Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 117, Issue 3, Pages 1438-1446Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1908898117
Keywords
cryoelectron microscopy; mass spectrometry; protein glycosylation; alphacoronavirus; feline infectious peritonitis virus
Categories
Funding
- Academia Sinica Cryo-EM Center [AS-CFII-108-110]
- Ministry of Science and Technology (MOST), Taiwan [MOST 106-2311-B-002-028-MY3, 107-2628-M-001-005-MY3]
- National Taiwan University [108L7842]
- Taiwan Protein Project [AS-KPQ-105-TPP]
- Academia Sinica
Ask authors/readers for more resources
Feline infectious peritonitis virus (FIPV) is an alphacoronavirus that causes a nearly 100% mortality rate without effective treatment. Here we report a 3.3-A 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available