| First Author | Avalos AM | Year | 2014 |
| Journal | J Exp Med | Volume | 211 |
| Issue | 2 | Pages | 365-79 |
| PubMed ID | 24493799 | Mgi Jnum | J:208440 |
| Mgi Id | MGI:5563301 | Doi | 10.1084/jem.20131603 |
| Citation | Avalos AM, et al. (2014) Monovalent engagement of the BCR activates ovalbumin-specific transnuclear B cells. J Exp Med 211(2):365-79 |
| abstractText | 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. |
