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• W2037117519 endingPage "9872" @default.
• W2037117519 startingPage "9868" @default.
• W2037117519 abstract "Immunoglobulins recognize and clear microbial pathogens and toxins through the coupling of variable region specificity to Fc-triggered cellular activation. These proinflammatory activities are regulated, thus avoiding the pathogenic sequelae of uncontrolled inflammation by modulating the composition of the Fc-linked glycan. Upon sialylation, the affinities for Fcγ receptors are reduced, whereas those for alternative cellular receptors, such as dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN)/CD23, are increased. We demonstrate that sialylation induces significant structural alterations in the Cγ2 domain and propose a model that explains the observed changes in ligand specificity and biological activity. By analogy to related complexes formed by IgE and its evolutionarily related Fc receptors, we conclude that this mechanism is general for the modulation of antibody-triggered immune responses, characterized by a shift between an “open” activating conformation and a “closed” anti-inflammatory state of antibody Fc fragments. This common mechanism has been targeted by pathogens to avoid host defense and offers targets for therapeutic intervention in allergic and autoimmune disorders." @default.
• W2037117519 created "2016-06-24" @default.
• W2037117519 creator A5006610576 @default.
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• W2037117519 date "2013-05-22" @default.
• W2037117519 modified "2023-10-16" @default.
• W2037117519 title "General mechanism for modulating immunoglobulin effector function" @default.
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• W2037117519 doi "https://doi.org/10.1073/pnas.1307864110" @default.
• W2037117519 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3683708" @default.
• W2037117519 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23697368" @default.
• W2037117519 hasPublicationYear "2013" @default.
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