Multivalent virus-like epitope display amplifies BCR signaling independent of avidity

Author:

Publisher

Springer Science and Business Media LLC

Subject

Immunology,Immunology and Allergy

Reference5 articles.

1. Tolar, P. & Pierce, S. K. Unveiling the B cell receptor structure. Science 377, 819–820 (2022). A commentary placing new cryo-electron microscopy (cryo-EM) structures of the BCR in the context of competing models for how BCR triggering and B cell activation occurs.

2. Batista, F. D., Iber, D. & Neuberger, M. S. B cells acquire antigen from target cells after synapse formation. Nature 411, 489–494 (2001). This paper reports that membrane antigen is much more potent than soluble antigen, and induces formation of an immune synapse with responding B cells that excludes key inhibitory signaling molecules.

3. Wholey, W.-Y., Mueller, J. L., Tan, C., Brooks, J. F., Zikherman, J. & Cheng, W. Synthetic liposomal mimics of biological viruses for the study of immune responses to infection and vaccination. Bioconjug. Chem. 31, 685–697 (2020). This paper reports the design and validation of liposomes displaying HEL affinity mutants at a precise density to produce SVLS, the approach we used in our study.

4. Wholey, W.-Y., Meyer, A. R., Yoda, S.-T., Chackerian, B., Zikherman, J. & Cheng, W. Initiation of neutralizing antibody response probed using synthetic virus-like structures. Preprint at bioRxiv https://doi.org/10.1101/2023.02.20.529089 (2023). This preprint reports robust in vivo antibody responses to SVLS with varying epitope density, even without T cell help.

5. Getahun, A. Role of inhibitory signaling in peripheral B cell tolerance. Immunol. Rev. 307, 27–42 (2022). A review article describing how inhibitory phosphatases are engaged to suppress B cell responses to self-antigen.

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