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9BLL

Cryo-EM of RBD(EG5.1)/1301B7 Fab Complex

Summary for 9BLL
Entry DOI10.2210/pdb9bll/pdb
EMDB information44666
Descriptor1301B7 Heavy Chain, 1301B7 Light Chain, Spike glycoprotein, ... (5 entities in total)
Functional Keywordsfab, rbd, complex, protein binding, viral protein-immune system complex, viral protein/immune system
Biological sourceHomo sapiens
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Total number of polymer chains3
Total formula weight163865.83
Authors
Walter, M.R.,Green, T.J. (deposition date: 2024-04-30, release date: 2025-03-12)
Primary citationPiepenbrink, M.S.,Khalil, A.M.,Chang, A.,Mostafa, A.,Basu, M.,Sarkar, S.,Panjwani, S.,Ha, Y.H.,Ma, Y.,Ye, C.,Wang, Q.,Green, T.J.,Kizziah, J.L.,Erdmann, N.B.,Goepfert, P.A.,Liu, L.,Ho, D.D.,Martinez-Sobrido, L.,Walter, M.R.,Kobie, J.J.
Potent neutralization by a RBD antibody with broad specificity for SARS-CoV-2 JN.1 and other variants.
Npj Viruses, 2:55-55, 2024
Cited by
PubMed Abstract: SARS-CoV-2 continues to be a public health burden, driven in-part by its continued antigenic diversification and resulting emergence of new variants. By increasing herd immunity, current vaccines have improved infection outcomes for many. However, prophylactic and treatment interventions that are not compromised by viral evolution of the Spike protein are still needed. Using a differential staining strategy with a rationally designed SARS-CoV-2 Receptor Binding Domain (RBD) - ACE2 fusion protein and a native Omicron RBD protein, we developed a recombinant human monoclonal antibody (hmAb) from a convalescent individual following SARS-CoV-2 Omicron infection. The resulting hmAb, 1301B7 potently neutralized a wide range of SARS-CoV-2 variants including the original Wuhan-1, the more recent Omicron JN.1 strain, and SARS-CoV. 1301B7 contacts the ACE2 binding site of RBD exclusively through its VH1-69 heavy chain. Broad specificity is achieved through 1301B7 binding to many conserved residues of Omicron variants including Y501 and H505. Consistent with its extensive binding epitope, 1301B7 is able to potently diminish viral burden in the upper and lower respiratory tract and protect mice from challenge with Omicron XBB1.5 and Omicron JN.1 viruses. These results suggest 1301B7 has broad potential to prevent or treat clinical SARS-CoV-2 infections and to guide development of RBD-based universal SARS-CoV-2 prophylactic vaccines and therapeutic approaches.
PubMed: 39553825
DOI: 10.1038/s44298-024-00063-z
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.1 Å)
Structure validation

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