8W5P
Cryo-EM structure of Qb-Ab40
Summary for 8W5P
| Entry DOI | 10.2210/pdb8w5p/pdb |
| EMDB information | 37300 |
| Descriptor | Light chain of Ab40, Heavy chain of Ab40, Minor capsid protein A1 (3 entities in total) |
| Functional Keywords | qb, antibody, cryo-em, immune system |
| Biological source | Mus musculus More |
| Total number of polymer chains | 4 |
| Total formula weight | 54431.78 |
| Authors | |
| Primary citation | Li, R.,Bao, K.,Liu, C.,Ma, X.,Hua, Z.,Zhu, P.,Hou, B. Competition propels, rather than limits, the success of low-affinity B cells in the germinal center response. Cell Rep, 44:115334-115334, 2025 Cited by PubMed Abstract: The germinal center (GC) sets an environment where antigen-specific B cells are compelled to continuously increase their affinity to compete for the antigen and obtain Tfh help for survival and propagation. Previous studies indicated that low-affinity B cells are disadvantaged in the presence of high-affinity ones, suggesting that competition may lead to the elimination of low-affinity B cells and their descendants. However, using a multivalent virus-mimicking antigen, our study demonstrates that low-affinity B cells not only successfully participate in GC responses alongside high-affinity B cells but also undergo accelerated affinity maturation under the more stringent competition. Furthermore, our cryo-electron-microscopy-based structural analysis reveals that both low-affinity and high-affinity B cells compete for the same antigenic epitope. Although the applicability of this idealized GC competition to true pathogen-induced responses remains uncertain, this change in perspective on the role of competition in low-affinity B cell evolution provides valuable insights for vaccine development. PubMed: 39955776DOI: 10.1016/j.celrep.2025.115334 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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