دورية أكاديمية
Monovalent engagement of the BCR activates ovalbumin-specific transnuclear B cells
| العنوان: | Monovalent engagement of the BCR activates ovalbumin-specific transnuclear B cells |
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| المؤلفون: | Avalos, Ana M., Bilate, Angelina M., Witte, Martin D., Tai, Albert K., He, Jiang, Frushicheva, Maria P., Thill, Peter D., Meyer-Wentrup, Friederike, Theile, Christopher S., Chakraborty, Arup K., Zhuang, Xiaowei, Ploegh, Hidde L. |
| المصدر: | Avalos , A M , Bilate , A M , Witte , M D , Tai , A K , He , J , Frushicheva , M P , Thill , P D , Meyer-Wentrup , F , Theile , C S , Chakraborty , A K , Zhuang , X & Ploegh , H L 2014 , ' Monovalent engagement of the BCR activates ovalbumin-specific transnuclear B cells ' , Journal of Experimental Medicine , vol. 211 , no. 2 , pp. 365-379 . https://doi.org/10.1084/jem.20131603Test |
| سنة النشر: | 2014 |
| المجموعة: | University of Groningen research database |
| مصطلحات موضوعية: | OPTICAL RECONSTRUCTION MICROSCOPY, ANTIGEN RECEPTOR, T-CELLS, EXPRESSION, AFFINITY, ANTIBODY, MICE, LYMPHOCYTES, INFECTION, RESPONSES |
| الوصف: | Valency requirements for B cell activation upon antigen encounter are poorly understood. OB1 transnuclear B cells express an IgG1 B cell receptor (BCR) specific for ovalbumin (OVA), the epitope of which can be mimicked using short synthetic peptides to allow antigen-specific engagement of the BCR. By altering length and valency of epitope-bearing synthetic peptides, we examined the properties of ligands required for optimal OB1 B cell activation. Monovalent engagement of the BCR with an epitope-bearing 17-mer synthetic peptide readily activated OB1 B cells. Dimers of the minimal peptide epitope oriented in an N to N configuration were more stimulatory than their C to C counterparts. Although shorter length correlated with less activation, a monomeric 8-mer peptide epitope behaved as a weak agonist that blocked responses to cell-bound peptide antigen, a blockade which could not be reversed by CD40 ligation. The 8-mer not only delivered a suboptimal signal, which blocked subsequent responses to OVA, anti-IgG, and anti-kappa, but also competed for binding with OVA. Our results show that fine-tuning of BCR-ligand recognition can lead to B cell nonresponsiveness, activation, or inhibition. |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | application/pdf |
| اللغة: | English |
| العلاقة: | https://research.rug.nl/en/publications/83b98406-651c-41da-933a-bffd7ad7cffcTest |
| DOI: | 10.1084/jem.20131603 |
| الإتاحة: | https://doi.org/10.1084/jem.20131603Test https://hdl.handle.net/11370/83b98406-651c-41da-933a-bffd7ad7cffcTest https://research.rug.nl/en/publications/83b98406-651c-41da-933a-bffd7ad7cffcTest https://pure.rug.nl/ws/files/66299588/365.full.pdfTest |
| حقوق: | info:eu-repo/semantics/openAccess |
| رقم الانضمام: | edsbas.D348365 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1084/jem.20131603 |
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