tetano
Editor, Senior Moderator
Immunity
. 2023 Oct 27:S1074-7613(23)00447-8.
doi: 10.1016/j.immuni.2023.10.007. Online ahead of print. Dissecting the intricacies of human antibody responses to SARS-CoV-1 and SARS-CoV-2 infection
Ruoke Wang[SUP] 1 [/SUP], Yang Han[SUP] 2 [/SUP], Rui Zhang[SUP] 3 [/SUP], Jiayi Zhu[SUP] 4 [/SUP], Xuanyu Nan[SUP] 4 [/SUP], Yaping Liu[SUP] 3 [/SUP], Ziqing Yang[SUP] 3 [/SUP], Bini Zhou[SUP] 5 [/SUP], Jinfang Yu[SUP] 6 [/SUP], Zichun Lin[SUP] 6 [/SUP], Jinqian Li[SUP] 3 [/SUP], Peng Chen[SUP] 3 [/SUP], Yangjunqi Wang[SUP] 4 [/SUP], Yujie Li[SUP] 5 [/SUP], Dongsheng Liu[SUP] 5 [/SUP], Xuanling Shi[SUP] 3 [/SUP], Xinquan Wang[SUP] 6 [/SUP], Qi Zhang[SUP] 3 [/SUP], Yuhe R Yang[SUP] 7 [/SUP], Taisheng Li[SUP] 8 [/SUP], Linqi Zhang[SUP] 9 [/SUP]
Affiliations
The 2003 severe acute respiratory syndrome coronavirus (SARS-CoV-1) causes more severe disease than SARS-CoV-2, which is responsible for COVID-19. However, our understanding of antibody response to SARS-CoV-1 infection remains incomplete. Herein, we studied the antibody responses in 25 SARS-CoV-1 convalescent patients. Plasma neutralization was higher and lasted longer in SARS-CoV-1 patients than in severe SARS-CoV-2 patients. Among 77 monoclonal antibodies (mAbs) isolated, 60 targeted the receptor-binding domain (RBD) and formed 7 groups (RBD-1 to RBD-7) based on their distinct binding and structural profiles. Notably, RBD-7 antibodies bound to a unique RBD region interfaced with the N-terminal domain of the neighboring protomer (NTD proximal) and were more prevalent in SARS-CoV-1 patients. Broadly neutralizing antibodies for SARS-CoV-1, SARS-CoV-2, and bat and pangolin coronaviruses were also identified. These results provide further insights into the antibody response to SARS-CoV-1 and inform the design of more effective strategies against diverse human and animal coronaviruses.
Keywords: RBD antibody; SARS-CoV-1; SARS-CoV-2; antibody grouping; antibody response; cross reactivity; cryo-EM structure; epitope mapping; monoclonal antibody; neutralizing antibodies.
. 2023 Oct 27:S1074-7613(23)00447-8.
doi: 10.1016/j.immuni.2023.10.007. Online ahead of print. Dissecting the intricacies of human antibody responses to SARS-CoV-1 and SARS-CoV-2 infection
Ruoke Wang[SUP] 1 [/SUP], Yang Han[SUP] 2 [/SUP], Rui Zhang[SUP] 3 [/SUP], Jiayi Zhu[SUP] 4 [/SUP], Xuanyu Nan[SUP] 4 [/SUP], Yaping Liu[SUP] 3 [/SUP], Ziqing Yang[SUP] 3 [/SUP], Bini Zhou[SUP] 5 [/SUP], Jinfang Yu[SUP] 6 [/SUP], Zichun Lin[SUP] 6 [/SUP], Jinqian Li[SUP] 3 [/SUP], Peng Chen[SUP] 3 [/SUP], Yangjunqi Wang[SUP] 4 [/SUP], Yujie Li[SUP] 5 [/SUP], Dongsheng Liu[SUP] 5 [/SUP], Xuanling Shi[SUP] 3 [/SUP], Xinquan Wang[SUP] 6 [/SUP], Qi Zhang[SUP] 3 [/SUP], Yuhe R Yang[SUP] 7 [/SUP], Taisheng Li[SUP] 8 [/SUP], Linqi Zhang[SUP] 9 [/SUP]
Affiliations
- PMID: 37924813
- DOI: 10.1016/j.immuni.2023.10.007
The 2003 severe acute respiratory syndrome coronavirus (SARS-CoV-1) causes more severe disease than SARS-CoV-2, which is responsible for COVID-19. However, our understanding of antibody response to SARS-CoV-1 infection remains incomplete. Herein, we studied the antibody responses in 25 SARS-CoV-1 convalescent patients. Plasma neutralization was higher and lasted longer in SARS-CoV-1 patients than in severe SARS-CoV-2 patients. Among 77 monoclonal antibodies (mAbs) isolated, 60 targeted the receptor-binding domain (RBD) and formed 7 groups (RBD-1 to RBD-7) based on their distinct binding and structural profiles. Notably, RBD-7 antibodies bound to a unique RBD region interfaced with the N-terminal domain of the neighboring protomer (NTD proximal) and were more prevalent in SARS-CoV-1 patients. Broadly neutralizing antibodies for SARS-CoV-1, SARS-CoV-2, and bat and pangolin coronaviruses were also identified. These results provide further insights into the antibody response to SARS-CoV-1 and inform the design of more effective strategies against diverse human and animal coronaviruses.
Keywords: RBD antibody; SARS-CoV-1; SARS-CoV-2; antibody grouping; antibody response; cross reactivity; cryo-EM structure; epitope mapping; monoclonal antibody; neutralizing antibodies.