7Y6D
Cryo-EM structure of SARS-CoV-2 Delta variant spike proteins on intact virions: 3 Closed RBD
Summary for 7Y6D
Entry DOI | 10.2210/pdb7y6d/pdb |
EMDB information | 33205 |
Descriptor | Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
Functional Keywords | trimer, viral protein |
Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV,SARS-CoV-2) |
Total number of polymer chains | 3 |
Total formula weight | 438120.04 |
Authors | |
Primary citation | Song, Y.,Yao, H.,Wu, N.,Xu, J.,Zhang, Z.,Peng, C.,Li, S.,Kong, W.,Chen, Y.,Zhu, M.,Wang, J.,Shi, D.,Zhao, C.,Lu, X.,Echavarria Galindo, M.,Li, S. In situ architecture and membrane fusion of SARS-CoV-2 Delta variant. Proc.Natl.Acad.Sci.USA, 120:e2213332120-e2213332120, 2023 Cited by PubMed Abstract: Among the current five Variants of Concern, infections caused by SARS-CoV-2 B.1.617.2 (Delta) variant are often associated with the greatest severity. Despite recent advances on the molecular basis of elevated pathogenicity using recombinant proteins, the architecture of intact Delta virions remains veiled. Moreover, pieces of molecular evidence for the detailed mechanism of S-mediated membrane fusion are missing. Here, we showed the pleomorphic nature of Delta virions from electron beam inactivated samples and reported the in situ structure and distribution of S on the authentic Delta variant. We also captured the virus-virus fusion events, which provided pieces of structural evidence for Delta's attenuated dependency on cellular factors for fusion activation, and proposed a model of S-mediated membrane fusion. Besides, site-specific glycan analysis revealed increased oligomannose-type glycosylation of native Delta S than that of the WT S. Together, these results disclose distinctive factors of Delta being the most virulent SARS-CoV-2 variant. PubMed: 37094167DOI: 10.1073/pnas.2213332120 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.39 Å) |
Structure validation
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