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Yorodumi- EMDB-65403: Local refinement region of HPV45 in complex with antibody A16E6 -
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Basic information
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| Title | Local refinement region of HPV45 in complex with antibody A16E6 | |||||||||
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Keywords | Human papillomavirus / Cryo-EM / STRUCTURAL PROTEIN/IMMUNE SYSTEM / STRUCTURAL PROTEIN-IMMUNE SYSTEM complex | |||||||||
| Function / homology | Function and homology informationT=7 icosahedral viral capsid / endocytosis involved in viral entry into host cell / virion attachment to host cell / host cell nucleus / structural molecule activity Similarity search - Function | |||||||||
| Biological species | Human papillomavirus 45 / ![]() human papillomavirus 45 | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 4.0 Å | |||||||||
Authors | Jiang Y / Sun H / Zheng Q / Li S / Xia N | |||||||||
| Funding support | 1 items
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Citation | Journal: Structure / Year: 2026Title: Structural and biochemical characterization of neutralizing antibodies targeting human papillomavirus type 45. Authors: Yanan Jiang / Zhiping Wang / Qin Xu / Shuyue Zhang / Jinfu Su / Hui Sun / Chengzong Zhang / Lizhi Zhou / Tingting Li / Zhibo Kong / Hai Yu / Jun Zhang / Qingbing Zheng / Ying Gu / Ningshao Xia / Shaowei Li / ![]() 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 ...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. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_65403.map.gz | 266.7 MB | EMDB map data format | |
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| Header (meta data) | emd-65403-v30.xml emd-65403.xml | 20.8 KB 20.8 KB | Display Display | EMDB header |
| Images | emd_65403.png | 59.8 KB | ||
| Filedesc metadata | emd-65403.cif.gz | 6.5 KB | ||
| Others | emd_65403_half_map_1.map.gz emd_65403_half_map_2.map.gz | 261.8 MB 261.8 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-65403 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-65403 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9vwzMC ![]() 9vz8C ![]() 9wlrC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_65403.map.gz / Format: CCP4 / Size: 282.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_65403_half_map_1.map | ||||||||||||
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-Half map: #1
| File | emd_65403_half_map_2.map | ||||||||||||
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Sample components
-Entire : Local refinement region of HPV45 in complex with antibody A16E6
| Entire | Name: Local refinement region of HPV45 in complex with antibody A16E6 |
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| Components |
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-Supramolecule #1: Local refinement region of HPV45 in complex with antibody A16E6
| Supramolecule | Name: Local refinement region of HPV45 in complex with antibody A16E6 type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: Human papillomavirus 45 |
-Supramolecule #2: Human papillomavirus type 45
| Supramolecule | Name: Human papillomavirus type 45 / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #3 |
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| Source (natural) | Organism: Human papillomavirus 45 |
-Supramolecule #3: The Fab fragment of A16E6
| Supramolecule | Name: The Fab fragment of A16E6 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #1-#2 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: A16E6 Fab light chain
| Macromolecule | Name: A16E6 Fab light chain / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 11.390643 KDa |
| Sequence | String: QIVLTQSPAI MSASPGEKVT ISCSASSSVS YMYWYQQKPG SSPKPWIYRT SNLASGVPAR FSGSGSGTSY SLTISSMEAE DAATYYCQQ YHSYPPTFGG GTKLEIK |
-Macromolecule #2: A16E6 Fab heavy chain
| Macromolecule | Name: A16E6 Fab heavy chain / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 13.618193 KDa |
| Sequence | String: QVQLQQSGPE LVRPGVSVKI SCKGSGYTFT DYSMHWVKQS HTKSLEWIGV ISTYYGKTNY NQRFKGKATM TVDKSSSTAY MELARLTSE DSAIYYCARR YDGKADYGMD YWGQGTSVTV SS |
-Macromolecule #3: Major capsid protein L1
| Macromolecule | Name: Major capsid protein L1 / type: protein_or_peptide / ID: 3 / Number of copies: 5 / Enantiomer: LEVO |
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| Source (natural) | Organism: human papillomavirus 45 |
| Molecular weight | Theoretical: 57.379891 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MALWRPSDST VYLPPPSVAR VVSTDDYVSR TSIFYHAGSS RLLTVGNPYF RVVPNGAGNK QAVPKVSAYQ YRVFRVALPD PNKFGLPDS TIYNPETQRL VWACVGMEIG RGQPLGIGLS GHPFYNKLDD TESAHAATAV ITQDVRDNVS VDYKQTQLCI L GCVPAIGE ...String: MALWRPSDST VYLPPPSVAR VVSTDDYVSR TSIFYHAGSS RLLTVGNPYF RVVPNGAGNK QAVPKVSAYQ YRVFRVALPD PNKFGLPDS TIYNPETQRL VWACVGMEIG RGQPLGIGLS GHPFYNKLDD TESAHAATAV ITQDVRDNVS VDYKQTQLCI L GCVPAIGE HWAKGTLCKP AQLQPGDCPP LELKNTIIED GDMVDTGYGA MDFSTLQDTK CEVPLDICQS ICKYPDYLQM SA DPYGDSM FFCLRREQLF ARHFWNRAGV MGDTVPTDLY IKGTSANMRE TPGSCVYSPS PSGSIITSDS QLFNKPYWLH KAQ GHNNGI CWHNQLFVTV VDTTRSTNLT LCASTQNPVP STYDPTKFKQ YSRHVEEYDL QFIFQLCTIT LTAEVMSYIH SMNS SILEN WNFGVPPPPT TSLVDTYRFV QSVAVTCQKD TTPPEKQDPY DKLKFWTVDL KEKFSSDLDQ YPLGRKFLVQ AGLRR RPTI GPRKRPAAST STASTASRPA KRVRIRSKK UniProtKB: Major capsid protein L1 |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.4 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TECNAI F30 |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.7 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Tecnai F30 / Image courtesy: FEI Company |
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Keywords
Human papillomavirus 45
Authors
Citation






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Processing
FIELD EMISSION GUN
