9WMQ
The cryo-electron microscopy complex structure of PCV3 VLPs and antibody 2B5
Summary for 9WMQ
| Entry DOI | 10.2210/pdb9wmq/pdb |
| EMDB information | 66101 |
| Descriptor | Cap, heavy chain of antibody 2B5, light chain of antibody 2B5 (3 entities in total) |
| Functional Keywords | porcine circovirus 3, cryo-em, pcv3 vlp, immunocomplexes, virus like particle/immune system, virus like particle-immune system complex |
| Biological source | Porcine circovirus 3 More |
| Total number of polymer chains | 3 |
| Total formula weight | 45942.34 |
| Authors | |
| Primary citation | Su, J.,Tong, X.,Jiang, Y.,Li, Y.,Yan, H.,Liu, Y.,Wang, Y.,Su, X.,Sun, Z.,Wang, M.,Xia, N.,Bostina, M.,Li, S.,Pang, W.,Zheng, Q.,Tian, K. Structural basis and immunogenic efficacy of porcine circovirus type 3 virus-like particle. Nat Commun, 2026 Cited by PubMed Abstract: Porcine circovirus type 3 (PCV3) is an emerging swine pathogen associated with reproductive failure and systemic inflammation, but vaccines for related PCV2 provide limited cross-protection. Here, we determine high-resolution cryo-EM structures of PCV3 capsid protein assembled into virus-like particles (VLPs) and of PCV3 VLPs bound to the PCV3-specific antibody 2B5. The structures reveal differences from PCV2 in surface loops and define a conserved 2B5 epitope mainly involving the BC, EF and HI loops, providing a structural basis for PCV3-specific recognition. PCV3 VLPs induce sustained antibody responses in mice and pigs. In a pig challenge model, VLP immunization prevents viremia and viral replication in lungs and lymph nodes, as measured by quantitative PCR and in situ hybridization, with protection maintained for at least five months after boosting. These findings support PCV3 VLPs as a vaccine candidate against PCV3 infection. PubMed: 42303972DOI: 10.1038/s41467-026-74388-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (1.73 Å) |
Structure validation
No wwPDB Validation report is currently available for this entry.
