Reconstituted B cell receptor signaling reveals carbohydrate-dependent mode of activation
AuthorVillar, RF; Patel, J; Weaver, GC; Kanekiyo, M; Wheatley, AK; Yassine, HM; Costello, CE; Chandler, KB; McTamney, PM; Nabel, GJ; ...
Source TitleScientific Reports
PublisherNATURE PUBLISHING GROUP
University of Melbourne Author/sWheatley, Adam
AffiliationMicrobiology and Immunology
Document TypeJournal Article
CitationsVillar, R. F., Patel, J., Weaver, G. C., Kanekiyo, M., Wheatley, A. K., Yassine, H. M., Costello, C. E., Chandler, K. B., McTamney, P. M., Nabel, G. J., McDermott, A. B., Mascola, J. R., Carr, S. A. & Lingwood, D. (2016). Reconstituted B cell receptor signaling reveals carbohydrate-dependent mode of activation. SCIENTIFIC REPORTS, 6 (1), https://doi.org/10.1038/srep36298.
Access StatusOpen Access
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.
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