{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T07:05:38Z","timestamp":1790751938610,"version":"4.1.0"},"reference-count":36,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2017,1,27]],"date-time":"2017-01-27T00:00:00Z","timestamp":1485475200000},"content-version":"vor","delay-in-days":26,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Scand J Immunol"],"published-print":{"date-parts":[[2017,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>IgM molecules circulate in serum as large polymers, mainly pentamers, which can be transported by the poly\u2010Ig receptor (<jats:styled-content style=\"fixed-case\">pIgR<\/jats:styled-content>) across epithelial cells to mucosal surfaces and released as secretory IgM (<jats:styled-content style=\"fixed-case\">SI<\/jats:styled-content>gM). The mucosal <jats:styled-content style=\"fixed-case\">SI<\/jats:styled-content>gM molecules have non\u2010covalently attached secretory component (<jats:styled-content style=\"fixed-case\">SC<\/jats:styled-content>), which is the extracellular part of <jats:styled-content style=\"fixed-case\">pIgR<\/jats:styled-content> which is cleaved from the epithelial cell membrane. Serum IgM antibodies do not contain <jats:styled-content style=\"fixed-case\">SC<\/jats:styled-content> and have previously been shown to make a conformational change from \u2018a star\u2019 to a \u2018staple\u2019 conformation upon reaction with antigens on a cell surface, enabling them to activate complement. However, it is not clear whether <jats:styled-content style=\"fixed-case\">SI<\/jats:styled-content>gM similarly can induce complement activation. To clarify this issue, we constructed recombinant chimeric (mouse\/human) IgM antibodies against hapten 5\u2010iodo\u20104\u2010hydroxy\u20103\u2010nitro\u2010phenacetyl (<jats:styled-content style=\"fixed-case\">NIP<\/jats:styled-content>) 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 <jats:styled-content style=\"fixed-case\">SC<\/jats:styled-content> in order to isolate joining\u2010chain (J\u2010chain) containing IgM, followed by addition of excess amounts of soluble <jats:styled-content style=\"fixed-case\">SC<\/jats:styled-content> to create <jats:styled-content style=\"fixed-case\">SI<\/jats:styled-content>gM (IgM J+ <jats:styled-content style=\"fixed-case\">SC<\/jats:styled-content>+). These <jats:styled-content style=\"fixed-case\">SI<\/jats:styled-content>gM preparations were tested for complement activation ability and shown to be nearly as active as the parental IgM J+ molecules. Thus, <jats:styled-content style=\"fixed-case\">SI<\/jats:styled-content>gM may offer protection against pathogens at mucosal surface by complement\u2010mediated cell lysis or by phagocytosis mediated by complement receptors present on effector cells on mucosa.<\/jats:p>","DOI":"10.1111\/sji.12508","type":"journal-article","created":{"date-parts":[[2016,11,16]],"date-time":"2016-11-16T20:02:34Z","timestamp":1479326554000},"page":"43-50","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["Human Secretory IgM Antibodies Activate Human Complement and Offer Protection at Mucosal Surface"],"prefix":"10.1111","volume":"85","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8877-8519","authenticated-orcid":false,"given":"T. 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