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

Volkmann, C., Brings, N., Becker, M., Hobeika, E., Yang, J., & Reth, M. (2016). Molecular requirements of the B-cell antigen receptor for sensing monovalent antigens. The EMBO Journal, 35, 2371-2381. doi:10.15252/embj.201694177.

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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-002C-C331-8 Versions-Permalink: https://hdl.handle.net/21.11116/0000-0008-9B3D-6
Genre: Zeitschriftenartikel

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https://www.embopress.org/doi/full/10.15252/embj.201694177 (Verlagsversion)
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 Urheber:
Volkmann, Christoph1, 2, Autor
Brings, Naema1, 2, Autor
Becker, Martin1, 2, Autor
Hobeika, Elias1, 2, 3, Autor
Yang, Jianying1, 2, 4, 5, Autor
Reth, Michael1, 2, Autor
Affiliations:
1BIOSS Centre for Biological Signalling Studies, Department of Molecular Immunology, Biology III, Faculty of Biology, University of Freiburg, Freiburg, Germany, ou_persistent22              
2Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society, 79108 Freiburg, DE, ou_2243640              
3Institute of Immunology, University Hospital Ulm, Ulm, Germany, ou_persistent22              
4Freiburg Institute for Advanced Studies (FRIAS), University of Freiburg, Freiburg, Germany, ou_persistent22              
5University of Strasbourg Institute for Advanced Study (USIAS) University of Strasbourg, Strasbourg, France, ou_persistent22              

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Schlagwörter: B-cell antigen receptor, dissociaton activation, monomeric antigen
 Zusammenfassung: 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.

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Sprache(n): eng - English
 Datum: 2016-09-15
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.15252/embj.201694177
 Art des Abschluß: -

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Titel: The EMBO Journal
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Nature Publishing Group
Seiten: - Band / Heft: 35 Artikelnummer: - Start- / Endseite: 2371 - 2381 Identifikator: ISSN: 0261-4189
CoNE: https://pure.mpg.de/cone/journals/resource/954925497061_1