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

MPS-Authors

Volkmann,  Christoph
BIOSS Centre for Biological Signalling Studies, Department of Molecular Immunology, Biology III, Faculty of Biology, University of Freiburg;
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Brings,  Naema
BIOSS Centre for Biological Signalling Studies, Department of Molecular Immunology, Biology III, Faculty of Biology, University of Freiburg;
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Becker,  Martin
BIOSS Centre for Biological Signalling Studies, Department of Molecular Immunology, Biology III, Faculty of Biology, University of Freiburg;
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Hobeika,  Elias
BIOSS Centre for Biological Signalling Studies, Department of Molecular Immunology, Biology III, Faculty of Biology, University of Freiburg;
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;
Institute of Immunology, University Hospital Ulm;

Yang,  Jianying
BIOSS Centre for Biological Signalling Studies, Department of Molecular Immunology, Biology III, Faculty of Biology, University of Freiburg;
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;
Freiburg Institute for Advanced Studies (FRIAS), University of Freiburg;
University of Strasbourg Institute for Advanced Study (USIAS) University of Strasbourg;

Reth,  Michael
BIOSS Centre for Biological Signalling Studies, Department of Molecular Immunology, Biology III, Faculty of Biology, University of Freiburg;
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002C-C331-8
Abstract
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.