Identification and characterization of DC‐SIGN‐binding glycoproteins in allergenic foods

Background DC‐SIGN (dendritic cell‐specific intercellular adhesion molecule‐3‐grabbing nonintegrin) is a C‐type lectin receptor expressed on macrophages and dendritic cells. DC‐SIGN has high affinity for fucosylated glycans in several plant glycoproteins and pathogens. DC‐SIGN is thought to be cruci...

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Published in:Allergy (Copenhagen) 2016-08, Vol.71 (8), p.1145-1155
Main Authors: Kamalakannan, M., Chang, L. M., Grishina, G., Sampson, H. A., Masilamani, M.
Format: Article
Language:English
Subjects:
Allergens - immunology
Allergens - metabolism
Arachis hypogaea
Biomarkers
Carrier Proteins - immunology
Carrier Proteins - metabolism
Cell Adhesion Molecules - metabolism
Cicer arietinum
Cross Reactions - immunology
DC‐SIGN
Dendritic cells
Dendritic Cells - immunology
Dendritic Cells - metabolism
Enzyme-Linked Immunosorbent Assay
Flow Cytometry
Food - adverse effects
food allergens
Food allergies
Food Analysis
Food Hypersensitivity
Glycoproteins
Glycoproteins - immunology
Glycoproteins - metabolism
Humans
Immunoglobulin E - immunology
Lectins, C-Type - metabolism
Ligands
peanut
peanut agglutinin
Plant Proteins - immunology
Plant Proteins - metabolism
Protein Binding
Receptors, Cell Surface - metabolism
soybean
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Summary:Background DC‐SIGN (dendritic cell‐specific intercellular adhesion molecule‐3‐grabbing nonintegrin) is a C‐type lectin receptor expressed on macrophages and dendritic cells. DC‐SIGN has high affinity for fucosylated glycans in several plant glycoproteins and pathogens. DC‐SIGN is thought to be crucial for the development of allergic sensitization. However, the precise role of DC‐SIGN in food allergy pathogenesis is not yet understood. Objective We sought to characterize DC‐SIGN‐binding glycoproteins in a panel of allergenic and non‐allergenic foods. Methods Fluorescent‐labeled peanut and soy extracts were used to test protein binding to human monocyte‐derived dendritic cells (DCs) by flow cytometry. DC‐SIGN‐blocking assays were performed by incubating DCs with food extracts followed by staining with anti‐DC‐SIGN antibody. Using a DC‐SIGN‐Fc chimera, food extracts were tested for binding by ELISA and autoradiography. IgE immunoblotting was performed with pooled sera from food‐allergic subjects. DC activation and maturation were assessed by flow cytometry. Results and Conclusions We demonstrate that peanut agglutinin, a minor peanut allergen, is a novel ligand for DC‐SIGN. Peanut agglutinin activates DCs to induce the expression of costimulatory molecules in vitro. We present a comprehensive report on the characterization of DC‐SIGN‐binding proteins in common allergenic foods such as peanut, soy, tree nuts, egg, and milk. Foods that rarely induce allergy, such as pine nuts, chickpea, and corn, showed no binding to DC‐SIGN. Several DC‐SIGN‐binding proteins show reactivity in serum IgE immunoblots. We have also identified novel non‐IgE‐binding proteins that interact with DC‐SIGN; these proteins may be important for regulating immune responses to these foods.
ISSN:0105-4538
1398-9995
DOI:10.1111/all.12873