6Y6Q

Structure of Andes virus envelope glycoprotein Gc in postfusion conformation

6Y6Q の概要

• エントリーDOI: 10.2210/pdb6y6q/pdb
• 分子名称: Envelope polyprotein, alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: class-ii fusion protein hantavirus bunyavirus, viral protein, postfusion conformation
• 由来する生物種: Andes orthohantavirus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55211.66

構造登録者

Serris, A.,Rey, F.A.,Guardado-Calvo, P. (登録日: 2020-02-27, 公開日: 2020-10-14, 最終更新日: 2024-11-13)

主引用文献

Serris, A.,Stass, R.,Bignon, E.A.,Muena, N.A.,Manuguerra, J.C.,Jangra, R.K.,Li, S.,Chandran, K.,Tischler, N.D.,Huiskonen, J.T.,Rey, F.A.,Guardado-Calvo, P.
The Hantavirus Surface Glycoprotein Lattice and Its Fusion Control Mechanism.
Cell, 183:442-, 2020

PubMed Abstract: Hantaviruses are rodent-borne viruses causing serious zoonotic outbreaks worldwide for which no treatment is available. Hantavirus particles are pleomorphic and display a characteristic square surface lattice. The envelope glycoproteins Gn and Gc form heterodimers that further assemble into tetrameric spikes, the lattice building blocks. The glycoproteins, which are the sole targets of neutralizing antibodies, drive virus entry via receptor-mediated endocytosis and endosomal membrane fusion. Here we describe the high-resolution X-ray structures of the heterodimer of Gc and the Gn head and of the homotetrameric Gn base. Docking them into an 11.4-Å-resolution cryoelectron tomography map of the hantavirus surface accounted for the complete extramembrane portion of the viral glycoprotein shell and allowed a detailed description of the surface organization of these pleomorphic virions. Our results, which further revealed a built-in mechanism controlling Gc membrane insertion for fusion, pave the way for immunogen design to protect against pathogenic hantaviruses.

PubMed: 32937107
DOI: 10.1016/j.cell.2020.08.023

実験手法

X-RAY DIFFRACTION (2.7 Å)