9VZ8
Local refinement region of HPV45 in complex with antibody 10G2
Summary for 9VZ8
| Entry DOI | 10.2210/pdb9vz8/pdb |
| EMDB information | 65478 |
| Descriptor | Major capsid protein L1, 10G2 Fab light chain, 10G2 Fab heavy chain (3 entities in total) |
| Functional Keywords | human papillomavirus, cryo-em, structural protein, virus like particle |
| Biological source | human papillomavirus 45 More |
| Total number of polymer chains | 5 |
| Total formula weight | 197721.04 |
| Authors | |
| Primary citation | Jiang, Y.,Wang, Z.,Xu, Q.,Zhang, S.,Su, J.,Sun, H.,Zhang, C.,Zhou, L.,Li, T.,Kong, Z.,Yu, H.,Zhang, J.,Zheng, Q.,Gu, Y.,Xia, N.,Li, S. Structural and biochemical characterization of neutralizing antibodies targeting human papillomavirus type 45. Structure, 34:588-598.e4, 2026 Cited by PubMed Abstract: Human papillomavirus type 45 (HPV45) is a high-risk genotype and the third most prevalent HPV type associated with cervical cancer worldwide, posing a significant public health concern. Although HPV45 is included in the commercial 9-valent HPV vaccine, its complete virion structure and the molecular basis of antibody-mediated neutralization remain incompletely understood. Here, we report the near-atomic resolution structure of the HPV45 pseudovirus (PsV45) determined by cryo-electron microscopy. We also isolated and structurally characterized several neutralizing monoclonal antibodies (nAbs) targeting PsV45. Our analysis reveals two distinct neutralizing epitopes on PsV45, and these nAbs likely neutralize the virus by a common mechanism involving the inhibition of viral attachment, despite differences in their binding interfaces. Biochemical assays confirmed that antibodies with non-overlapping binding modes can engage PsV45 simultaneously, indicating potential for synergistic combinations. These findings elucidate the structural basis of HPV45 type specificity and provide insights into HPV neutralization mechanisms. PubMed: 41722563DOI: 10.1016/j.str.2026.01.012 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.81 Å) |
Structure validation
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