tetano
Editor, Senior Moderator
Nat Commun
. 2021 May 11;12(1):2697.
doi: 10.1038/s41467-021-23036-9.
A SARS-CoV-2 antibody curbs viral nucleocapsid protein-induced complement hyperactivation
Sisi Kang[SUP] #[/SUP][SUP] 1 [/SUP], Mei Yang[SUP] #[/SUP][SUP] 1 [/SUP], Suhua He[SUP] #[/SUP][SUP] 1 [/SUP], Yueming Wang[SUP] #[/SUP][SUP] 2 3 [/SUP], Xiaoxue Chen[SUP] 1 [/SUP], Yao-Qing Chen[SUP] 4 [/SUP], Zhongsi Hong[SUP] 5 [/SUP], Jing Liu[SUP] 6 [/SUP], Guanmin Jiang[SUP] 7 [/SUP], Qiuyue Chen[SUP] 1 [/SUP], Ziliang Zhou[SUP] 1 [/SUP], Zhechong Zhou[SUP] 1 [/SUP], Zhaoxia Huang[SUP] 1 [/SUP], Xi Huang[SUP] 8 [/SUP], Huanhuan He[SUP] 1 [/SUP], Weihong Zheng[SUP] 2 3 [/SUP], Hua-Xin Liao[SUP] 9 10 [/SUP], Fei Xiao[SUP] 11 12 [/SUP], Hong Shan[SUP] 13 14 [/SUP], Shoudeng Chen[SUP] 15 [/SUP]
Affiliations
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.
. 2021 May 11;12(1):2697.
doi: 10.1038/s41467-021-23036-9.
A SARS-CoV-2 antibody curbs viral nucleocapsid protein-induced complement hyperactivation
Sisi Kang[SUP] #[/SUP][SUP] 1 [/SUP], Mei Yang[SUP] #[/SUP][SUP] 1 [/SUP], Suhua He[SUP] #[/SUP][SUP] 1 [/SUP], Yueming Wang[SUP] #[/SUP][SUP] 2 3 [/SUP], Xiaoxue Chen[SUP] 1 [/SUP], Yao-Qing Chen[SUP] 4 [/SUP], Zhongsi Hong[SUP] 5 [/SUP], Jing Liu[SUP] 6 [/SUP], Guanmin Jiang[SUP] 7 [/SUP], Qiuyue Chen[SUP] 1 [/SUP], Ziliang Zhou[SUP] 1 [/SUP], Zhechong Zhou[SUP] 1 [/SUP], Zhaoxia Huang[SUP] 1 [/SUP], Xi Huang[SUP] 8 [/SUP], Huanhuan He[SUP] 1 [/SUP], Weihong Zheng[SUP] 2 3 [/SUP], Hua-Xin Liao[SUP] 9 10 [/SUP], Fei Xiao[SUP] 11 12 [/SUP], Hong Shan[SUP] 13 14 [/SUP], Shoudeng Chen[SUP] 15 [/SUP]
Affiliations
- PMID: 33976229
- DOI: 10.1038/s41467-021-23036-9
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.