๐ Cryo-EM analysis of a feline coronavirus spike protein reveals a unique structure and camouflaging glycans
Feline infectious peritonitis virus (FIPV) is an alphacoronavirus that causes a nearly 100% mortality rate without effective treatment. Here we report a 3.3-ร
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 N-glycans 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 bettermolecular understanding of the pathogenesis of FIP.
keywords
๐ cleavage site (85)
๐ infectious peritonitis (181)
๐ peritonitis virus (67)
๐ viral entry (91)
๐ electron microscopy (149)
author
๐ค Yang, Tzu Jing
๐ค Chang, Yen Chen
๐ค Ko, Tzu Ping
๐ค Draczkowski, Piotr
๐ค Chien, Yu Chun
๐ค Chang, Yuan Chih
๐ค Wu, Kuen Phon
๐ค Khoo, Kay Hooi
๐ค Chang, Hui Wen
๐ค Danny Hsu, Shang Te
year
โฐ 2020
issn
๐ 10916490 00278424
volume
117
number
3
page
1438-1446
citedbycount
0
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