3J9D

Atomic structure of a non-enveloped virus reveals pH sensors for a coordinated process of cell entry

3J9D の概要

• エントリーDOI: 10.2210/pdb3j9d/pdb
• 関連するPDBエントリー: 3J9E
• EMDBエントリー: 6239 6240
• 分子名称: Outer capsid protein VP2, ZINC ION (2 entities in total)
• 機能のキーワード: non-enveloped virus, cell entry, ph sensor, viral protein
• 由来する生物種: Bluetongue virus 1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 112190.87

構造登録者

Zhang, X.,Patel, A.,Celma, C.,Roy, P.,Zhou, Z.H. (登録日: 2015-01-09, 公開日: 2015-12-09, 最終更新日: 2024-02-21)

主引用文献

Zhang, X.,Patel, A.,Celma, C.C.,Yu, X.,Roy, P.,Zhou, Z.H.
Atomic model of a nonenveloped virus reveals pH sensors for a coordinated process of cell entry.
Nat.Struct.Mol.Biol., 23:74-80, 2016

PubMed Abstract: Viruses sense environmental cues such as pH to engage in membrane interactions for cell entry during infection, but how nonenveloped viruses sense pH is largely undefined. Here, we report both high- and low-pH structures of bluetongue virus (BTV), which enters cells via a two-stage endosomal process. The receptor-binding protein VP2 possesses a zinc finger that may function to maintain VP2 in a metastable state and a conserved His866, which senses early-endosomal pH. The membrane-penetration protein VP5 has three domains: dagger, unfurling and anchoring. Notably, the β-meander motif of the anchoring domain contains a histidine cluster that can sense late-endosomal pH and also possesses four putative membrane-interaction elements. Exposing BTV to low pH detaches VP2 and dramatically refolds the dagger and unfurling domains of VP5. Our biochemical and structure-guided-mutagenesis studies support these coordinated pH-sensing mechanisms.

PubMed: 26641711
DOI: 10.1038/nsmb.3134

実験手法

ELECTRON MICROSCOPY (3.3 Å)