8RJJ
HCV E1/E2 homodimer complex
Summary for 8RJJ
| Entry DOI | 10.2210/pdb8rjj/pdb |
| EMDB information | 19243 |
| Descriptor | Genome polyprotein, HCV S52 E2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | hepatitis c virus s52 e1 e2 homodimer structure, viral protein |
| Biological source | Hepacivirus hominis More |
| Total number of polymer chains | 4 |
| Total formula weight | 132843.97 |
| Authors | Augestad, E.H.,Olesen, C.H.,Groenberg, C.,Soerensen, A.,Velazquez-Moctezuma, R.,Fanalista, M.,Bukh, J.,Wang, K.,Gourdon, P.,Prentoe, J. (deposition date: 2023-12-21, release date: 2024-09-04, Last modification date: 2024-10-23) |
| Primary citation | Augestad, E.H.,Holmboe Olesen, C.,Gronberg, C.,Soerensen, A.,Velazquez-Moctezuma, R.,Fanalista, M.,Bukh, J.,Wang, K.,Gourdon, P.,Prentoe, J. The hepatitis C virus envelope protein complex is a dimer of heterodimers. Nature, 633:704-709, 2024 Cited by PubMed Abstract: Fifty-eight million individuals worldwide are affected by chronic hepatitis C virus (HCV) infection, a primary driver of liver cancer for which no vaccine is available. The HCV envelope proteins E1 and E2 form a heterodimer (E1/E2), which is the target for neutralizing antibodies. However, the higher-order organization of these E1/E2 heterodimers, as well as that of any Hepacivirus envelope protein complex, remains unknown. Here we determined the cryo-electron microscopy structure of two E1/E2 heterodimers in a homodimeric arrangement. We reveal how the homodimer is established at the molecular level and provide insights into neutralizing antibody evasion and membrane fusion by HCV, as orchestrated by E2 motifs such as hypervariable region 1 and antigenic site 412, as well as the organization of the transmembrane helices, including two internal to E1. This study addresses long-standing questions on the higher-order oligomeric arrangement of Hepacivirus envelope proteins and provides a critical framework in the design of novel HCV vaccine antigens. PubMed: 39232163DOI: 10.1038/s41586-024-07783-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.55 Å) |
Structure validation
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