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Sci Rep DOI:10.1038/srep36298

Reconstituted B cell receptor signaling reveals carbohydrate-dependent mode of activation.

Publication TypeJournal Article
Year of Publication2016
AuthorsVillar, RF, Patel, J, Weaver, GC, Kanekiyo, M, Wheatley, AK, Yassine, HM, Costello, CE, Chandler, KB, McTamney, PM, Nabel, GJ, McDermott, AB, Mascola, JR, Carr, SA, Lingwood, D
JournalSci Rep
Volume6
Pages36298
Date Published2016 Oct 31
ISSN2045-2322
Abstract

Activation 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.

DOI10.1038/srep36298
Pubmed

http://www.ncbi.nlm.nih.gov/pubmed/27796362?dopt=Abstract

Alternate JournalSci Rep
PubMed ID27796362
PubMed Central IDPMC5087089
Grant ListP30 AI060354 / AI / NIAID NIH HHS / United States
S10 OD010724 / OD / NIH HHS / United States