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 Daniel, Meyer-Wentrup, Friederike, Theile, Christopher S., Chakraborty, Arup K., Zhuang, Xiaowei, Ploegh, Hidde |
| المساهمون: | Massachusetts Institute of Technology. Institute for Medical Engineering & Science, Massachusetts Institute of Technology. Department of Biological Engineering, Massachusetts Institute of Technology. Department of Chemical Engineering, Massachusetts Institute of Technology. Department of Chemistry, Massachusetts Institute of Technology. Department of Physics, Ragon Institute of MGH, MIT and Harvard, Whitehead Institute for Biomedical Research, Frushicheva, Maria P., Thill, Peter Daniel, Chakraborty, Arup K., Ploegh, Hidde |
| المصدر: | Rockefeller University Press |
| بيانات النشر: | Rockefeller University Press |
| سنة النشر: | 2013 |
| المجموعة: | DSpace@MIT (Massachusetts Institute of Technology) |
| 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. ; National Institutes of Health (U.S.) (grant R01 AI087879) ; National Institutes of Health (U.S.) (grant R01 GM100518) ; National Institutes of Health (U.S.) (grant P01 AI091580) ; Netherlands Organization for Scientific Research |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | application/pdf |
| اللغة: | English |
| تدمد: | 0022-1007 1540-9538 |
| العلاقة: | http://dx.doi.org/10.1084/jem.20131603Test; Journal of Experimental Medicine; http://hdl.handle.net/1721.1/90353Test; Avalos, A. M., A. M. Bilate, M. D. Witte, A. K. Tai, J. He, M. P. Frushicheva, P. D. Thill, et al. “Monovalent Engagement of the BCR Activates Ovalbumin-Specific Transnuclear B Cells.” Journal of Experimental Medicine 211, no. 2 (February 3, 2014): 365–379.; orcid:0000-0001-6259-8800; orcid:0000-0002-7487-8858; orcid:0000-0003-1268-9602; orcid:0000-0002-1090-6071 |
| الإتاحة: | https://doi.org/10.1084/jem.20131603Test http://hdl.handle.net/1721.1/90353Test |
| حقوق: | Creative Commons Attribution-Noncommercial-Share Alike ; http://creativecommons.org/licenses/by-nc-sa/3.0Test/ |
| رقم الانضمام: | edsbas.34D82AB7 |
| قاعدة البيانات: | BASE |
Full Text Finder | تدمد: | 00221007 15409538 |
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