English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Zendy Plus

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Zendy Tools

Zendy Open

How the B‐cell antigen receptor ( BCR ) is activated upon interaction with its cognate antigen or with anti‐ BCR  antibodies is not fully understood. We have recently shown that B‐cell activation is accompanied by the opening of the pre‐organized  BCR  oligomers, an observation that strengthens the role of receptor reorganization in signalling. We have now analysed the  BCR  oligomer opening and signalling upon treatment with different monovalent stimuli. Our results indicate that monovalent antigens are able to disturb and open the  BCR  oligomer, but that this requires the presence and activity of the Src family kinase ( SFK ) Lyn. We have also shown that monovalent Fab fragments of anti‐ BCR  antibodies can open the  BCR  oligomers as long as they directly interact with the antigen‐binding site. We found that monovalent antigen binding opens both the IgM‐ BCR  and IgD‐ BCR , but calcium signalling is only seen in cells expressing IgM‐ BCR ; this provides a molecular basis for IgM‐ and IgD‐ BCR  functional segregation.

Molecular requirements of the B‐cell antigen receptor for sensing monovalent antigens