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9VWZ

Local refinement region of HPV45 in complex with antibody A16E6

This is a non-PDB format compatible entry.
Summary for 9VWZ
Entry DOI10.2210/pdb9vwz/pdb
EMDB information65403
DescriptorA16E6 Fab light chain, A16E6 Fab heavy chain, Major capsid protein L1 (3 entities in total)
Functional Keywordshuman papillomavirus, cryo-em, structural protein/immune system, structural protein-immune system complex
Biological sourcehuman papillomavirus 45
More
Total number of polymer chains7
Total formula weight311908.29
Authors
Jiang, Y.,Sun, H.,Zheng, Q.,Li, S. (deposition date: 2025-07-17, release date: 2026-02-11, Last modification date: 2026-07-01)
Primary citationJiang, 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: 41722563
DOI: 10.1016/j.str.2026.01.012
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4 Å)
Structure validation

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