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Orchestration of an Uncommon Maturation Cascade of the House Dust Mite Protease Allergen Quartet
In more than 20% of the world population, sensitization to house dust mite allergens triggers typical allergic diseases such as allergic rhinitis and asthma. Amongst the 23 mite allergen groups hitherto identified, group 1 is cysteine proteases belonging to the papain-like family whereas groups 3, 6...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3978338/ https://www.ncbi.nlm.nih.gov/pubmed/24744761 http://dx.doi.org/10.3389/fimmu.2014.00138 |
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author | Dumez, Marie-Eve Herman, Julie Campizi, Vincenzo Galleni, Moreno Jacquet, Alain Chevigné, Andy |
author_facet | Dumez, Marie-Eve Herman, Julie Campizi, Vincenzo Galleni, Moreno Jacquet, Alain Chevigné, Andy |
author_sort | Dumez, Marie-Eve |
collection | PubMed |
description | In more than 20% of the world population, sensitization to house dust mite allergens triggers typical allergic diseases such as allergic rhinitis and asthma. Amongst the 23 mite allergen groups hitherto identified, group 1 is cysteine proteases belonging to the papain-like family whereas groups 3, 6, and 9 are serine proteases displaying trypsin, chymotrypsin, and collagenolytic activities, respectively. While these proteases are more likely to be involved in the mite digestive system, they also play critical roles in the initiation and in the chronicity of the allergic response notably through the activation of innate immune pathways. All these allergenic proteases are expressed in mite as inactive precursor form. Until recently, the exact mechanisms of their maturation into active proteases remained to be fully elucidated. Recent breakthroughs in the understanding of the activation mechanisms of mite allergenic protease precursors have highlighted an uncommon and unique maturation pathway orchestrated by group 1 proteases that tightly regulates the proteolytic activities of groups 1, 3, 6, and 9 through complex intra- or inter-molecular mechanisms. This review presents and discusses the currently available knowledge of the activation mechanisms of group 1, 3, 6, and 9 allergens of Dermatophagoides pteronyssinus laying special emphasis on their localization, regulation, and interconnection. |
format | Online Article Text |
id | pubmed-3978338 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-39783382014-04-17 Orchestration of an Uncommon Maturation Cascade of the House Dust Mite Protease Allergen Quartet Dumez, Marie-Eve Herman, Julie Campizi, Vincenzo Galleni, Moreno Jacquet, Alain Chevigné, Andy Front Immunol Immunology In more than 20% of the world population, sensitization to house dust mite allergens triggers typical allergic diseases such as allergic rhinitis and asthma. Amongst the 23 mite allergen groups hitherto identified, group 1 is cysteine proteases belonging to the papain-like family whereas groups 3, 6, and 9 are serine proteases displaying trypsin, chymotrypsin, and collagenolytic activities, respectively. While these proteases are more likely to be involved in the mite digestive system, they also play critical roles in the initiation and in the chronicity of the allergic response notably through the activation of innate immune pathways. All these allergenic proteases are expressed in mite as inactive precursor form. Until recently, the exact mechanisms of their maturation into active proteases remained to be fully elucidated. Recent breakthroughs in the understanding of the activation mechanisms of mite allergenic protease precursors have highlighted an uncommon and unique maturation pathway orchestrated by group 1 proteases that tightly regulates the proteolytic activities of groups 1, 3, 6, and 9 through complex intra- or inter-molecular mechanisms. This review presents and discusses the currently available knowledge of the activation mechanisms of group 1, 3, 6, and 9 allergens of Dermatophagoides pteronyssinus laying special emphasis on their localization, regulation, and interconnection. Frontiers Media S.A. 2014-03-31 /pmc/articles/PMC3978338/ /pubmed/24744761 http://dx.doi.org/10.3389/fimmu.2014.00138 Text en Copyright © 2014 Dumez, Herman, Campizi, Galleni, Jacquet and Chevigné. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Immunology Dumez, Marie-Eve Herman, Julie Campizi, Vincenzo Galleni, Moreno Jacquet, Alain Chevigné, Andy Orchestration of an Uncommon Maturation Cascade of the House Dust Mite Protease Allergen Quartet |
title | Orchestration of an Uncommon Maturation Cascade of the House Dust Mite Protease Allergen Quartet |
title_full | Orchestration of an Uncommon Maturation Cascade of the House Dust Mite Protease Allergen Quartet |
title_fullStr | Orchestration of an Uncommon Maturation Cascade of the House Dust Mite Protease Allergen Quartet |
title_full_unstemmed | Orchestration of an Uncommon Maturation Cascade of the House Dust Mite Protease Allergen Quartet |
title_short | Orchestration of an Uncommon Maturation Cascade of the House Dust Mite Protease Allergen Quartet |
title_sort | orchestration of an uncommon maturation cascade of the house dust mite protease allergen quartet |
topic | Immunology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3978338/ https://www.ncbi.nlm.nih.gov/pubmed/24744761 http://dx.doi.org/10.3389/fimmu.2014.00138 |
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