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 (HDM) allergens triggers typical allergic diseases such as allergic rhinitis and asthma. Amongst the 23 mite allergen groups hitherto identified, groups 1 are cysteine proteases belonging to the papain-like family whereas gro...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2014-03-01
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| Series: | Frontiers in Immunology |
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| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fimmu.2014.00138/full |
| _version_ | 1819037438120558592 |
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| author | Marie-Eve eDumez Marie-Eve eDumez Julie eHerman Vincenzo eCampisi Vincenzo eCampisi Moreno eGalleni Alain eJacquet Andy eChevigné |
| author_facet | Marie-Eve eDumez Marie-Eve eDumez Julie eHerman Vincenzo eCampisi Vincenzo eCampisi Moreno eGalleni Alain eJacquet Andy eChevigné |
| author_sort | Marie-Eve eDumez |
| collection | DOAJ |
| description | In more than 20% of the world population, sensitization to house dust mite (HDM) allergens triggers typical allergic diseases such as allergic rhinitis and asthma. Amongst the 23 mite allergen groups hitherto identified, groups 1 are 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 intermolecular 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. |
| first_indexed | 2024-12-21T08:21:25Z |
| format | Article |
| id | doaj.art-4b5e6d620efd4b739fe0795643fc8c26 |
| institution | Directory Open Access Journal |
| issn | 1664-3224 |
| language | English |
| last_indexed | 2024-12-21T08:21:25Z |
| publishDate | 2014-03-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Immunology |
| spelling | doaj.art-4b5e6d620efd4b739fe0795643fc8c262022-12-21T19:10:25ZengFrontiers Media S.A.Frontiers in Immunology1664-32242014-03-01510.3389/fimmu.2014.0013878240Orchestration of an uncommon maturation cascade of the house dust mite protease allergen quartetMarie-Eve eDumez0Marie-Eve eDumez1Julie eHerman2Vincenzo eCampisi3Vincenzo eCampisi4Moreno eGalleni5Alain eJacquet6Andy eChevigné7CRP-SantéUniversity of LiègeUniversity of LiègeCRP-SantéUniversity of LiègeUniversity of LiègeUniversity of BangkokCRP-SantéIn more than 20% of the world population, sensitization to house dust mite (HDM) allergens triggers typical allergic diseases such as allergic rhinitis and asthma. Amongst the 23 mite allergen groups hitherto identified, groups 1 are 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 intermolecular 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.http://journal.frontiersin.org/Journal/10.3389/fimmu.2014.00138/fulllocalizationInteractionProteasesDer p 1miteallergen |
| spellingShingle | Marie-Eve eDumez Marie-Eve eDumez Julie eHerman Vincenzo eCampisi Vincenzo eCampisi Moreno eGalleni Alain eJacquet Andy eChevigné Orchestration of an uncommon maturation cascade of the house dust mite protease allergen quartet Frontiers in Immunology localization Interaction Proteases Der p 1 mite allergen |
| 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 | localization Interaction Proteases Der p 1 mite allergen |
| url | http://journal.frontiersin.org/Journal/10.3389/fimmu.2014.00138/full |
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