Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9OCL

PV2-10D2 Complex

Summary for 9OCL
Entry DOI10.2210/pdb9ocl/pdb
EMDB information70318
DescriptorCapsid protein VP1, Capsid protein VP2, Capsid protein VP3, ... (7 entities in total)
Functional Keywordsvirus, antibody, complex
Biological sourcePoliovirus 2
More
Total number of polymer chains6
Total formula weight122905.91
Authors
Waddey, B.T.,Hafenstein, S.L. (deposition date: 2025-04-24, release date: 2025-12-17, Last modification date: 2026-01-14)
Primary citationWaddey, B.T.,Charnesky, A.J.,Faust, J.E.,DiNunno, N.M.,Puligedda, R.D.,Cho, S.H.,Bator, C.M.,Dong, S.D.,Mahmood, K.,Chumakov, K.M.,Dessain, S.K.,Hafenstein, S.L.
Neutralizing human monoclonal antibodies to poliovirus map to the receptor binding site.
Nat Commun, 2026
Cited by
PubMed Abstract: Poliovirus remains a serious threat to human health. Complete eradication of wild-type poliovirus has not yet succeeded, making the development of successful antivirals critical. Microneutralization assays against all three poliovirus serotypes identified a panel of human monoclonal IgGs, which are either serotype-specific or cross-neutralizing. Here, through cryoEM single particle analysis, we solved high resolution structures of four distinct poliovirus-FAb complexes. These antibodies bind to capsids at the circular depression (canyon) surrounding the icosahedral five-fold symmetry axis, which is also the binding site of the poliovirus receptor (PVR). Analysis of these structures confirms overlap of FAb contacts on the viral capsid with those of PVR. For three of the FAbs, the capsid residues are identified that dictate serotype-specific recognition. Contacts for the cross-neutralizing mAb 10D2 are located deep in the capsid canyon. These structural analyses indicate that antibody competition with the receptor likely leads to neutralization of virus particles and inhibition of poliovirus entry into host cells. Thus, the human IgGs studied here may facilitate development of therapeutics for the ongoing efforts in global eradication of poliovirus.
PubMed: 41484135
DOI: 10.1038/s41467-025-68226-x
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.65 Å)
Structure validation

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon