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Functional monovalency amplifies the pathogenicity of anti-MuSK IgG4 in myasthenia gravis
Human IgG4 usually displays anti-inflammatory activity, and observations of IgG4 autoantibodies causing severe autoimmune disorders are therefore poorly understood. In blood, IgG4 antibodies naturally engage in a stochastic process termed Fab-arm exchange in which unrelated IgG4s exchange half-molecules continuously. The resulting IgG4 antibodies are composed of two different binding sites, thereby acquiring monovalent binding and inability to cross-link for each antigen recognized. Here, wedoi:10.1101/2020.09.24.296293 fatcat:pqnbigtptnfmvpq3zct2wvq23y