MERS-CoV spike protein: a key target for antivirals
Open accessAbstract
INTRODUCTION: The continual Middle East respiratory syndrome (MERS) threat highlights the importance of developing effective antiviral therapeutics to prevent and treat MERS coronavirus (MERS-CoV) infection. A surface spike (S) protein guides MERS-CoV entry into host cells by binding to cellular receptor dipeptidyl peptidase-4 (DPP4), followed by fusion between virus and host cell membranes. MERS-CoV S protein represents a key target for developing therapeutics to block viral entry and inhibit membrane fusion. Areas covered: This review illustrates MERS-CoV S protein's structure and function, particularly S1 receptor-binding domain (RBD) and S2 heptad repeat 1 (HR1) as therapeutic targets, and summarizes current advancement on developing anti-MERS-CoV therapeutics, focusing on neutralizing monoclonal antibodies (mAbs) and antiviral peptides. Expert opinion: No anti-MERS-CoV therapeutic is approved for human use. Several S-targeting neutralizing mAbs and peptides have demonstrated efficacy against MERS-CoV infection, providing feasibility for development. Generally, human neutralizing mAbs targeting RBD are more potent than those targeting other regions of S protein. However, emergence of escape mutant viruses and mAb's limitations make it necessary for combining neutralizing mAbs recognizing different neutralizing epitopes and engineering them with improved efficacy and reduced cost. Optimization of the peptide sequences is expected to produce next-generation anti-MERS-CoV peptides with improved potency.
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Most MERS-CoV and SARS-CoV-1 neutralizing antibodies were directed to the Spike protein, in particular its receptor-binding domain.
“most of the MERS-CoV and SARS-CoV-1 neutralizing antibodies were directed to the S protein, in particular to its receptor-binding domain (RBD) [18,19]”
From The dawn of mRNA vaccines: the COVID-19 case (2021) · cites this paper as [18]
The Spike protein mediates viral entry by binding to its cellular receptor, ACE2 for SARS-CoV-1 or DPP4/CD26 for MERS-CoV, and then undergoes structural changes resulting in fusion of viral and host cell membranes.
“This protein mediates viral entry by first binding to its cellular receptor (i.e. angiotensin-converting enzyme 2, ACE2 for SARS-CoV-1 or dipeptidyl peptidase 4, DPP4/CD26 for MERS-CoV). Upon interaction, the S protein undergoes structural changes resulting in the fusion of viral and host cell membranes.”
From The dawn of mRNA vaccines: the COVID-19 case (2021) · cites this paper as [18]
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- Authors
- Du, L., Yang, Y., Zhou, Y., Lu, L., Li, F., & Jiang, S.
- Affiliations
- New York Blood Center (US)
- University of Minnesota (US)
- Beijing Institute of Microbiology and Epidemiology (CN)
- Shanghai Medical College of Fudan University (CN)
- Corresponding author
- Du, Lanying
- Jiang, Shibo
- Venue
- Expert Opinion on Therapeutic Targets
- Publisher
- Informa UK Limited
- Published
- 2016-12-21
- Volume
- 21
- Issue
- 2
- Pages
- 131-143
- ISSN
- 1472-8222 (ISSN-L)
- 1744-7631
- PMC
- PMC5457961
- OpenAlex
- W2560886679
- Cited by
- 301
- References
- 98
- Citations by year
- 2026: 10 · 2025: 6 · 2024: 30 · 2023: 25 · 2022: 28 · 2021: 75 · 2020: 87 · 2019: 27 · 2018: 10 · 2017: 2 · 2016: 1
- FWCI
- 2.05
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Expert Opinion on Therapeutic Targets (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (R01AI089728, R01AI098775, R01AI110700, R21AI109094)
- New York Blood Center (NYB000348)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- MERS-CoV, spike protein, dipeptidyl peptidase IV, receptor binding domain, heptad repeat 1, neutralizing monoclonal antibodies, antiviral peptides, viral entry inhibition, membrane fusion inhibition, antibody combination therapy, peptide optimization
- MeSH terms
- Animals, Antibodies, Monoclonal, Antiviral Agents, Humans, Peptides, Drug Design, Coronavirus Infections, Virus Internalization, Antibodies, Neutralizing, Middle East Respiratory Syndrome Coronavirus
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