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• W2034211044 startingPage "955" @default.
• W2034211044 abstract "Growing evidence suggests that allergenicity arises as an incidental, if pernicious, result of mistaken identity; that is, that proteins tend to generate allergic responses when they directly intrude on and activate innate immune pathways that evolved to signal the presence of infection. This gift (German: poison) of mimicry is clearest for the major house dust mite allergen Der p 2, which is a functional mimic of an essential TLR4 complex molecule. It appears likely, however, that similar intrinsic adjuvant activity provided by the hydrophobic cargo of lipid-binding allergens, carbohydrate structures on glycoprotein allergens, and allergen-associated protease activity has considerable generality as a molecular substrate of allergenicity. A better molecular understanding of the relevant ligands, receptors, and signaling pathways has clear translational promise for novel preventive and therapeutic approaches to allergic disease.What do we know?•The recent revolution in innate immunology has led to a highly productive reframing of fundamental questions in allergy research, driving a paradigm shift in our understanding of the molecular and cellular substrates of allergenicity.•The TH2-polarized T-cell immune responses that mark and underlie both adaptive responses to helminth infection and maladaptive allergic responses can be induced by several apparently unrelated pathways of innate immune activation.•The intrinsic adjuvant activity provided by direct engagement of these diverse pathways of innate immune activation appears central to allergenicity and allergic disease.What is still unknown?•The lipids associated with most lipid-binding allergens under conditions of natural exposure and the receptors and signaling pathways engaged by such protein/lipid complexes•The innate immune sensor for helminth- and allergen-associated soluble protease activity and the structural requirements (and receptors) for TH2-promoting carbohydrate structures on glycoprotein allergens•Which of these conserved pathways will be most tractable for targeting for translational development of novel preventive and therapeutic approaches to allergic disease" @default.
• W2034211044 created "2016-06-24" @default.
• W2034211044 creator A5071121564 @default.
• W2034211044 date "2010-05-01" @default.
• W2034211044 modified "2023-09-27" @default.
• W2034211044 title "Guilt by intimate association: What makes an allergen an allergen?" @default.
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• W2034211044 doi "https://doi.org/10.1016/j.jaci.2010.03.002" @default.
• W2034211044 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2868504" @default.
• W2034211044 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20381850" @default.
• W2034211044 hasPublicationYear "2010" @default.
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