3J7G
Electron cryo-microscopy of human papillomavirus 16 and H16.V5 Fab fragments
Summary for 3J7G
| Entry DOI | 10.2210/pdb3j7g/pdb |
| Related | 3J7E |
| EMDB information | 5991 5992 5993 5994 |
| Descriptor | L1 (1 entity in total) |
| Functional Keywords | pentamer of human papillomavirus, qv16-v5 complex, virus-fab complex, neutralization antibody, maturation, virus |
| Biological source | Human papillomavirus type 16 |
| Total number of polymer chains | 5 |
| Total formula weight | 254367.11 |
| Authors | Lee, H.,Hafenstein, S. (deposition date: 2014-06-24, release date: 2014-11-26, Last modification date: 2024-02-21) |
| Primary citation | Lee, H.,Brendle, S.A.,Bywaters, S.M.,Guan, J.,Ashley, R.E.,Yoder, J.D.,Makhov, A.M.,Conway, J.F.,Christensen, N.D.,Hafenstein, S. A cryo-electron microscopy study identifies the complete H16.V5 epitope and reveals global conformational changes initiated by binding of the neutralizing antibody fragment. J.Virol., 89:1428-1438, 2015 Cited by PubMed Abstract: Human papillomavirus 16 (HPV16) is a worldwide health threat and an etiologic agent of cervical cancer. To understand the antigenic properties of HPV16, we pursued a structural study to elucidate HPV capsids and antibody interactions. The cryo-electron microscopy (cryo-EM) structures of a mature HPV16 particle and an altered capsid particle were solved individually and as complexes with fragment of antibody (Fab) from the neutralizing antibody H16.V5. Fitted crystal structures provided a pseudoatomic model of the virus-Fab complex, which identified a precise footprint of H16.V5, including previously unrecognized residues. The altered-capsid-Fab complex map showed that binding of the Fab induced significant conformational changes that were not seen in the altered-capsid structure alone. These changes included more ordered surface loops, consolidated so-called "invading-arm" structures, and tighter intercapsomeric connections at the capsid floor. The H16.V5 Fab preferentially bound hexavalent capsomers likely with a stabilizing effect that directly correlated with the number of bound Fabs. Additional cryo-EM reconstructions of the virus-Fab complex for different incubation times and structural analysis provide a model for a hyperstabilization of the capsomer by H16.V5 Fab and showed that the Fab distinguishes subtle differences between antigenic sites. PubMed: 25392224DOI: 10.1128/JVI.02898-14 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (13.6 Å) |
Structure validation
Download full validation report
