Abstract
Background
DC-SIGN (Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Non-integrin) 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 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 T cell polarization in a mixed lymphocyte reaction were assessed by flow cytometry.
Results & Conclusions
We demonstrate that peanut agglutinin, a minor peanut allergen is a novel ligand for DC-SIGN. Peanut agglutinin activates DCs to induce expression of co-stimulatory molecules in vitro. We present a comprehensive report on characterization of DC-SIGN-binding proteins in common allergenic foods like 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.
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