7CR5
Complex structure of a human monoclonal antibody with SARS-CoV-2 nucleocapsid protein NTD
Summary for 7CR5
Entry DOI | 10.2210/pdb7cr5/pdb |
Descriptor | Nucleoprotein, monoclonal antibody chain H, monoclonal antibody chain L, ... (5 entities in total) |
Functional Keywords | human monoclonal antibody, sars-cov-2, nucleocapsid protein, complex, viral protein, viral protein-immune system complex, viral protein/immune system |
Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) More |
Total number of polymer chains | 3 |
Total formula weight | 62038.24 |
Authors | |
Primary citation | Kang, S.,Yang, M.,He, S.,Wang, Y.,Chen, X.,Chen, Y.Q.,Hong, Z.,Liu, J.,Jiang, G.,Chen, Q.,Zhou, Z.,Zhou, Z.,Huang, Z.,Huang, X.,He, H.,Zheng, W.,Liao, H.X.,Xiao, F.,Shan, H.,Chen, S. A SARS-CoV-2 antibody curbs viral nucleocapsid protein-induced complement hyperactivation. Nat Commun, 12:2697-2697, 2021 Cited by PubMed Abstract: Although human antibodies elicited by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) nucleocapsid (N) protein are profoundly boosted upon infection, little is known about the function of N-reactive antibodies. Herein, we isolate and profile a panel of 32 N protein-specific monoclonal antibodies (mAbs) from a quick recovery coronavirus disease-19 (COVID-19) convalescent patient who has dominant antibody responses to the SARS-CoV-2 N protein rather than to the SARS-CoV-2 spike (S) protein. The complex structure of the N protein RNA binding domain with the highest binding affinity mAb (nCoV396) reveals changes in the epitopes and antigen's allosteric regulation. Functionally, a virus-free complement hyperactivation analysis demonstrates that nCoV396 specifically compromises the N protein-induced complement hyperactivation, which is a risk factor for the morbidity and mortality of COVID-19 patients, thus laying the foundation for the identification of functional anti-N protein mAbs. PubMed: 33976229DOI: 10.1038/s41467-021-23036-9 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.08 Å) |
Structure validation
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