6JX7
Cryo-EM structure of spike protein of feline infectious peritonitis virus strain UU4
Summary for 6JX7
| Entry DOI | 10.2210/pdb6jx7/pdb |
| EMDB information | 9891 |
| Descriptor | Feline Infectious Peritonitis Virus Spike Protein, alpha-D-mannopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total) |
| Functional Keywords | cov spike protein, viral protein |
| Biological source | Feline infectious peritonitis virus |
| Total number of polymer chains | 3 |
| Total formula weight | 534059.71 |
| Authors | Hsu, S.T.D.,Yang, T.J.,Ko, T.P.,Draczkowski, P. (deposition date: 2019-04-22, release date: 2020-01-15, Last modification date: 2024-11-06) |
| Primary citation | Yang, T.J.,Chang, Y.C.,Ko, T.P.,Draczkowski, P.,Chien, Y.C.,Chang, Y.C.,Wu, K.P.,Khoo, K.H.,Chang, H.W.,Hsu, S.D. Cryo-EM analysis of a feline coronavirus spike protein reveals a unique structure and camouflaging glycans. Proc.Natl.Acad.Sci.USA, 117:1438-1446, 2020 Cited by PubMed 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 Nglycans 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. PubMed: 31900356DOI: 10.1073/pnas.1908898117 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.31 Å) |
Structure validation
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