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Comparative proteomics of common allergenic tree pollens of birch, alder, and hazel

BACKGROUND: In addition to known allergens, other proteins in pollen can aid the development of an immune response in allergic individuals. The contribution of the “unknown” protein allergens is apparent in phylogenetically related species where, despite of high homology of the lead allergens, the d...

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Autores principales: Darnhofer, Barbara, Tomin, Tamara, Liesinger, Laura, Schittmayer, Matthias, Tomazic, Peter Valentin, Birner‐Gruenberger, Ruth
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8248232/
https://www.ncbi.nlm.nih.gov/pubmed/33301602
http://dx.doi.org/10.1111/all.14694
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author Darnhofer, Barbara
Tomin, Tamara
Liesinger, Laura
Schittmayer, Matthias
Tomazic, Peter Valentin
Birner‐Gruenberger, Ruth
author_facet Darnhofer, Barbara
Tomin, Tamara
Liesinger, Laura
Schittmayer, Matthias
Tomazic, Peter Valentin
Birner‐Gruenberger, Ruth
author_sort Darnhofer, Barbara
collection PubMed
description BACKGROUND: In addition to known allergens, other proteins in pollen can aid the development of an immune response in allergic individuals. The contribution of the “unknown” protein allergens is apparent in phylogenetically related species where, despite of high homology of the lead allergens, the degree of allergenic potential can vary greatly. The aim of this study was to identify other potentially allergenic proteins in pollen of three common and highly related allergenic tree species: birch (Betula pendula), hazel (Corylus avellana) and alder (Alnus glutinosa). METHODS: For that purpose, we carried out a comprehensive, comparative proteomic screening of the pollen from the three species. In order to maximize protein recovery and coverage, different protein extraction and isolation strategies during sample preparation were employed. RESULTS: As a result, we report 2500–3000 identified proteins per each of the pollen species. Identified proteins were further used for a number of annotation steps, providing insight into differential distribution of peptidases, peptidase inhibitors and other potential allergenic proteins across the three species. Moreover, we carried out functional enrichment analyses that, interestingly, corroborated high species similarity in spite of their relatively distinct protein profiles. CONCLUSION: We provide to our knowledge first insight into proteomes of two very important allergenic pollen types, hazel and alder, where not even transcriptomics data are available, and compared them to birch. Datasets from this study can be readily used as protein databases and as such serve as basis for further functional studies.
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spelling pubmed-82482322021-07-06 Comparative proteomics of common allergenic tree pollens of birch, alder, and hazel Darnhofer, Barbara Tomin, Tamara Liesinger, Laura Schittmayer, Matthias Tomazic, Peter Valentin Birner‐Gruenberger, Ruth Allergy ORIGINAL ARTICLES BACKGROUND: In addition to known allergens, other proteins in pollen can aid the development of an immune response in allergic individuals. The contribution of the “unknown” protein allergens is apparent in phylogenetically related species where, despite of high homology of the lead allergens, the degree of allergenic potential can vary greatly. The aim of this study was to identify other potentially allergenic proteins in pollen of three common and highly related allergenic tree species: birch (Betula pendula), hazel (Corylus avellana) and alder (Alnus glutinosa). METHODS: For that purpose, we carried out a comprehensive, comparative proteomic screening of the pollen from the three species. In order to maximize protein recovery and coverage, different protein extraction and isolation strategies during sample preparation were employed. RESULTS: As a result, we report 2500–3000 identified proteins per each of the pollen species. Identified proteins were further used for a number of annotation steps, providing insight into differential distribution of peptidases, peptidase inhibitors and other potential allergenic proteins across the three species. Moreover, we carried out functional enrichment analyses that, interestingly, corroborated high species similarity in spite of their relatively distinct protein profiles. CONCLUSION: We provide to our knowledge first insight into proteomes of two very important allergenic pollen types, hazel and alder, where not even transcriptomics data are available, and compared them to birch. Datasets from this study can be readily used as protein databases and as such serve as basis for further functional studies. John Wiley and Sons Inc. 2021-01-15 2021-06 /pmc/articles/PMC8248232/ /pubmed/33301602 http://dx.doi.org/10.1111/all.14694 Text en © 2021 The Authors. Allergy published by European Academy of Allergy and Clinical Immunology and John Wiley & Sons Ltd https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle ORIGINAL ARTICLES
Darnhofer, Barbara
Tomin, Tamara
Liesinger, Laura
Schittmayer, Matthias
Tomazic, Peter Valentin
Birner‐Gruenberger, Ruth
Comparative proteomics of common allergenic tree pollens of birch, alder, and hazel
title Comparative proteomics of common allergenic tree pollens of birch, alder, and hazel
title_full Comparative proteomics of common allergenic tree pollens of birch, alder, and hazel
title_fullStr Comparative proteomics of common allergenic tree pollens of birch, alder, and hazel
title_full_unstemmed Comparative proteomics of common allergenic tree pollens of birch, alder, and hazel
title_short Comparative proteomics of common allergenic tree pollens of birch, alder, and hazel
title_sort comparative proteomics of common allergenic tree pollens of birch, alder, and hazel
topic ORIGINAL ARTICLES
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8248232/
https://www.ncbi.nlm.nih.gov/pubmed/33301602
http://dx.doi.org/10.1111/all.14694
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