A SARS-CoV-2 antibody curbs viral nucleocapsid protein-induced complement hyperactivation.
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.
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
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