Differences in self-recognition between secreted antibody and membrane-bound B cell antigen receptor
The random gene segment rearrangement during B cell development ensures Ab repertoire diversity. Because this process might generate autoreactive specificities, it has been proposed that stringent selection mechanisms prevent the development of autoreactive B cells. However, conventional assays to i...
Guardado en:
| Autores principales: | , |
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| Formato: | Article (Journal) |
| Lenguaje: | inglés |
| Publicado: |
25 January 2019
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| In: |
The journal of immunology
Year: 2019, Volumen: 202, Número: 5, Pages: 1417-1427 |
| ISSN: | 1550-6606 |
| DOI: | 10.4049/jimmunol.1800690 |
| Acceso en línea: | Verlag, Volltext: https://doi.org/10.4049/jimmunol.1800690 Verlag, Volltext: https://www.jimmunol.org/content/202/5/1417 
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| Notas de Autor: | Joseena Iype, Moumita Datta, Ahmad Khadour, Rudolf Übelhart, Antonella Nicolò, Tim Rollenske, Marcus Dühren-von Minden, Hedda Wardemann, Palash C. Maity and Hassan Jumaa |
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| 520 | |a The random gene segment rearrangement during B cell development ensures Ab repertoire diversity. Because this process might generate autoreactive specificities, it has been proposed that stringent selection mechanisms prevent the development of autoreactive B cells. However, conventional assays to identify autoreactive B cells usually employ in vitro-generated Abs, which differ from membrane-bound BCRs. In this study, we used a cell-based assay to investigate the autoreactivity of membrane-bound BCRs derived from different B cell developmental stages of human peripheral blood. Contrasted to soluble Ab counterparts, only a few of the tested BCRs were autoreactive, although the cell-based assay sensitively detects feeble Ag recognition of a germline-reverted murine BCR that was selected after OVA immunization of mice, whereas conventional assays failed to do so. Together, these data suggest that proper identification of autoreactive B cells requires the membrane-bound BCR, as the soluble Ab may largely differ from its BCR counterpart in Ag binding. | ||
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