ArticleNature communications2019
Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoprotein.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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Who cites it
91 citing papers in PubMed.
- Cryo-ET of IgG bivalent binding on SARS-CoV-2 provides structural basis for antibody avidity.Nature communications · 2026Article
- Structural Basis of MERS-CoV Receptor Interactions and Antibody Neutralisations.Reviews in medical virology · 2026Review
- Spike conformational and glycan heterogeneity associated with furin cleavage causes incomplete neutralization of SARS-CoV-2.Nature communications · 2025Article
- Article
- Cross-neutralization ability of anti-MERS-CoV monoclonal antibodies against a variety of merbecoviruses.Frontiers in microbiology · 2025Article
- Protein nanoparticle vaccines induce potent neutralizing antibody responses against MERS-CoV.Cell reports · 2024Article
- Structural characterization of human monoclonal antibodies targeting uncommon antigenic sites on spike glycoprotein of SARS-CoV.The Journal of clinical investigation · 2024Article
- Mapping immunodominant sites on the MERS-CoV spike glycoprotein targeted by infection-elicited antibodies in humans.Cell reports · 2024Article
- Structure defining of ultrapotent neutralizing nanobodies against MERS-CoV with novel epitopes on receptor binding domain.PLoS pathogens · 2024Article
- Enhanced potency of an IgM-like nanobody targeting conserved epitope in SARS-CoV-2 spike N-terminal domain.Signal transduction and targeted therapy · 2024Article
- Humoral Immunity across the SARS-CoV-2 Spike after Sputnik V (Gam-COVID-Vac) Vaccination.Antibodies (Basel, Switzerland) · 2024Article
- Mapping immunodominant sites on the MERS-CoV spike glycoprotein targeted by infection-elicited antibodies in humans.bioRxiv : the preprint server for biology · 2024Article
- Protein nanoparticle vaccines induce potent neutralizing antibody responses against MERS-CoV.bioRxiv : the preprint server for biology · 2024Article
- A broadly reactive antibody targeting the N-terminal domain of SARS-CoV-2 spike confers Fc-mediated protection.Cell reports. Medicine · 2023Article
- Article
- Broad-spectrum pan-genus and pan-family virus vaccines.Cell host & microbe · 2023Review
- Broad strategies for neutralizing SARS-CoV-2 and other human coronaviruses with monoclonal antibodies.Science China. Life sciences · 2023Review
- Variants of SARS-CoV-2: Influences on the Vaccines' Effectiveness and Possible Strategies to Overcome Their Consequences.Medicina (Kaunas, Lithuania) · 2023Review
- Towards Quantum-Chemical Level Calculations of SARS-CoV-2 Spike Protein Variants of Concern by First Principles Density Functional Theory.Biomedicines · 2023Review
- Broadly neutralizing and protective nanobodies against SARS-CoV-2 Omicron subvariants BA.1, BA.2, and BA.4/5 and diverse sarbecoviruses.Nature communications · 2022Article
31 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most neutralizing antibodies against Middle East respiratory syndrome coronavirus (MERS-CoV) target the receptor-binding domain (RBD) of the spike glycoprotein and block its binding to the cellular receptor dipeptidyl peptidase 4 (DPP4). The epitopes and mechanisms of mAbs targeting non-RBD regions have not been well characterized yet. Here we report the monoclonal antibody 7D10 that binds to the N-terminal domain (NTD) of the spike glycoprotein and inhibits the cell entry of MERS-CoV with high potency. Structure determination and mutagenesis experiments reveal the epitope and critical residues on the NTD for 7D10 binding and neutralization. Further experiments indicate that the neutralization by 7D10 is not solely dependent on the inhibition of DPP4 binding, but also acts after viral cell attachment, inhibiting the pre-fusion to post-fusion conformational change of the spike. These properties give 7D10 a wide neutralization breadth and help explain its synergistic effects with several RBD-targeting antibodies.
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