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http://purl.uniprot.org/citations/25824821http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25824821http://www.w3.org/2000/01/rdf-schema#comment"Immunoglobulin ε (IgE) antibodies are the primary mediators of allergic diseases, which affect more than 1 in 10 individuals worldwide. IgE specific for innocuous environmental antigens, or allergens, binds and sensitizes tissue-resident mast cells expressing the high-affinity IgE receptor, FcεRI. Subsequent allergen exposure cross-links mast cell-bound IgE, resulting in the release of inflammatory mediators and initiation of the allergic cascade. It is well established that precise glycosylation patterns exert profound effects on the biological activity of IgG. However, the contribution of glycosylation to IgE biology is less clear. Here, we demonstrate an absolute requirement for IgE glycosylation in allergic reactions. The obligatory glycan was mapped to a single N-linked oligomannose structure in the constant domain 3 (Cε3) of IgE, at asparagine-394 (N394) in human IgE and N384 in mouse. Genetic disruption of the site or enzymatic removal of the oligomannose glycan altered IgE secondary structure and abrogated IgE binding to FcεRI, rendering IgE incapable of eliciting mast cell degranulation, thereby preventing anaphylaxis. These results underscore an unappreciated and essential requirement of glycosylation in IgE biology."xsd:string
http://purl.uniprot.org/citations/25824821http://purl.org/dc/terms/identifier"doi:10.1084/jem.20142182"xsd:string
http://purl.uniprot.org/citations/25824821http://purl.uniprot.org/core/author"Fiebiger E."xsd:string
http://purl.uniprot.org/citations/25824821http://purl.uniprot.org/core/author"Anthony R.M."xsd:string
http://purl.uniprot.org/citations/25824821http://purl.uniprot.org/core/author"Mempel T.R."xsd:string
http://purl.uniprot.org/citations/25824821http://purl.uniprot.org/core/author"Platzer B."xsd:string
http://purl.uniprot.org/citations/25824821http://purl.uniprot.org/core/author"Mani V."xsd:string
http://purl.uniprot.org/citations/25824821http://purl.uniprot.org/core/author"Conroy M."xsd:string
http://purl.uniprot.org/citations/25824821http://purl.uniprot.org/core/author"Bartsch Y.C."xsd:string
http://purl.uniprot.org/citations/25824821http://purl.uniprot.org/core/author"Bosques C."xsd:string
http://purl.uniprot.org/citations/25824821http://purl.uniprot.org/core/author"Pagan J.D."xsd:string
http://purl.uniprot.org/citations/25824821http://purl.uniprot.org/core/author"Shade K.T."xsd:string
http://purl.uniprot.org/citations/25824821http://purl.uniprot.org/core/author"Washburn N."xsd:string
http://purl.uniprot.org/citations/25824821http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25824821http://purl.uniprot.org/core/name"J Exp Med"xsd:string
http://purl.uniprot.org/citations/25824821http://purl.uniprot.org/core/pages"457-467"xsd:string
http://purl.uniprot.org/citations/25824821http://purl.uniprot.org/core/title"A single glycan on IgE is indispensable for initiation of anaphylaxis."xsd:string
http://purl.uniprot.org/citations/25824821http://purl.uniprot.org/core/volume"212"xsd:string
http://purl.uniprot.org/citations/25824821http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/25824821
http://purl.uniprot.org/citations/25824821http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/25824821
http://purl.uniprot.org/uniprot/#_A0A0A6YXC5-mappedCitation-25824821http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25824821
http://purl.uniprot.org/uniprot/#_P20489-mappedCitation-25824821http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25824821
http://purl.uniprot.org/uniprot/A0A0A6YXC5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/25824821
http://purl.uniprot.org/uniprot/P20489http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/25824821