Y31, H68, Y65, F78) have been localized on the protein surface, and a role for sugar binding is suggested. The epitope mapping of CtD-Ole e 9 shows that B-cell epitopes are mainly located on loops, although some of them are contained in secondary structural elements. Interestingly, the IgG and IgE epitopes are contiguous or overlapped, rather than coincident. The three-dimensional structure of CtD-Ole e 9 might help to understand the underlying mechanism of its biochemical function and to determine possible structure-allergenicity relationships.
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