7WWM
S protein of Delta variant in complex with ZWC6
Summary for 7WWM
Entry DOI | 10.2210/pdb7wwm/pdb |
EMDB information | 32871 |
Descriptor | Spike glycoprotein, heavy chain of ZWC6, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
Functional Keywords | sars-cov-2, viral protein |
Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2) More |
Total number of polymer chains | 9 |
Total formula weight | 514492.93 |
Authors | Guo, Y.Y.,Zhang, Y.Y.,Zhou, Q. (deposition date: 2022-02-13, release date: 2022-06-01, Last modification date: 2024-10-16) |
Primary citation | Chi, X.,Guo, Y.,Zhang, G.,Sun, H.,Zhang, J.,Li, M.,Chen, Z.,Han, J.,Zhang, Y.,Zhang, X.,Fan, P.,Zhang, Z.,Wang, B.,Zai, X.,Han, X.,Hao, M.,Fang, T.,Xu, J.,Wu, S.,Chen, Y.,Fang, Y.,Dong, Y.,Sun, B.,Zhang, J.,Li, J.,Zhao, G.,Yu, C.,Zhou, Q.,Chen, W. Broadly neutralizing antibodies against Omicron-included SARS-CoV-2 variants induced by vaccination. Signal Transduct Target Ther, 7:139-139, 2022 Cited by PubMed Abstract: The SARS-CoV-2 Omicron variant shows substantial resistance to neutralization by infection- and vaccination-induced antibodies, highlighting the demands for research on the continuing discovery of broadly neutralizing antibodies (bnAbs). Here, we developed a panel of bnAbs against Omicron and other variants of concern (VOCs) elicited by vaccination of adenovirus-vectored COVID-19 vaccine (Ad5-nCoV). We also investigated the human longitudinal antibody responses following vaccination and demonstrated how the bnAbs evolved over time. A monoclonal antibody (mAb), named ZWD12, exhibited potent and broad neutralization against SARS-CoV-2 variants Alpha, Beta, Gamma, Kappa, Delta, and Omicron by blocking the spike protein binding to the angiotensin-converting enzyme 2 (ACE2) and provided complete protection in the challenged prophylactic and therapeutic K18-hACE2 transgenic mouse model. We defined the ZWD12 epitope by determining its structure in complex with the spike (S) protein via cryo-electron microscopy. This study affords the potential to develop broadly therapeutic mAb drugs and suggests that the RBD epitope bound by ZWD12 is a rational target for the design of a broad spectrum of vaccines. PubMed: 35478188DOI: 10.1038/s41392-022-00987-z PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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