ArticleCell reports2018
Structural Definition of a Unique Neutralization Epitope on the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein.
Article in Cell reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- The role of DPP4 in viral infections: from receptor biology to antiviral target.Archives of virology · 2026Review
- Article
- Cross-neutralization ability of anti-MERS-CoV monoclonal antibodies against a variety of merbecoviruses.Frontiers in microbiology · 2025Article
- 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
- Mapping immunodominant sites on the MERS-CoV spike glycoprotein targeted by infection-elicited antibodies in humans.bioRxiv : the preprint server for biology · 2024Article
- Article
- From Cell to Symptoms: The Role of SARS-CoV-2 Cytopathic Effects in the Pathogenesis of COVID-19 and Long COVID.International journal of molecular sciences · 2023Review
- Variants of SARS-CoV-2: Influences on the Vaccines' Effectiveness and Possible Strategies to Overcome Their Consequences.Medicina (Kaunas, Lithuania) · 2023Review
- Robust antiviral activity of commonly prescribed antidepressants against emerging coronaviruses: in vitro and in silico drug repurposing studies.Scientific reports · 2022Article
- Functional reconstitution of the MERS CoV receptor binding motif.Molecular immunology · 2022Article
- Advances in mRNA and other vaccines against MERS-CoV.Translational research : the journal of laboratory and clinical medicine · 2022Review
- The structure of a novel antibody against the spike protein inhibits Middle East respiratory syndrome coronavirus infections.Scientific reports · 2022Article
- Structural Characterization of a Neutralizing Nanobody With Broad Activity Against SARS-CoV-2 Variants.Frontiers in microbiology · 2022Article
- Cryoelectron microscopy structures of a human neutralizing antibody bound to MERS-CoV spike glycoprotein.Frontiers in microbiology · 2022Article
- Identification of potent human neutralizing antibodies against SARS-CoV-2 implications for development of therapeutics and prophylactics.Nature communications · 2021Article
- Computational design and modeling of nanobodies toward SARS-CoV-2 receptor binding domain.Chemical biology & drug design · 2021Article
- The significance of bioengineered nanoplatforms against SARS-CoV-2: From detection to genome editing.Life sciences · 2021Review
- Potent germline-like monoclonal antibodies: rapid identification of promising candidates for antibody-based antiviral therapy.Antibody therapeutics · 2021Article
- SARS-CoV-2 vaccine research and development: Conventional vaccines and biomimetic nanotechnology strategies.Asian journal of pharmaceutical sciences · 2021Review
Corrections and comments
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Authors and funding
15 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The major mechanism of antibody-mediated neutralization of the Middle East respiratory syndrome coronavirus (MERS-CoV) involves competition with the cellular receptor dipeptidyl peptidase 4 (DPP4) for binding to the receptor-binding domain (RBD) of the spike (S) glycoprotein. Here, we report a unique epitope and unusual neutralizing mechanism of the isolated human antibody MERS-4. Structurally, MERS-4 approached the RBD from the outside of the RBD-DPP4 binding interface. Such binding resulted in the folding of the β5-β6 loop toward a shallow groove on the RBD interface critical for accommodating DPP4. The key residues for binding are identified through site-directed mutagenesis. Structural modeling revealed that MERS-4 binds to RBD only in the "up" position in the S trimer. Furthermore, MERS-4 demonstrated synergy with several reported antibodies. These results indicate that MERS-4 neutralizes MERS-CoV by indirect rather than direct competition with DPP4. This mechanism provides a valuable addition for the combined use of antibodies against MERS-CoV infection.
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