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dc.contributor.authorVillar, Rina F.en_US
dc.contributor.authorPatel, Jinalen_US
dc.contributor.authorWeaver, Grant C.en_US
dc.contributor.authorKanekiyo, Masaruen_US
dc.contributor.authorWheatley, Adam K.en_US
dc.contributor.authorYassine, Hadi M.en_US
dc.contributor.authorCostello, Catherine E.en_US
dc.contributor.authorChandler, Kevin B.en_US
dc.contributor.authorMcTamney, Patrick. M.en_US
dc.contributor.authorNabel, Gary J.en_US
dc.contributor.authorMcDermott, Adrian B.en_US
dc.contributor.authorMascola, John R.en_US
dc.contributor.authorCarr, Steven A.en_US
dc.contributor.authorLingwood, Danielen_US
dc.date.accessioned2016-12-02T15:24:51Z
dc.date.issued2016en_US
dc.identifier.citationVillar, R. F., J. Patel, G. C. Weaver, M. Kanekiyo, A. K. Wheatley, H. M. Yassine, C. E. Costello, et al. 2016. “Reconstituted B cell receptor signaling reveals carbohydrate-dependent mode of activation.” Scientific Reports 6 (1): 36298. doi:10.1038/srep36298. http://dx.doi.org/10.1038/srep36298.en
dc.identifier.issn2045-2322en
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:29626094
dc.description.abstractActivation of immune cells (but not B cells) with lectins is widely known. We used the structurally defined interaction between influenza hemagglutinin (HA) and its cell surface receptor sialic acid (SA) to identify a B cell receptor (BCR) activation modality that proceeded through non-cognate interactions with antigen. Using a new approach to reconstitute antigen-receptor interactions in a human reporter B cell line, we found that sequence-defined BCRs from the human germline repertoire could be triggered by both complementarity to influenza HA and a separate mode of signaling that relied on multivalent ligation of BCR sialyl-oligosaccharide. The latter suggested a new mechanism for priming naïve B cell responses and manifested as the induction of SA-dependent pan-activation by peripheral blood B cells. BCR crosslinking in the absence of complementarity is a superantigen effect induced by some microbial products to subvert production of antigen-specific immune responses. B cell superantigen activity through affinity for BCR carbohydrate is discussed.en
dc.language.isoen_USen
dc.publisherNature Publishing Groupen
dc.relation.isversionofdoi:10.1038/srep36298en
dc.relation.hasversionhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC5087089/pdf/en
dash.licenseLAAen_US
dc.titleReconstituted B cell receptor signaling reveals carbohydrate-dependent mode of activationen
dc.typeJournal Articleen_US
dc.description.versionVersion of Recorden
dc.relation.journalScientific Reportsen
dash.depositing.authorLingwood, Danielen_US
dc.date.available2016-12-02T15:24:51Z
dc.identifier.doi10.1038/srep36298*
dash.authorsorderedfalse
dash.contributor.affiliatedLingwood, Daniel


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