Summary for 8YEH
Entry DOI | 10.2210/pdb8yeh/pdb |
EMDB information | 39195 |
Descriptor | heavy chain of F5-196, light chain of F5-196, Major capsid protein L1 (3 entities in total) |
Functional Keywords | hpv16, l1, antibody, viral protein, viral protein-immune system complex, viral protein/immune system |
Biological source | Homo sapiens More |
Total number of polymer chains | 15 |
Total formula weight | 378429.90 |
Authors | |
Primary citation | Hu, J.,Jia, Z.,Wang, M.,Nie, L.,Fu, W.,Zhang, Q.,Qin, H.,Nie, J.,Xu, X.,Xu, L.,Wang, F.,Chen, Y.,Xing, B.,Li, T.,Li, D.,Li, S.,Xia, N.,Wang, X.,Huang, W. Establishing a universal IVRP method for quadrivalent HPV vaccines to replace in vivo potency tests. Npj Vaccines, 10:55-55, 2025 Cited by PubMed Abstract: Several human papillomavirus (HPV) L1-based virus-like particle (VLP) vaccines are in development to meet future global vaccination needs. Type-specific monoclonal antibodies with good reactivity to all types of vaccines are urgently needed to evaluate vaccine potency. In this study, binding activity, neutralizing activity, conformational sensitivity, immunodominance in human serum, and versatility were compared among antibodies. A broad-spectrum binding antibody (C4-F5-127) was selected as the capture antibody; four type-specific neutralizing antibodies (6-F5-77, 11-F5-187, 16-F5-196, and 18-F5-203) were selected as detection antibodies for HPV6, 11, 16, and 18, respectively. These antibodies formed a standardized and universal in vitro relative potency (IVRP) assay kit. High-resolution cryo-electron microscopy (cryo-EM) structures of HPV6-6-F5-77, HPV11-11-F5-187, HPV16-16-F5-196 and HPV18-18-F5-203 complexes define the location and nature of epitopes, revealing serotype specific binding modes and neutralization mechanisms. The IVRP results were correlated with potency data from mouse models, offering an efficient alternative to in vivo potency experiments. PubMed: 40118915DOI: 10.1038/s41541-025-01106-z PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.86 Å) |
Structure validation
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