Please use this identifier to cite or link to this item: https://covid-19.conacyt.mx/jspui/handle/1000/1521
Cryo-EM analysis of a feline coronavirus spike protein reveals a unique structure and camouflaging glycans
Yang, T
Chang, Y
Ko, T
Draczkowski, P
Chien, Y
Chang, Y
Wu, K
Khoo, K
Chang, H
Danny Hsu, S
Acceso Abierto
Atribución-NoComercial-SinDerivadas
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 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 better molecular understanding of the pathogenesis of FIP.
Proceedings of the National Academy of Sciences of the United States of America
2020
Preimpreso
https://coronavirus.1science.com/item/05e598ca76f07599810563c65bc1d304ddd3ef86
Inglés
VIRUS RESPIRATORIOS
Appears in Collections:Artículos científicos

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