8UFC

Eastern equine encephalitis virus (PE-6) VLP in complex with VLDLR LA(1-2) (asymmetric unit)

これはPDB形式変換不可エントリーです。

8UFC の概要

• エントリーDOI: 10.2210/pdb8ufc/pdb
• EMDBエントリー: 42192
• 分子名称: E1 protein, E2 protein, Capsid protein, ... (6 entities in total)
• 機能のキーワード: virus, receptor, structural genomics, center for structural biology of infectious diseases, csbid, viral protein
• 由来する生物種: Eastern equine encephalitis virus; 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 479847.80

構造登録者

Adams, L.J.,Fremont, D.H.,Center for Structural Biology of Infectious Diseases (CSBID) (登録日: 2023-10-04, 公開日: 2024-01-17, 最終更新日: 2025-06-04)

主引用文献

Adams, L.J.,Raju, S.,Ma, H.,Gilliland Jr., T.,Reed, D.S.,Klimstra, W.B.,Fremont, D.H.,Diamond, M.S.
Structural and functional basis of VLDLR usage by Eastern equine encephalitis virus.
Cell, 187:360-374.e19, 2024

PubMed Abstract: The very-low-density lipoprotein receptor (VLDLR) comprises eight LDLR type A (LA) domains and supports entry of distantly related alphaviruses, including Eastern equine encephalitis virus (EEEV) and Semliki Forest virus (SFV). Here, by resolving multiple cryo-electron microscopy structures of EEEV-VLDLR complexes and performing mutagenesis and functional studies, we show that EEEV uses multiple sites (E1/E2 cleft and E2 A domain) to engage more than one LA domain simultaneously. However, no single LA domain is necessary or sufficient to support efficient EEEV infection. Whereas all EEEV strains show conservation of two VLDLR-binding sites, the EEEV PE-6 strain and a few other EEE complex members feature a single amino acid substitution that enables binding of LA domains to an additional site on the E2 B domain. These structural and functional analyses informed the design of a minimal VLDLR decoy receptor that neutralizes EEEV infection and protects mice from lethal challenge.

PubMed: 38176410
DOI: 10.1016/j.cell.2023.11.031

実験手法

ELECTRON MICROSCOPY (3.09 Å)