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      Tree pollen allergens—an update from a molecular perspective

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          Abstract

          It is estimated that pollen allergies affect approximately 40% of allergic individuals. In general, tree pollen allergies are mainly elicited by allergenic trees belonging to the orders Fagales, Lamiales, Proteales, and Pinales. Over 25 years ago, the gene encoding the major birch pollen allergen Bet v 1 was the first such gene to be cloned and its product characterized. Since that time, 53 tree pollen allergens have been identified and acknowledged by the WHO/ IUIS allergen nomenclature subcommittee. Molecule‐based profiling of allergic sensitization has helped to elucidate the immunological connections of allergen cross‐reactivity, whereas advances in biochemistry have revealed structural and functional aspects of allergenic proteins. In this review, we provide a comprehensive overview of the present knowledge of the molecular aspects of tree pollen allergens. We analyze the geographic distribution of allergenic trees, discuss factors pivotal for allergic sensitization, and describe the role of tree pollen panallergens. Novel allergenic tree species as well as tree pollen allergens are continually being identified, making research in this field highly competitive and instrumental for clinical applications.

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          Most cited references77

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          Hemisphere-scale differences in conifer evolutionary dynamics.

          Fundamental differences in the distribution of oceans and landmasses in the Northern and Southern Hemispheres potentially impact patterns of biological diversity in the two areas. The evolutionary history of conifers provides an opportunity to explore these dynamics, because the majority of extant conifer species belong to lineages that have been broadly confined to the Northern or Southern Hemisphere during the Cenozoic. Incorporating genetic information with a critical review of fossil evidence, we developed an age-calibrated phylogeny sampling ∼80% of living conifer species. Most extant conifer species diverged recently during the Neogene within clades that generally were established during the later Mesozoic, but lineages that diversified mainly in the Southern Hemisphere show a significantly older distribution of divergence ages than their counterparts in the Northern Hemisphere. Our tree topology and divergence times also are best fit by diversification models in which Northern Hemisphere conifer lineages have higher rates of species turnover than Southern Hemisphere lineages. The abundance of recent divergences in northern clades may reflect complex patterns of migration and range shifts during climatic cycles over the later Neogene leading to elevated rates of speciation and extinction, whereas the scattered persistence of mild, wetter habitats in the Southern Hemisphere may have favored the survival of older lineages.
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            Structural and functional aspects of PR-10 proteins.

            Physical, chemical and biological stress factors, such as microbial infection, upregulate the transcription levels of a number of plant genes, coding for the so-called pathogenesis-related (PR) proteins. For PR proteins of class-10 (PR-10), the biological function remains unclear, despite two decades of scientific research. PR-10 proteins have a wide distribution throughout the plant kingdom and the class members share size and secondary structure organization. Throughout the years, we and other groups have determined the structures of a number of PR-10 proteins, both in the crystalline state by X-ray diffraction and in solution by NMR spectroscopy. Despite the accumulating structural information, our understanding of PR-10 function is still limited. PR-10 proteins are rather small (~ 160 amino acids) with a fold consisting of three α helices and seven antiparallel β strands. These structural elements enclose a large hydrophobic cavity that is most probably the key to their functional relevance. Also, the outer surface of these proteins is of extreme interest, as epitopes from a PR-10 subclass cause allergic reactions in humans. © 2013 The Authors Journal compilation © 2013 FEBS.
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              Current understanding of cross-reactivity of food allergens and pollen.

              Pollen-allergic patients frequently present allergic symptoms after ingestion of several kinds of plant-derived foods. The majority of these reactions is caused by four distinct cross-reactive structures that are present in birch pollen. Proteins that share common epitopes with Bet v 1, the major birch pollen allergen, occur in pollens of several tree species: apples, stone fruits, celery, carrot, nuts, and soybeans. Approximately 70% of our patients who are allergic to birch pollen may experience symptoms after consumption of foods from these groups. In contrast, two minor allergenic structures-profilins and cross-reactive carbohydrate determinants (CCD)-that sensitize approximately 10-20% of all pollen-allergic patients are also present in grass pollen and weed pollen. Moreover, IgE-binding proteins related to the birch pollen minor allergen Bet v 6 have been found in many vegetable foods such as apple, peach, orange, lychee fruit, strawberry, persimmon, zucchini, and carrot. Frequently, the occurrence of cross-reactive IgE antibodies is not correlated with the development of clinical food allergy. In particular, the clinical relevance of sensitization to CCD is doubtful. Generally, pollen-related allergens tend to be more labile during heating procedures and in the digestive tract compared to allergens from classical allergenic foods such as peanut. However, recent DBPCFC studies have shown that both cooked celery and roasted hazelnuts still pose an allergenic risk for pollen-sensitized subjects. Since pathogenesis-related proteins share several common features with allergens and both the Bet v 1 and the Bet v 6-related food allergens are defense-related proteins, approaches to introduce such proteins as a measure to protect plants against diseases should be performed with caution as they may increase the allergenicity of these crops.
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                Author and article information

                Journal
                Allergy
                Allergy
                10.1111/(ISSN)1398-9995
                ALL
                Allergy
                John Wiley and Sons Inc. (Hoboken )
                0105-4538
                1398-9995
                06 August 2015
                October 2015
                : 70
                : 10 ( doiID: 10.1111/all.2015.70.issue-10 )
                : 1201-1211
                Affiliations
                [ 1 ] Department of Molecular BiologyUniversity of Salzburg SalzburgAustria
                Author notes
                [*] [* ] Correspondence

                Dr. Michael Wallner, Department of Molecular Biology, University of Salzburg, Hellbrunnerstr. 34, A‐5020 Salzburg, Austria.

                Tel.: +43‐662‐8044‐5975

                Fax: +43‐662‐8044‐183

                E‐mail: michael.wallner@ 123456sbg.ac.at

                Article
                ALL12696
                10.1111/all.12696
                5102629
                26186076
                648fad70-b575-4327-8cb0-c087d958c904
                © 2015 The Authors. Allergy Published by John Wiley & Sons Ltd.

                This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

                History
                : 12 July 2015
                Page count
                Pages: 11
                Funding
                Funded by: Austrian Science Fund
                Award ID: P 23417
                Award ID: W 1213
                Funded by: Priority Program ‘Allergy, Cancer, Bio‐Nano Research Center’ of the University of Salzburg
                Categories
                Review Article
                Review Articles
                Custom metadata
                2.0
                all12696
                October 2015
                Converter:WILEY_ML3GV2_TO_NLMPMC version:4.9.7 mode:remove_FC converted:09.11.2016

                Immunology
                allergen cross‐reactivity,allergen exposure,molecular allergology,tree pollen allergy,tree pollen sensitization

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