ArticleThe Biochemical journal2005
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.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.
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Who cites it
33 citing papers in PubMed, 1 synthesis or guideline pooled it, 88 citations in OpenAlex.
- Whole-genome meta-analysis coupled with haplotype analysis reveal new genes and functional haplotypes conferring pre-harvest sprouting in rice.BMC plant biology · 2025Pooled it
- Exploring the role of β-1,3-glucanase in aerenchyma development in sugarcane roots.Annals of botany · 2026Article
- Analysis of Wheat Pollen Ole E I Proteins Reveals Potential Roles in Fertility and Stress Adaptation.International journal of molecular sciences · 2025Article
- Genome-Wide Identification and Analysis of Carbohydrate-Binding Modules inInternational journal of molecular sciences · 2025Article
- Genome-wide identification of GH17 family genes and their expression patterns associated with bud dormancy-regrowth regulation inFrontiers in plant science · 2025Article
- Comprehensive Proteomic Analysis of Common Bean (Biomolecules · 2024Article
- Article
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- Characterization of an Unknown Region Linked to the Glycoside Hydrolase Family 17 β-1,3-Glucanase ofMarine drugs · 2022Article
- Enzymatic fingerprinting reveals specific xyloglucan and pectin signatures in the cell wall purified with primary plasmodesmata.Frontiers in plant science · 2022Article
- Basic β-1,3-Glucanase fromPlants (Basel, Switzerland) · 2021Article
- Intercellular trafficking via plasmodesmata: molecular layers of complexity.Cellular and molecular life sciences : CMLS · 2021Review
- Comparative Transcriptome Analysis inFrontiers in genetics · 2021Article
- Absence of the highly expressed small carbohydrate-binding protein Cgt improves the acarbose formation in Actinoplanes sp. SE50/110.Applied microbiology and biotechnology · 2020Article
- Expression, purification, and characterization of the recombinant exo-1,3-β-glucanase (Exo1) of the pathogenic oomyceteHeliyon · 2020Article
- Poplar carbohydrate-active enzymes: whole-genome annotation and functional analyses based on RNA expression data.The Plant journal : for cell and molecular biology · 2019Article
- Transcriptome Analysis of Intrusively Growing Flax Fibers Isolated by Laser Microdissection.Scientific reports · 2018Article
- Molecular characterization and evolution of carnivorous sundew (Drosera rotundifolia L.) class V β-1,3-glucanase.Planta · 2017Article
- Glycosylphosphatidylinositol (GPI) Modification Serves as a Primary Plasmodesmal Sorting Signal.Plant physiology · 2016Article
- Origin and Functional Prediction of Pollen Allergens in Plants.Plant physiology · 2016Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CBMs (carbohydrate-binding modules) are the most common non-catalytic modules associated with enzymes active in plant cell-wall hydrolysis. They have been frequently identified by amino acid sequence alignments, but only a few have been experimentally established to have a carbohydrate-binding activity. A small olive pollen protein, Ole e 10 (10 kDa), has been described as a major inducer of type I allergy in humans. In the present study, the ability of Ole e 10 to bind several polysaccharides has been analysed by affinity gel electrophoresis, which demonstrated that the protein bound 1,3-beta-glucans preferentially. Analytical ultracentrifugation studies confirmed binding to laminarin, at a protein/ligand ratio of 1:1. The interaction of Ole e 10 with laminarin induced a conformational change in the protein, as detected by CD and fluorescence analyses, and an increase of 3.6 degrees C in the thermal denaturation temperature of Ole e 10 in the presence of the glycan. These results, and the absence of alignment of the sequence of Ole e 10 with that of any classified CBM, indicate that this pollen protein defines a novel family of CBMs, which we propose to name CBM43. Immunolocalization of Ole e 10 in mature and germinating pollen by transmission electron microscopy and confocal laser scanning microscopy demonstrated the co-localization of Ole e 10 and callose (1,3-beta-glucan) in the growing pollen tube, suggesting a role for this protein in the metabolism of carbohydrates and in pollen tube wall re-formation during germination.
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