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Open data
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Basic information
| Entry | Database: PDB / ID: 9i40 | |||||||||
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| Title | Structure of anti-EV71 human monoclonal antibody 16-3-4D Fab | |||||||||
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Keywords | ANTIVIRAL PROTEIN / EV71 / antibody / 16-3-4D / Fab | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.78 Å | |||||||||
Authors | Zhou, D. / Ren, J. / Stuart, D.I. | |||||||||
| Funding support | United Kingdom, 2items
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Citation | Journal: Sci Adv / Year: 2026Title: Structural and functional mapping of protective human monoclonal antibodies against enterovirus A71. Authors: Daming Zhou / Abhay Kotecha / James T Kelly / Peng-Nien Huang / Yi-Yin Chen / Thomas S Walter / Helen M E Duyvesteyn / Raymond J Owens / Shu-Yuan Ho / Tzou-Yien Lin / Elizabeth E Fry / ...Authors: Daming Zhou / Abhay Kotecha / James T Kelly / Peng-Nien Huang / Yi-Yin Chen / Thomas S Walter / Helen M E Duyvesteyn / Raymond J Owens / Shu-Yuan Ho / Tzou-Yien Lin / Elizabeth E Fry / Jingshan Ren / Kuan-Ying A Huang / David I Stuart / ![]() Abstract: EV-A71 has been responsible for recent severe HFMD outbreaks. We report structures for 12 potently neutralizing human anti-EV-A71 monoclonal antibody Fabs, alone and complexed with virus. Most ...EV-A71 has been responsible for recent severe HFMD outbreaks. We report structures for 12 potently neutralizing human anti-EV-A71 monoclonal antibody Fabs, alone and complexed with virus. Most recognize the native antigenic state with epitopes that span interfaces, together covering 85% of the capsid surface. The majority (8 of 12) bind the canyon, while the others cluster around the icosahedral two- and threefold axes. Blocking SCARB2 receptor binding likely contributes to neutralization for all, and a subset induces empty particles. A predominant gene family (IGHV4-39) does not dictate a common binding pose. Long CDR-H3 loops are frequently key to binding, especially at the canyon, suggesting that antigenicity data based on antibodies with shorter CDR3s (e.g., murine) may be misleading. This dataset reveals neutralization mechanisms for recently circulating EV-A71 genotypes, which will inform immunotherapies. We demonstrate synergy in vitro between canyon binding and both two- and threefold binding antibodies to increase neutralization potency. | |||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9i40.cif.gz | 424.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9i40.ent.gz | 294.8 KB | Display | PDB format |
| PDBx/mmJSON format | 9i40.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i4/9i40 ftp://data.pdbj.org/pub/pdb/validation_reports/i4/9i40 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 9i3wC ![]() 9i3zC ![]() 9i41C ![]() 9i42C ![]() 9i43C ![]() 9i45C ![]() 9i4bC ![]() 9i4cC ![]() 9i4dC ![]() 9i4eC ![]() 9rigC ![]() 9rihC ![]() 9riiC ![]() 9rijC ![]() 9rikC ![]() 9rilC ![]() 9rimC ![]() 9rinC ![]() 9rioC ![]() 9ripC ![]() 9riqC ![]() 9rirC ![]() 9t6zC C: citing same article ( |
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Assembly
| Deposited unit | ![]()
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| Noncrystallographic symmetry (NCS) | NCS domain:
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Components
About Yorodumi




Homo sapiens (human)
X-RAY DIFFRACTION
United Kingdom, 2items
Citation





































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