9DQX

Structure of western equine encephalitis virus CBA87 VLP

9DQX の概要

• エントリーDOI: 10.2210/pdb9dqx/pdb
• EMDBエントリー: 47117
• 分子名称: Structural polyprotein, Capsid protein, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: western equine encephalitis virus, weev, virus like particles, virus like particle
• 由来する生物種: Western equine encephalitis virus; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 443735.71

構造登録者

Abraham, J.,Fan, X.,Li, W. (登録日: 2024-09-24, 公開日: 2025-03-26, 最終更新日: 2026-04-08)

主引用文献

Fan, X.,Li, W.,Oros, J.,Plante, J.A.,Mitchell, B.M.,Plung, J.S.,Basu, H.,Nagappan-Chettiar, S.,Boeckers, J.M.,Tjang, L.V.,Mann, C.J.,Brusic, V.,Buck, T.K.,Varnum, H.,Yang, P.,Malcolm, L.M.,Choi, S.Y.,de Souza, W.M.,Chiu, I.M.,Umemori, H.,Weaver, S.C.,Plante, K.S.,Abraham, J.
Molecular basis for shifted receptor recognition by an encephalitic arbovirus.
Cell, 188:2957-2973.e28, 2025

PubMed Abstract: Western equine encephalitis virus (WEEV) is an arbovirus that historically caused large outbreaks of encephalitis throughout the Americas. WEEV binds protocadherin 10 (PCDH10) as a receptor, and highly virulent ancestral WEEV strains also bind low-density lipoprotein receptor (LDLR)-related proteins. As WEEV declined as a human pathogen in North America over the past century, isolates have lost the ability to bind mammalian receptors while still recognizing avian receptors. To explain shifts in receptor dependencies and assess the risk of WEEV re-emergence, we determined cryoelectron microscopy structures of WEEV bound to human PCDH10, avian PCDH10, and human very-low-density lipoprotein receptor (VLDLR). We show that one to three E2 glycoprotein substitutions are sufficient for a nonpathogenic strain to regain the ability to bind mammalian receptors. A soluble VLDLR fragment protects mice from lethal challenge by a virulent ancestral WEEV strain. Because WEEV recently re-emerged in South America after decades of inactivity, our findings have important implications for outbreak preparedness.

PubMed: 40187345
DOI: 10.1016/j.cell.2025.03.029

実験手法

ELECTRON MICROSCOPY (3.4 Å)