Structural Definition of a Neutralization-sensitive Epitope on the MERS-CoV S1-NTD
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Middle East respiratory syndrome coronavirus (MERS-CoV) emerged into the human population in 2012 and has caused substantial morbidity and mortality. Potently neutralizing antibodies targeting the receptor-binding domain (RBD) on MERS-CoV spike (S) protein have been characterized, but much less is known about antibodies targeting non-RBD epitopes. Here, we report the structural and functional characterization of G2, a neutralizing antibody targeting the MERS-CoV S1 N-terminal domain (S1-NTD). Structures of G2 alone and in complex with the MERS-CoV S1-NTD define a site of vulnerability comprising two loops, each of which contain a residue mutated in G2-escape variants. Cell-surface binding studies and in vitro competition experiments demonstrate that G2 strongly disrupts the attachment of MERS-CoV S to its receptor, dipeptidyl peptidase-4 (DPP4), with the inhibition requiring the native trimeric S conformation. These results advance our understanding of antibody-mediated neutralization of coronaviruses and should facilitate the development of immunotherapeutics and vaccines against MERS-CoV.
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S-2P conformational stability translates into greater immunogenicity, based on preservation of neutralization-sensitive epitopes and improved protein expression.
“Moreover, S-2P conformational stability translates into greater immunogenicity,27-29 based on preservation of neutralization-sensitive epitopes at the apex of the prefusion molecule, as shown for respiratory syncytial virus F glycoprotein,30 and improved protein expression,27 which is particularly advantageous for gene-based antigen delivery.”
From An mRNA Vaccine against SARS-CoV-2 — Preliminary Report (2020) · cites this paper as [29]
The Methods describe S-2P as a stabilized MERS-CoV spike protein, and the Discussion says the S1-NTD is immunogenic. Neither passage reports that S-2P’s conformational stability increases immunogenicity; a search for an S-2P immunogenicity comparison and improved expression found no such result in our copy. The citing sentence attaches the preservation-of-epitopes and expression explanations to other citations. (LLM, conf=0.74)
Experimental — accuracy not yet measuredPolyclonal antibodies against multiple non-RBD spike epitopes might block viral attachment, add neutralizing activity, or prevent post-attachment fusion.
“A polyclonal antibody against multiple epitopes of the S protein beyond the RBD might, for example, inhibit viral attachment156–160, provide additional neutralizing activity161 and/or prevent post-attachment fusion162.”
From Immunological mechanisms of vaccine-induced protection against COVID-19 in humans (2021) · cites this paper as [157]
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Brouwer, P. J. M., Caniels, T. G., van der Straten, K., Snitselaar, J. L., Aldon, Y., Bangaru, S., Torres, J. L., Okba, N. M. A., Claireaux, M., Kerster, G., et al. (2020) · Science · doi:10.1126/science.abc5902 · Cited by 1,140 · see citing works
Self-citationPotently neutralizing and protective human antibodies against SARS-CoV-2
Zost, S. J., Gilchuk, P., Case, J. B., Binshtein, E., Chen, R. E., Nkolola, J. P., Schäfer, A., Reidy, J. X., Trivette, A., Nargi, R. S., et al. (2020) · Nature · doi:10.1038/s41586-020-2548-6 · Cited by 1,041 · see citing works
Evaluation of the mRNA-1273 Vaccine against SARS-CoV-2 in Nonhuman Primates
Corbett, K. S., Flynn, B., Foulds, K. E., Francica, J. R., Boyoglu-Barnum, S., Werner, A. P., Flach, B., O’Connell, S., Bock, K. W., Minai, M., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2024671 · Cited by 1,066 · see citing works
Self-citationN-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2
McCallum, M., De Marco, A., Lempp, F. A., Tortorici, M. A., Pinto, D., Walls, A. C., Beltramello, M., Chen, A., Liu, Z., Zatta, F., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.028 · Cited by 901 · see citing works
“Likewise, previous work on MERS-CoV established that the NTD is the target of several potent and protective neutralizing mAbs and an attractive target for vaccine design (Chen et al., 2017; Jiaming et al., 2017; Wang et al., 2018; Wang et al., 2019; Zhou et al., 2019).”
Immunological mechanisms of vaccine-induced protection against COVID-19 in humans
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Microstructure, pathophysiology, and potential therapeutics of COVID‐19: A comprehensive review
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N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2
McCallum, M., Marco, A. D., Lempp, F., Tortorici, M. A., Pinto, D., Walls, A. C., Beltramello, M., Chen, A., Liu, Z., Zatta, F., et al. (2021) · doi:10.1101/2021.01.14.426475 · Cited by 901 · see citing works
- Authors
- Wang, N., Rosen, O., Wang, L., Turner, H. L., Stevens, L. J., Corbett, K. S., Bowman, C. A., Pallesen, J., Shi, W., Zhang, Y., Leung, K., Kirchdoerfer, R. N., Becker, M. M., Denison, M. R., Chappell, J. D., Ward, A. B., Graham, B. S., & McLellan, J. S.
- Affiliations
- The University of Texas at Austin (US)
- National Institute of Allergy and Infectious Diseases (US)
- Scripps Research Institute (US)
- Vanderbilt University (US)
- Corresponding author
- McLellan, Jason S.
- ORCID
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2019-09
- Volume
- 28
- Issue
- 13
- Pages
- 3395-3405.e6
- ISSN
- 2211-1247 (ISSN-L)
- PMC
- PMC6935267
- OpenAlex
- W2975856930
- Cited by
- 86
- References
- 77
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 6 · 2023: 7 · 2022: 4 · 2021: 19 · 2020: 40
- FWCI
- 12.27
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cell Reports (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- IUScholarWorks Open (Indiana University) (submittedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- Vaccine Research Center
- National Institutes of Health (16x142, R01AI127521)
- U.S. Department of Energy
- National Institute of Allergy and Infectious Diseases
- Biological and Environmental Research (DE-AC02-06CH11357)
- Argonne National Laboratory
- 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, SARS-CoV-2, neutralizing antibodies, antibody epitopes, dipeptidyl peptidase IV, receptor binding, spike protein trimer, antibody-antigen complex structure, vaccine development, immunotherapeutics
- MeSH terms
- Epitopes, Humans, Middle East Respiratory Syndrome Coronavirus
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