3JCX
Canine Parvovirus complexed with Fab E
Summary for 3JCX
| Entry DOI | 10.2210/pdb3jcx/pdb |
| EMDB information | 6629 |
| Descriptor | Capsid protein 2, Fab E heavy chain, Fab E light chain (3 entities in total) |
| Functional Keywords | parvovirus, antibody, virus-immune system complex, virus/immune system |
| Biological source | Canine parvovirus (CPV-2) More |
| Total number of polymer chains | 3 |
| Total formula weight | 89267.99 |
| Authors | Organtini, L.J.,Iketani, S.,Huang, K.,Ashley, R.E.,Makhov, A.M.,Conway, J.F.,Parrish, C.R.,Hafenstein, S. (deposition date: 2016-03-21, release date: 2016-07-20, Last modification date: 2024-11-06) |
| Primary citation | Organtini, L.J.,Lee, H.,Iketani, S.,Huang, K.,Ashley, R.E.,Makhov, A.M.,Conway, J.F.,Parrish, C.R.,Hafenstein, S. Near-Atomic Resolution Structure of a Highly Neutralizing Fab Bound to Canine Parvovirus. J.Virol., 90:9733-9742, 2016 Cited by PubMed Abstract: Canine parvovirus (CPV) is a highly contagious pathogen that causes severe disease in dogs and wildlife. Previously, a panel of neutralizing monoclonal antibodies (MAb) raised against CPV was characterized. An antibody fragment (Fab) of MAb E was found to neutralize the virus at low molar ratios. Using recent advances in cryo-electron microscopy (cryo-EM), we determined the structure of CPV in complex with Fab E to 4.1 Å resolution, which allowed de novo building of the Fab structure. The footprint identified was significantly different from the footprint obtained previously from models fitted into lower-resolution maps. Using single-chain variable fragments, we tested antibody residues that control capsid binding. The near-atomic structure also revealed that Fab binding had caused capsid destabilization in regions containing key residues conferring receptor binding and tropism, which suggests a mechanism for efficient virus neutralization by antibody. Furthermore, a general technical approach to solving the structures of small molecules is demonstrated, as binding the Fab to the capsid allowed us to determine the 50-kDa Fab structure by cryo-EM. PubMed: 27535057DOI: 10.1128/JVI.01112-16 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.1 Å) |
Structure validation
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