Linear Epitope Landscape of SARS-CoV-2 Spike Protein Constructed from 1,051 COVID-19 Patients

Li, Yang; Ma, Ming‐liang; Lei, Qing; Wang, Rui; Lai, Dan‐yun; Hou, Hongyan; Xu, Zhaowei; Zhang, Bo; Chen, Hong; Yu, Caizheng; Xue, Jun‐biao; Zheng, Yun-xiao; Wang, Xue-ning; Jiang, He‐wei; Zhang, Hainan; Qi, Huan; Guo, Shujuan; Zhang, Yandi; Lin, Xiang; Yao, Zongjie; Wu, Jiaoxiang; Sheng, Huiming; Sun, Ziyong; Fan, Xue‐Gong; Tao, Sheng Ce

doi:10.2139/ssrn.3671941

Cited by 16 publications

(27 citation statements)

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“…Significant epitopes were also identified on the cytoplasmic C-terminal end of S protein. These results are highly consistent to a peptide microarray-based study, of which about 4,000 samples were analyzed against a set of 197 peptides that covers the entire S protein (14,15).…”

Section: A Map Of Sars-cov-2 Specific Igg Binding Epitopessupporting

confidence: 82%

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Systematic profiling of SARS-CoV-2 specific IgG epitopes at single amino acid resolution

Jiang

et al. 2020

Preprint

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SARS-CoV-2 specific IgG responses play critical roles for patients to recover from COVID-19, in-depth dissecting of the IgG responses on systems level is of great interest. Herein, we adopted a newly developed high-throughput epitope mapping technology (AbMap), analyzed 55 COVID-19 convalescent sera and 226 antibody samples enriched by specific proteins or peptides from these sera. We revealed three areas that are rich of IgG epitopes, two are on Spike protein but outside of RBD, and one is on Nucleocapsid protein. We identified 29 significant epitopes on Spike protein, from two of these significant epitopes, two critical epitope residues were found, i. e., D936 and P1263, which are highly related to the infectivity of SARS-CoV-2. In summary, we provided the first global map of IgG binding epitopes for SARS-CoV-2 at single amino acid resolution. This map will facilitate the precise development of therapeutic antibodies and vaccines.

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Section: A Map Of Sars-cov-2 Specific Igg Binding Epitopessupporting

confidence: 82%

“…On S protein, RBD domain is presently the central target to develop SARS-CoV-2 antibodies and vaccines (6)(7)(8)(9)(10). Other areas of S protein can also elicit B cell responses and neutralization antibodies (11)(12)(13)(14)(15). Nucleocapsid protein (N protein) is highly abundant and triggers significant IgG response (16)(17)(18).…”

Section: Introductionmentioning

confidence: 99%

Systematic profiling of SARS-CoV-2 specific IgG epitopes at single amino acid resolution

Jiang

et al. 2020

Preprint

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“…We noted that cross-reactive antibodies directed to CC40.8 S2 stem-helix epitope are relatively less frequently elicited in human coronavirus natural infections as compared to strain-specific neutralizing antibody responses (27). However, a few recent studies using more sensitive antibody detection assays have revealed higher prevalence of polyclonal stem-helix region-directed antibodies in COVID-19 donors and their association with reduced disease severity (64)(65)(66). Regardless, the small subset of individuals in our sample cohort that do make cross-reactive Abs, seem to exhibit broad reactivity to human β-coronaviruses, which is promising for pan-coronavirus vaccine strategies.…”

Section: )mentioning

confidence: 74%

A human antibody reveals a conserved site on beta-coronavirus spike proteins and confers protection against SARS-CoV-2 infection

Zhou

Yuan

Song

et al. 2021

Preprint

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We recently described CC40.8 bnAb from a COVID-19 donor that exhibits broad reactivity with human β-CoVs. Here, we show that CC40.8 targets the conserved S2 stem-helix region of the coronavirus spike fusion machinery. We determined a crystal structure of CC40.8 Fab with a SARS-CoV-2 S2 stem-peptide at 1.6 A resolution and found that the peptide adopts a mainly helical structure. Conserved residues in β-CoVs interact with the antibody, thereby providing a molecular basis for its broad reactivity. CC40.8 exhibits in vivo protective efficacy against SARS-CoV-2 challenge in a hamster model with reduction in weight loss and lung viral titers. Furthermore, we noted CC40.8-like bnAbs are relatively rare in human COVID-19 infection and therefore their elicitation may require rational vaccine strategies. Overall, our study describes a new target on CoV spikes for protective antibodies that may facilitate the development of pan-β-CoV vaccines.

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“…Of the in silico SARS-CoV-2 studies that have been reviewed ( Table 1 ), many had also predicted B cell epitopes for potentially eliciting a neutralizing antibody response. Some of these epitope predictions, particularly those made by methods leveraging SARS-CoV data [ 20 , 22 ], have also been observed experimentally [ 35 , [189] , [190] , [191] , [192] , [193] ]. The development of in silico methods to identify B cell epitopes for SARS-CoV-2 is currently an active area of research.…”

Section: Summary and Perspectivesmentioning

confidence: 91%

In silico T cell epitope identification for SARS-CoV-2: Progress and perspectives

Sohail

Ahmed

Quadeer

et al. 2021

Advanced Drug Delivery Reviews

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Linear Epitope Landscape of SARS-CoV-2 Spike Protein Constructed from 1,051 COVID-19 Patients

Cited by 16 publications

References 0 publications

Systematic profiling of SARS-CoV-2 specific IgG epitopes at single amino acid resolution

Systematic profiling of SARS-CoV-2 specific IgG epitopes at single amino acid resolution

A human antibody reveals a conserved site on beta-coronavirus spike proteins and confers protection against SARS-CoV-2 infection

In silico T cell epitope identification for SARS-CoV-2: Progress and perspectives

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