5FT2

Sub-tomogram averaging of Lassa virus glycoprotein spike from virus- like particles at pH 5

5FT2 の概要

• エントリーDOI: 10.2210/pdb5ft2/pdb
• EMDBエントリー: 3292
• 分子名称: PRE-GLYCOPROTEIN POLYPROTEIN GP COMPLEX, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: cell adhesion, membrane protein, glycoprotein, receptor binding, membrane fusion
• 由来する生物種: LASSA VIRUS (LASSA MAMMARENAVIRUS, LASV)
• 細胞内の位置: Stable signal peptide: Virion membrane ; Multi-pass membrane protein . Glycoprotein G2: Virion membrane ; Single-pass membrane protein : P08669
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20670.91

構造登録者

Li, S.,Zhaoyang, S.,Pryce, R.,Parsy, M.L.,Fehling, S.K.,Schlie, K.,Siebert, C.A.,Garten, W.,Bowden, T.A.,Strecker, T.,Huiskonen, J.T. (登録日: 2016-01-09, 公開日: 2016-03-02, 最終更新日: 2024-11-20)

主引用文献

Li, S.,Sun, Z.,Pryce, R.,Parsy, M.,Fehling, S.K.,Schlie, K.,Siebert, C.A.,Garten, W.,Bowden, T.A.,Strecker, T.,Huiskonen, J.T.
Acidic Ph-Induced Conformations and Lamp1 Binding of the Lassa Virus Glycoprotein Spike.
Plos Pathog., 12:5418-, 2016

PubMed Abstract: Lassa virus is an enveloped, bi-segmented RNA virus and the most prevalent and fatal of all Old World arenaviruses. Virus entry into the host cell is mediated by a tripartite surface spike complex, which is composed of two viral glycoprotein subunits, GP1 and GP2, and the stable signal peptide. Of these, GP1 binds to cellular receptors and GP2 catalyzes fusion between the viral envelope and the host cell membrane during endocytosis. The molecular structure of the spike and conformational rearrangements induced by low pH, prior to fusion, remain poorly understood. Here, we analyzed the three-dimensional ultrastructure of Lassa virus using electron cryotomography. Sub-tomogram averaging yielded a structure of the glycoprotein spike at 14-Å resolution. The spikes are trimeric, cover the virion envelope, and connect to the underlying matrix. Structural changes to the spike, following acidification, support a viral entry mechanism dependent on binding to the lysosome-resident receptor LAMP1 and further dissociation of the membrane-distal GP1 subunits.

PubMed: 26849049
DOI: 10.1371/JOURNAL.PPAT.1005418

実験手法

ELECTRON MICROSCOPY (16.4 Å)