ArticleScientific reports2015
Structural basis for the neutralization of MERS-CoV by a human monoclonal antibody MERS-27.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 1 of them a synthesis that pooled it.
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Who cites it
52 citing papers in PubMed, 1 synthesis or guideline pooled it, 70 citations in OpenAlex.
- A systematic review of SARS-CoV-2 vaccine candidates.Signal transduction and targeted therapy · 2020Pooled it
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- Plant Molecular Pharming and Plant-Derived Compounds towards Generation of Vaccines and Therapeutics against Coronaviruses.Vaccines · 2022Review
- Recent Progress in the Discovery and Development of Monoclonal Antibodies against Viral Infections.Biomedicines · 2022Review
- Middle East Respiratory Syndrome coronavirus vaccine development: updating clinical studies using platform technologies.Journal of microbiology (Seoul, Korea) · 2022Review
- The structure of a novel antibody against the spike protein inhibits Middle East respiratory syndrome coronavirus infections.Scientific reports · 2022Article
- Cryoelectron microscopy structures of a human neutralizing antibody bound to MERS-CoV spike glycoprotein.Frontiers in microbiology · 2022Article
- A platform technology for generating subunit vaccines against diverse viral pathogens.Frontiers in immunology · 2022Article
- Potential for Developing Plant-Derived Candidate Vaccines and Biologics against Emerging Coronavirus Infections.Pathogens (Basel, Switzerland) · 2021Review
- Conformational flexibility and structural variability of SARS-CoV2 S protein.Structure (London, England : 1993) · 2021Article
- Computational design and modeling of nanobodies toward SARS-CoV-2 receptor binding domain.Chemical biology & drug design · 2021Article
- Gastrointestinal and renal complications in SARS-CoV-2-infected patients: Role of immune system.Scandinavian journal of immunology · 2021Review
- Therapeutics for COVID-19: from computation to practices-where we are, where we are heading to.Molecular diversity · 2021Review
- Development of Coronavirus Treatments Using Neutralizing Antibodies.Microorganisms · 2021Review
- Role of plasmonics in detection of deadliest viruses: a review.European physical journal plus · 2021Review
- Exploring the multifocal therapeutic approaches in COVID-19: A ray of hope.International immunopharmacology · 2021Review
- Cross-Protection against MERS-CoV by Prime-Boost Vaccination Using Viral Spike DNA and Protein.Journal of virology · 2020Article
- Coronavirus disease 2019 (COVID-19): Immunological approaches and emerging pharmacologic treatments.International immunopharmacology · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The recently reported Middle East respiratory syndrome coronavirus (MERS-CoV) causes severe respiratory illness in humans with an approximately 30% mortality rate. The envelope spike glycoprotein on the surface of MERS-CoV mediates receptor binding, membrane fusion, and viral entry. We previously reported two human monoclonal antibodies that target the receptor binding domain (RBD) of the spike and exhibit strong neutralization activity against live and pesudotyped MERS-CoV infection. Here we determined the crystal structure of MERS-CoV RBD bound to the Fab fragment of MERS-27 antibody at 3.20 Å resolution. The MERS-27 epitope in the RBD overlaps with the binding site of the MERS-CoV receptor DPP4. Further biochemical, viral entry, and neutralization analyses identified two critical residues in the RBD for both MERS-27 recognition and DPP4 binding. One of the residues, Trp535, was found to function as an anchor residue at the binding interface with MERS-27. Upon receptor binding, Trp535 interacts with the N-linked carbohydrate moiety of DPP4. Thus, MERS-27 inhibits MERS-CoV infection by directly blocking both protein-protein and protein-carbohydrate interactions between MERS-CoV RBD and DPP4. These results shed light on the molecular basis of MERS-27 neutralization and will assist in the optimization of MERS-27 as a tool to combat MERS-CoV infection.
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