Proteolytic, lipidergic and polysaccharide molecular recognition shape innate responses to house dust mite allergens.
Toll-like receptors
house dust mite
lipid-binding protein
polysaccharide
protease allergen
Journal
Allergy
ISSN: 1398-9995
Titre abrégé: Allergy
Pays: Denmark
ID NLM: 7804028
Informations de publication
Date de publication:
01 2020
01 2020
Historique:
received:
14
12
2018
revised:
05
04
2019
accepted:
23
05
2019
pubmed:
6
6
2019
medline:
12
1
2021
entrez:
6
6
2019
Statut:
ppublish
Résumé
House dust mites (HDMs) are sources of an extensive repertoire of allergens responsible for a range of allergic conditions. Technological advances have accelerated the identification of these allergens and characterized their putative roles within HDMs. Understanding their functional bioactivities is illuminating how they interact with the immune system to cause disease and how interrelations between them are essential to maximize allergic responses. Two types of allergen bioactivity, namely proteolysis and peptidolipid/lipid binding, elicit IgE and stimulate bystander responses to unrelated allergens. Much of this influence arises from Toll-like receptor (TLR) 4 or TLR2 signalling and, in the case of protease allergens, the activation of additional pleiotropic effectors with strong disease linkage. Of related interest is the interaction of HDM allergens with common components of the house dust matrix, through either their binding to allergens or their autonomous modulation of immune receptors. Herein, we provide a contemporary view of how proteolysis, lipid-binding activity and interactions with polysaccharides and polysaccharide molecular recognition systems coordinate the principal responses which underlie allergy. The power of the catalytically competent group 1 HDM protease allergen component is demonstrated by a review of disclosures surrounding the efficacy of novel inhibitors produced by structure-based design.
Substances chimiques
Antigens, Dermatophagoides
0
Lipids
0
Pathogen-Associated Molecular Pattern Molecules
0
Polysaccharides
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
33-53Subventions
Organisme : Chulalongkorn University
ID : GRB-BSS_83_59_30_24
Pays : International
Organisme : Center of Excellence on Medical Biotechnology (CEMB), S&T Postgraduate Education and Research Development Office (PERDO)
ID : SB-60-003-03
Pays : International
Organisme : Wellcome Trust
ID : 083625
Pays : United Kingdom
Organisme : Chulalongkorn Academic Advancement (2nd Century Project-CUAASC)
Pays : International
Organisme : Thailand Research Fund
ID : TRG5680005
Pays : International
Organisme : National Research University Project, Office of Higher Education Commission
ID : NRU59-003-HR
Pays : International
Informations de copyright
© 2019 EAACI and John Wiley and Sons A/S. Published by John Wiley and Sons Ltd.
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