6WO4

Structure of Hepatitis C Virus Envelope Glycoprotein E2 core from genotype 6a bound to broadly neutralizing antibody HC11

6WO4 の概要

• エントリーDOI: 10.2210/pdb6wo4/pdb
• 分子名称: Fab HC11 heavy chain, Envelope glycoprotein E2, Fab HC11 light chain, ... (6 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: 71593.33

構造登録者

Tzarum, N.,Wilson, I.A.,Law, M. (登録日: 2020-04-24, 公開日: 2020-08-19, 最終更新日: 2024-11-13)

主引用文献

Tzarum, N.,Giang, E.,Kadam, R.U.,Chen, F.,Nagy, K.,Augestad, E.H.,Velazquez-Moctezuma, R.,Keck, Z.Y.,Hua, Y.,Stanfield, R.L.,Dreux, M.,Prentoe, J.,Foung, S.K.H.,Bukh, J.,Wilson, I.A.,Law, M.
An alternate conformation of HCV E2 neutralizing face as an additional vaccine target.
Sci Adv, 6:eabb5642-eabb5642, 2020

PubMed Abstract: To achieve global elimination of hepatitis C virus (HCV), an effective cross-genotype vaccine is needed. The HCV envelope glycoprotein E2 is the main target for neutralizing antibodies (nAbs), which aid in HCV clearance and protection. E2 is structurally flexible and functions in engaging host receptors. Many nAbs bind to the "neutralizing face" on E2, including several broadly nAbs encoded by the germline gene family that bind to a similar conformation (A) of this face. Here, a previously unknown conformation (B) of the neutralizing face is revealed in crystal structures of two of four additional E2-V1-69 nAb complexes. In this conformation, the E2 front-layer region is displaced upon antibody binding, exposing residues in the back layer for direct antibody interaction. This E2 B structure may represent another conformational state in the viral entry process that is susceptible to antibody neutralization and thus provide a new target for rational vaccine development.

PubMed: 32754640
DOI: 10.1126/sciadv.abb5642

実験手法

X-RAY DIFFRACTION (2.349 Å)