Identification of human neutralizing antibodies against MERS-CoV and their role in virus adaptive evolution
Open accessAbstract
The newly emerging Middle East Respiratory Syndrome coronavirus (MERS-CoV) causes a Severe Acute Respiratory Syndrome-like disease with ∼43% mortality. Given the recent detection of virus in dromedary camels, zoonotic transfer of MERS-CoV to humans is suspected. In addition, little is known about the role of human neutralizing Ab (nAb) pressure as a driving force in MERS-CoV adaptive evolution. Here, we used a well-characterized nonimmune human Ab-phage library and a panning strategy with proteoliposomes and cells to identify seven human nAbs against the receptor-binding domain (RBD) of the MERS-CoV Spike protein. These nAbs bind to three different epitopes in the RBD and human dipeptidyl peptidase 4 (hDPP4) interface with subnanomolar/nanomolar binding affinities and block the binding of MERS-CoV Spike protein with its hDPP4 receptor. Escape mutant assays identified five amino acid residues that are critical for neutralization escape. Despite the close proximity of the three epitopes on the RBD interface, escape from one epitope did not have a major impact on neutralization with Abs directed to a different epitope. Importantly, the majority of escape mutations had negative impacts on hDPP4 receptor binding and viral fitness. To our knowledge, these results provide the first report on human nAbs against MERS-CoV that may contribute to MERS-CoV clearance and evolution. Moreover, in the absence of a licensed vaccine or antiviral for MERS, this panel of nAbs offers the possibility of developing human mAb-based immunotherapy, especially for health-care workers.
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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 [19]
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- Authors
- Tang, X.-C., Agnihothram, S. S., Jiao, Y., Stanhope, J., Graham, R. L., Peterson, E. C., Avnir, Y., Tallarico, A. S. C., Sheehan, J., Zhu, Q., Baric, R. S., & Marasco, W. A.
- Affiliations
- Harvard University (US)
- Departments of bMicrobiology and Immunology and
- Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02215; and
- University of North Carolina at Chapel Hill (US)
- Corresponding author
- Tang, Xian-Chun
- Agnihothram, Sudhakar S.
- Graham, Rachel L.
- Baric, Ralph S.
- Marasco, Wayne A.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2014-04-28
- Volume
- 111
- Issue
- 19
- Pages
- E2018-26
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC4024880
- OpenAlex
- W2170239105
- Cited by
- 232
- References
- 62
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 9 · 2023: 7 · 2022: 14 · 2021: 34 · 2020: 41 · 2019: 17 · 2018: 12 · 2017: 19 · 2016: 36 · 2015: 27 · 2014: 7
- FWCI
- 20.86
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
- UNC Libraries
- Funders
- Public Health England
- National Institutes of Health
- Advanced Research Projects Agency
- National Institute of Allergy and Infectious Diseases (R01AI085524)
- 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, neutralizing antibodies, spike protein receptor-binding domain, antibody escape mutations, antibody phage display, epitope mapping, zoonotic transmission, Camelus dromedarius, monoclonal antibody therapy, viral fitness
- MeSH terms
- Amino Acid Sequence, Animals, Antibodies, Viral, Antiviral Agents, Biological Evolution, Humans, Immunoglobulin G, Molecular Sequence Data, Phylogeny, Viral Vaccines, Zoonoses, Coronavirus, Coronavirus Infections, Dipeptidyl Peptidase 4, Communicable Diseases, Emerging, Antibodies, Neutralizing, HEK293 Cells, Spike Glycoprotein, Coronavirus
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Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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