ArticleThe Biochemical journal2003
The C-terminal segment of the 1,3-beta-glucanase Ole e 9 from olive (Olea europaea) pollen is an independent domain with allergenic activity: expression in Pichia pastoris and characterization.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed, 43 citations in OpenAlex.
- Safety evaluation of a food enzyme containing cellulase and endo-1,3(4)-β-glucanase activities from the non-genetically modifiedEFSA journal. European Food Safety Authority · 2026Article
- Safety evaluation of the food enzyme containing cellulase and endo-1,3(4)-β-glucanase activities from the non-genetically modifiedEFSA journal. European Food Safety Authority · 2026Article
- Safety evaluation of the food enzyme containing endo-1,4-β-xylanase and endo-1,3(4)-β-glucanase from the non-genetically modifiedEFSA journal. European Food Safety Authority · 2026Article
- Safety evaluation of a food enzyme containing cellulase, endo-1,3(4)-β-glucanase and endo-1,4-β-xylanase activities from the non-genetically modifiedEFSA journal. European Food Safety Authority · 2026Article
- Safety evaluation of the food enzyme endo-1,3(4)-β-glucanase from the non-genetically modifiedEFSA journal. European Food Safety Authority · 2025Article
- 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
- Extra Virgin Olive Oil Quality as Affected by Yeast Species Occurring in the Extraction Process.Foods (Basel, Switzerland) · 2019Article
- An Enzymatically Active β-1,3-Glucanase from Ash Pollen with Allergenic Properties: A Particular Member in the Oleaceae Family.PloS one · 2015Article
- Molecular characterization of recombinant mus a 5 allergen from banana fruit.Molecular biotechnology · 2014Article
- Solution structure of the C-terminal domain of Ole e 9, a major allergen of olive pollen.Protein science : a publication of the Protein Society · 2008Article
- Three-dimensional structure of the catalytic domain of the yeast beta-(1,3)-glucan transferase Gas1: a molecular modeling investigation.Journal of molecular modeling · 2006Article
- NMR assignment of the C-terminal domain of Ole e 9, a major allergen from the olive tree pollen.Journal of biomolecular NMR · 2006Article
- An olive pollen protein with allergenic activity, Ole e 10, defines a novel family of carbohydrate-binding modules and is potentially implicated in pollen germination.The Biochemical journal · 2005Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several allergenic proteins, such as the 1,3-beta-glucanases, have been associated with plant defence responses. Ole e 9 (46 kDa) is a 1,3-beta-glucanase and major allergen from olive pollen, which is a principal cause of allergy in Mediterranean countries. Its C-terminal segment (101 amino acid residues) has been produced as a recombinant polypeptide in the yeast Pichia pastoris. The cDNA encoding the polypeptide was inserted into the plasmid vector pPICZalpha-A and overexpressed in KM71 yeast cells. The recombinant product was purified by size-exclusion chromatography followed by reversed-phase HPLC. Edman degradation, MS and CD were used to determine molecular properties of the recombinant polypeptide, which exhibited 16% alpha-helix and 30% beta-sheet as regular elements of secondary structure. Disulphide bridges of the molecule were determined at positions Cys-14-Cys-76, Cys-33-Cys-94 and Cys-39-Cys-48. The high IgE-binding capability of the recombinant C-terminal segment of Ole e 9 against sera from Ole e 9-sensitive individuals, which was determined by immunoblotting and ELISA inhibition, supported the proper folding of the polypeptide and the maintenance of antigenic properties that it exhibits as a part of the whole allergen. These data indicated that this portion of Ole e 9 constitutes an independent domain, which could be used to study its three-dimensional structure and function, as well as for clinical purposes such as diagnosis and specific immunotherapy. Since it shows sequence similarity with portions of 1,3-beta-glucanases from plant tissues and the Gas/Phr/Epd protein families involved in yeast morphogenesis, we suggest that this domain could play an equivalent functional role within these enzymes.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.