5VOD
Crystal structure of HCMV Pentamer in complex with neutralizing antibody 9I6
Summary for 5VOD
| Entry DOI | 10.2210/pdb5vod/pdb |
| Related | 5COB 5VOC |
| Descriptor | Envelope glycoprotein H, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, Envelope glycoprotein L, ... (10 entities in total) |
| Functional Keywords | hcmv, neutralizing epitope, immunogen, viral entry, pentamer, vaccine, immune system, viral protein-immune system complex, viral protein/immune system |
| Biological source | Human cytomegalovirus (HHV-5) More |
| Cellular location | Virion membrane ; Single-pass type I membrane protein : Q6SW67 Virion membrane ; Peripheral membrane protein ; Extracellular side : Q68674 Virion : F5HET4 |
| Total number of polymer chains | 7 |
| Total formula weight | 237952.80 |
| Authors | Malito, E.,Chandramouli, S. (deposition date: 2017-05-02, release date: 2017-07-05, Last modification date: 2024-10-16) |
| Primary citation | Chandramouli, S.,Malito, E.,Nguyen, T.,Luisi, K.,Donnarumma, D.,Xing, Y.,Norais, N.,Yu, D.,Carfi, A. Structural basis for potent antibody-mediated neutralization of human cytomegalovirus. Sci Immunol, 2:-, 2017 Cited by PubMed Abstract: Human cytomegalovirus (HCMV) is the leading viral cause of birth defects and organ transplant rejection. The HCMV gH/gL/UL128/UL130/UL131A complex (Pentamer) is the main target of humoral responses and thus a key vaccine candidate. We report two structures of Pentamer bound to human neutralizing antibodies, 8I21 and 9I6, at 3.0 and 5.9 Å resolution, respectively. The HCMV gH/gL architecture is similar to that of Epstein-Barr virus (EBV) except for amino-terminal extensions on both subunits. The extension of gL forms a subdomain composed of a three-helix bundle and a β hairpin that acts as a docking site for UL128/UL130/UL131A. Structural analysis reveals that Pentamer is a flexible molecule, and suggests sites for engineering stabilizing mutations. We also identify immunogenic surfaces important for cellular interactions by epitope mapping and functional assays. These results can guide the development of effective vaccines and immunotherapeutics against HCMV. PubMed: 28783665DOI: 10.1126/sciimmunol.aan1457 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (5.9 Å) |
Structure validation
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