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Identification of Proteases and Protease Inhibitors in Allergenic and Non-Allergenic Pollen

Pollen is one of the most common causes of allergy worldwide, making the study of their molecular composition crucial for the advancement of allergy research. Despite substantial efforts in this field, it is not yet clear why some plant pollens strongly provoke allergies while others do not. However...

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Autores principales: Höllbacher, Barbara, Schmitt, Armin O., Hofer, Heidi, Ferreira, Fatima, Lackner, Peter
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5486022/
https://www.ncbi.nlm.nih.gov/pubmed/28587253
http://dx.doi.org/10.3390/ijms18061199
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author Höllbacher, Barbara
Schmitt, Armin O.
Hofer, Heidi
Ferreira, Fatima
Lackner, Peter
author_facet Höllbacher, Barbara
Schmitt, Armin O.
Hofer, Heidi
Ferreira, Fatima
Lackner, Peter
author_sort Höllbacher, Barbara
collection PubMed
description Pollen is one of the most common causes of allergy worldwide, making the study of their molecular composition crucial for the advancement of allergy research. Despite substantial efforts in this field, it is not yet clear why some plant pollens strongly provoke allergies while others do not. However, proteases and protease inhibitors from allergen sources are known to play an important role in the development of pollen allergies. In this study, we aim to uncover differences in the transcriptional pattern of proteases and protease inhibitors in Betula verrucosa and Pinus sylvestris pollen as models for high and low allergenic potential, respectively. We applied RNA sequencing to Betula verrucosa and Pinus sylvestris pollen. After de-novo assembly we derived general functional profiles of the protein coding transcripts. By utilization of domain based functional annotation we identified potential proteases and protease inhibitors and compared their expression in the two types of pollen. Functional profiles are highly similar between Betula verrucosa and Pinus sylvestris pollen. Both pollen contain proteases and inhibitors from 53 and 7 Pfam families, respectively. Some of the members comprised within those families are implicated in facilitating allergen entry, while others are known allergens themselves. Our work revealed several candidate proteins which, with further investigation, represent exciting new leads in elucidating the process behind allergic sensitization.
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spelling pubmed-54860222017-06-29 Identification of Proteases and Protease Inhibitors in Allergenic and Non-Allergenic Pollen Höllbacher, Barbara Schmitt, Armin O. Hofer, Heidi Ferreira, Fatima Lackner, Peter Int J Mol Sci Article Pollen is one of the most common causes of allergy worldwide, making the study of their molecular composition crucial for the advancement of allergy research. Despite substantial efforts in this field, it is not yet clear why some plant pollens strongly provoke allergies while others do not. However, proteases and protease inhibitors from allergen sources are known to play an important role in the development of pollen allergies. In this study, we aim to uncover differences in the transcriptional pattern of proteases and protease inhibitors in Betula verrucosa and Pinus sylvestris pollen as models for high and low allergenic potential, respectively. We applied RNA sequencing to Betula verrucosa and Pinus sylvestris pollen. After de-novo assembly we derived general functional profiles of the protein coding transcripts. By utilization of domain based functional annotation we identified potential proteases and protease inhibitors and compared their expression in the two types of pollen. Functional profiles are highly similar between Betula verrucosa and Pinus sylvestris pollen. Both pollen contain proteases and inhibitors from 53 and 7 Pfam families, respectively. Some of the members comprised within those families are implicated in facilitating allergen entry, while others are known allergens themselves. Our work revealed several candidate proteins which, with further investigation, represent exciting new leads in elucidating the process behind allergic sensitization. MDPI 2017-06-05 /pmc/articles/PMC5486022/ /pubmed/28587253 http://dx.doi.org/10.3390/ijms18061199 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Höllbacher, Barbara
Schmitt, Armin O.
Hofer, Heidi
Ferreira, Fatima
Lackner, Peter
Identification of Proteases and Protease Inhibitors in Allergenic and Non-Allergenic Pollen
title Identification of Proteases and Protease Inhibitors in Allergenic and Non-Allergenic Pollen
title_full Identification of Proteases and Protease Inhibitors in Allergenic and Non-Allergenic Pollen
title_fullStr Identification of Proteases and Protease Inhibitors in Allergenic and Non-Allergenic Pollen
title_full_unstemmed Identification of Proteases and Protease Inhibitors in Allergenic and Non-Allergenic Pollen
title_short Identification of Proteases and Protease Inhibitors in Allergenic and Non-Allergenic Pollen
title_sort identification of proteases and protease inhibitors in allergenic and non-allergenic pollen
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5486022/
https://www.ncbi.nlm.nih.gov/pubmed/28587253
http://dx.doi.org/10.3390/ijms18061199
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