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• W2556856248 abstract "Abstract IgM molecules circulate in serum as large polymers, mainly pentamers, which can be transported by the poly‐Ig receptor ( pIgR ) across epithelial cells to mucosal surfaces and released as secretory IgM ( SI gM). The mucosal SI gM molecules have non‐covalently attached secretory component ( SC ), which is the extracellular part of pIgR which is cleaved from the epithelial cell membrane. Serum IgM antibodies do not contain SC and have previously been shown to make a conformational change from ‘a star’ to a ‘staple’ conformation upon reaction with antigens on a cell surface, enabling them to activate complement. However, it is not clear whether SI gM similarly can induce complement activation. To clarify this issue, we constructed recombinant chimeric (mouse/human) IgM antibodies against hapten 5‐iodo‐4‐hydroxy‐3‐nitro‐phenacetyl ( NIP ) and in addition studied polyclonal IgM formed after immunization with a meningococcal group B vaccine. The monoclonal and polyclonal IgM molecules were purified by affinity chromatography on a column containing human SC in order to isolate joining‐chain (J‐chain) containing IgM, followed by addition of excess amounts of soluble SC to create SI gM (IgM J+ SC +). These SI gM preparations were tested for complement activation ability and shown to be nearly as active as the parental IgM J+ molecules. Thus, SI gM may offer protection against pathogens at mucosal surface by complement‐mediated cell lysis or by phagocytosis mediated by complement receptors present on effector cells on mucosa." @default.
• W2556856248 created "2016-11-30" @default.
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• W2556856248 date "2017-01-01" @default.
• W2556856248 modified "2023-10-03" @default.
• W2556856248 title "Human Secretory IgM Antibodies Activate Human Complement and Offer Protection at Mucosal Surface" @default.
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• W2556856248 doi "https://doi.org/10.1111/sji.12508" @default.
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