7C2L

S protein of SARS-CoV-2 in complex bound with 4A8

Summary for 7C2L

• Entry DOI: 10.2210/pdb7c2l/pdb
• EMDB information: 30276
• Related PRD ID: PRD_900017
• Descriptor: Spike glycoprotein, heavy chain of 4A8, light chain of 4A8, ... (6 entities in total)
• Functional Keywords: ace2-b0at1 complex, membrane protein, membrane protein-immune system complex, membrane protein/immune system
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV); More
• Total number of polymer chains: 9
• Total formula weight: 668918.58

Authors

Yan, R.H.,Zhang, Y.Y.,Guo, Y.Y.,Li, Y.N.,Xia, L.,Zhou, Q. (deposition date: 2020-05-08, release date: 2020-07-01, Last modification date: 2024-10-16)

Primary citation

Chi, X.,Yan, R.,Zhang, J.,Zhang, G.,Zhang, Y.,Hao, M.,Zhang, Z.,Fan, P.,Dong, Y.,Yang, Y.,Chen, Z.,Guo, Y.,Zhang, J.,Li, Y.,Song, X.,Chen, Y.,Xia, L.,Fu, L.,Hou, L.,Xu, J.,Yu, C.,Li, J.,Zhou, Q.,Chen, W.
A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2.
Science, 369:650-655, 2020

PubMed Abstract: Developing therapeutics against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) could be guided by the distribution of epitopes, not only on the receptor binding domain (RBD) of the Spike (S) protein but also across the full Spike (S) protein. We isolated and characterized monoclonal antibodies (mAbs) from 10 convalescent COVID-19 patients. Three mAbs showed neutralizing activities against authentic SARS-CoV-2. One mAb, named 4A8, exhibits high neutralization potency against both authentic and pseudotyped SARS-CoV-2 but does not bind the RBD. We defined the epitope of 4A8 as the N-terminal domain (NTD) of the S protein by determining with cryo-eletron microscopy its structure in complex with the S protein to an overall resolution of 3.1 angstroms and local resolution of 3.3 angstroms for the 4A8-NTD interface. This points to the NTD as a promising target for therapeutic mAbs against COVID-19.

PubMed: 32571838
DOI: 10.1126/science.abc6952

Experimental method

ELECTRON MICROSCOPY (3.1 Å)