6BKC
Structure of Hepatitis C Virus Envelope Glycoprotein E2 core from genotype 6a bound to broadly neutralizing antibody AR3B
6BKC の概要
エントリーDOI | 10.2210/pdb6bkc/pdb |
分子名称 | Fab AR3B heavy chain, Fab AR3B light chain, Polyprotein, ... (5 entities in total) |
機能のキーワード | hcv, broadly neutralizing antibodies, bnabs, e2 core, ighv1-69, immune system |
由来する生物種 | Homo sapiens (Human) 詳細 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 69046.24 |
構造登録者 | |
主引用文献 | Tzarum, N.,Giang, E.,Kong, L.,He, L.,Prentoe, J.,Augestad, E.,Hua, Y.,Castillo, S.,Lauer, G.M.,Bukh, J.,Zhu, J.,Wilson, I.A.,Law, M. Genetic and structural insights into broad neutralization of hepatitis C virus by human VH1-69 antibodies. Sci Adv, 5:eaav1882-eaav1882, 2019 Cited by PubMed Abstract: An effective vaccine to the antigenically diverse hepatitis C virus (HCV) must target conserved immune epitopes. Here, we investigate cross-neutralization of HCV genotypes by broadly neutralizing antibodies (bNAbs) encoded by the relatively abundant human gene family . We have deciphered the molecular requirements for cross-neutralization by this unique class of human antibodies from crystal structures of HCV E2 in complex with bNAbs. An unusually high binding affinity is found for germ line-reverted versions of V1-69 precursor antibodies, and neutralization breadth is acquired during affinity maturation. Deep sequencing analysis of an HCV-immune B cell repertoire further demonstrates the importance of the gene family in the generation of HCV bNAbs. This study therefore provides critical insights into immune recognition of HCV with important implications for rational vaccine design. PubMed: 30613781DOI: 10.1126/sciadv.aav1882 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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