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Cryo-EM analysis of a feline coronavirus spike protein reveals a unique structure and camouflaging glycans.
Yang, Tzu-Jing; Chang, Yen-Chen; Ko, Tzu-Ping; Draczkowski, Piotr; Chien, Yu-Chun; Chang, Yuan-Chih; Wu, Kuen-Phon; Khoo, Kay-Hooi; Chang, Hui-Wen; Hsu, Shang-Te Danny.
  • Yang TJ; Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
  • Chang YC; Institute of Biochemical Sciences, National Taiwan University, Taipei 10617, Taiwan.
  • Ko TP; Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
  • Draczkowski P; Graduate Institute of Molecular and Comparative Pathobiology, School of Veterinary Medicine, National Taiwan University, Taipei 10617, Taiwan.
  • Chien YC; Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
  • Chang YC; Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
  • Wu KP; Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
  • Khoo KH; Institute of Biochemical Sciences, National Taiwan University, Taipei 10617, Taiwan.
  • Chang HW; Institute of Cellular and Organismic Biology, Academia Sinica, Taipei 11529, Taiwan.
  • Hsu SD; Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
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.
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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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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