8UA8

Structure of Semliki Forest virus VLP in complex with VLDLR LA2

8UA8 の概要

• エントリーDOI: 10.2210/pdb8ua8/pdb
• EMDBエントリー: 42054
• 分子名称: Glycoprotein E1, Glycoprotein E2, Assembly protein E3, ... (9 entities in total)
• 機能のキーワード: semliki forest virus, receptor, virus like particle
• 由来する生物種: Semliki Forest virus; 詳細
• タンパク質・核酸の鎖数: 17
• 化学式量合計: 476837.58

構造登録者

Abraham, J.,Yang, P.,Li, W.,Fan, X.,Pan, J. (登録日: 2023-09-20, 公開日: 2024-08-14, 最終更新日: 2025-05-28)

主引用文献

Yang, P.,Li, W.,Fan, X.,Pan, J.,Mann, C.J.,Varnum, H.,Clark, L.E.,Clark, S.A.,Coscia, A.,Basu, H.,Smith, K.N.,Brusic, V.,Abraham, J.
Structural basis for VLDLR recognition by eastern equine encephalitis virus.
Nat Commun, 15:6548-6548, 2024

PubMed Abstract: Eastern equine encephalitis virus (EEEV) is the most virulent alphavirus that infects humans, and many survivors develop neurological sequelae, including paralysis and intellectual disability. Alphavirus spike proteins comprise trimers of heterodimers of glycoproteins E2 and E1 that mediate binding to cellular receptors and fusion of virus and host cell membranes during entry. We recently identified very-low density lipoprotein receptor (VLDLR) and apolipoprotein E receptor 2 (ApoER2) as cellular receptors for EEEV and a distantly related alphavirus, Semliki Forest virus (SFV). Here, we use single-particle cryo-electron microscopy (cryo-EM) to determine structures of the EEEV and SFV spike glycoproteins bound to the VLDLR ligand-binding domain and found that EEEV and SFV interact with the same cellular receptor through divergent binding modes. Our studies suggest that the ability of LDLR-related proteins to interact with viral spike proteins through very small footprints with flexible binding modes results in a low evolutionary barrier to the acquisition of LDLR-related proteins as cellular receptors for diverse sets of viruses.

PubMed: 39095394
DOI: 10.1038/s41467-024-50887-9

実験手法

ELECTRON MICROSCOPY (3.7 Å)