7FJO
Cryo-EM structure of South African (B.1.351) SARS-CoV-2 spike glycoprotein in complex with three T6 Fab
Summary for 7FJO
Entry DOI | 10.2210/pdb7fjo/pdb |
EMDB information | 31625 |
Descriptor | T6 heavy chain, T6 light chain, Spike glycoprotein, ... (4 entities in total) |
Functional Keywords | sars-cov-2, spike, antibody, viral protein, immune system-viral protein complex, immune system/viral protein |
Biological source | Homo sapiens More |
Total number of polymer chains | 9 |
Total formula weight | 572109.18 |
Authors | |
Primary citation | Liang, Q.,Wang, Y.,Zhang, S.,Sun, J.,Sun, W.,Li, J.,Liu, Y.,Li, M.,Cheng, L.,Jiang, Y.,Wang, R.,Zhang, R.,Yang, Z.,Ren, Y.,Chen, P.,Gao, P.,Yan, H.,Zhang, Z.,Zhang, Q.,Shi, X.,Wang, J.,Liu, W.,Wang, X.,Ying, B.,Zhao, J.,Qi, H.,Zhang, L. RBD trimer mRNA vaccine elicits broad and protective immune responses against SARS-CoV-2 variants. Iscience, 25:104043-104043, 2022 Cited by PubMed Abstract: With the rapid emergence and spread of SARS-CoV-2 variants, development of vaccines with broad and potent protectivity has become a global priority. Here, we designed a lipid nanoparticle-encapsulated, nucleoside-unmodified mRNA (mRNA-LNP) vaccine encoding the trimerized receptor-binding domain (RBD trimer) and showed its robust capability in inducing broad and protective immune responses against wild-type and major variants of concern (VOCs) in the mouse model of SARS-CoV-2 infection. The protectivity was correlated with RBD-specific B cell responses especially the long-lived plasma B cells in bone marrow, strong ability in triggering BCR clustering, and downstream signaling. Monoclonal antibodies isolated from vaccinated animals demonstrated broad and potent neutralizing activity against VOCs tested. Structure analysis of one representative antibody identified a novel epitope with a high degree of conservation among different variants. Collectively, these results demonstrate that the RBD trimer mRNA vaccine serves as a promising vaccine candidate against SARS-CoV-2 variants and beyond. PubMed: 35291264DOI: 10.1016/j.isci.2022.104043 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.34 Å) |
Structure validation
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