6JX7

Cryo-EM structure of spike protein of feline infectious peritonitis virus strain UU4

6JX7 の概要

• エントリーDOI: 10.2210/pdb6jx7/pdb
• EMDBエントリー: 9891
• 分子名称: Feline Infectious Peritonitis Virus Spike Protein, alpha-D-mannopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total)
• 機能のキーワード: cov spike protein, viral protein
• 由来する生物種: Feline infectious peritonitis virus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 534059.71

構造登録者

Hsu, S.T.D.,Yang, T.J.,Ko, T.P.,Draczkowski, P. (登録日: 2019-04-22, 公開日: 2020-01-15, 最終更新日: 2024-11-06)

主引用文献

Yang, T.J.,Chang, Y.C.,Ko, T.P.,Draczkowski, P.,Chien, Y.C.,Chang, Y.C.,Wu, K.P.,Khoo, K.H.,Chang, H.W.,Hsu, S.D.
Cryo-EM analysis of a feline coronavirus spike protein reveals a unique structure and camouflaging glycans.
Proc.Natl.Acad.Sci.USA, 117:1438-1446, 2020

PubMed Abstract: Feline infectious peritonitis virus (FIPV) is an alphacoronavirus that causes a nearly 100% mortality rate without effective treatment. Here we report a 3.3-Å cryoelectron microscopy (cryo-EM) structure of the serotype I FIPV spike (S) protein, which is responsible for host recognition and viral entry. Mass spectrometry provided site-specific compositions of densely distributed high-mannose and complex-type Nglycans that account for 1/4 of the total molecular mass; most of the N-glycans could be visualized by cryo-EM. Specifically, the N-glycans that wedge between 2 galectin-like domains within the S1 subunit of FIPV S protein result in a unique propeller-like conformation, underscoring the importance of glycosylation in maintaining protein structures. The cleavage site within the S2 subunit responsible for activation also showed distinct structural features and glycosylation. These structural insights provide a blueprint for a better molecular understanding of the pathogenesis of FIP.

PubMed: 31900356
DOI: 10.1073/pnas.1908898117

実験手法

ELECTRON MICROSCOPY (3.31 Å)