6BZU
Structure of the Hepatitis C virus envelope glycoprotein E2 antigenic region 412-423 bound to the broadly neutralizing antibody 19B3
Summary for 6BZU
| Entry DOI | 10.2210/pdb6bzu/pdb |
| Descriptor | 19B3 Heavy Chain, 19B3 Light Chain, E2 AS412 peptide, ... (4 entities in total) |
| Functional Keywords | hepatitis c virus, immune system, antibodies, broadly neutralizing antibodies, rational vaccine design, as412, e2, viral protein |
| Biological source | Mus musculus More |
| Total number of polymer chains | 12 |
| Total formula weight | 196922.21 |
| Authors | Tzarum, N.,Aleman, F.,Kong, L.,Wilson, I.A.,Law, M. (deposition date: 2017-12-26, release date: 2018-06-20, Last modification date: 2024-10-23) |
| Primary citation | Aleman, F.,Tzarum, N.,Kong, L.,Nagy, K.,Zhu, J.,Wilson, I.A.,Law, M. Immunogenetic and structural analysis of a class of HCV broadly neutralizing antibodies and their precursors. Proc. Natl. Acad. Sci. U.S.A., 115:7569-7574, 2018 Cited by PubMed Abstract: Elicitation of broadly neutralizing antibodies (bnAbs) is a leading strategy in rational vaccine design against antigenically diverse pathogens. Here, we studied a panel of monoclonal antibodies (mAbs) from mice immunized with the hepatitis C virus (HCV) envelope glycoproteins E1E2. Six of the mAbs recognize the conserved E2 antigenic site 412-423 (AS412) and cross-neutralize diverse HCV genotypes. Immunogenetic and structural analysis revealed that the antibodies originated from two different germline (GL) precursors and bind AS412 in a β-hairpin conformation. Intriguingly, the anti-HCV activity of one antibody lineage is associated with maturation of the light chain (LC), whereas the other lineage is dependent on heavy-chain (HC) maturation. Crystal structures of GL precursors of the LC-dependent lineage in complex with AS412 offer critical insights into the maturation process of bnAbs to HCV, providing a scientific foundation for utilizing the mouse model to study AS412-targeting vaccine candidates. PubMed: 29954862DOI: 10.1073/pnas.1802378115 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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