Cryo-EM analysis of a feline coronavirus spike protein reveals a unique structure and camouflaging glycans.
Proc Natl Acad Sci U S A
; 117(3): 1438-1446, 2020 01 21.
Article
in English
| MEDLINE | ID: covidwho-833187
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 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.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Coronavirus, Feline
/
Spike Glycoprotein, Coronavirus
Limits:
Humans
Language:
English
Journal:
Proc Natl Acad Sci U S A
Year:
2020
Document Type:
Article
Affiliation country:
Pnas.1908898117
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