Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors
Open accessAbstract
The Middle East respiratory syndrome coronavirus (MERS-CoV) causes severe and often lethal respiratory illness in humans, and no vaccines or specific treatments are available. Infections are initiated via binding of the MERS-CoV spike (S) glycoprotein to sialosides and dipeptidyl-peptidase 4 (the attachment and entry receptors, respectively). To understand MERS-CoV engagement of sialylated receptors, we determined the cryo-EM structures of S in complex with 5-N-acetyl neuraminic acid, 5-N-glycolyl neuraminic acid, sialyl-Lewis X, α2,3-sialyl-N-acetyl-lactosamine and α2,6-sialyl-N-acetyl-lactosamine at 2.7-3.0 Å resolution. We show that recognition occurs via a conserved groove that is essential for MERS-CoV S-mediated attachment to sialosides and entry into human airway epithelial cells. Our data illuminate MERS-CoV S sialoside specificity and suggest that selectivity for α2,3-linked over α2,6-linked receptors results from enhanced interactions with the former class of oligosaccharides. This study provides a structural framework explaining MERS-CoV attachment to sialoside receptors and identifies a site of potential vulnerability to inhibitors of viral entry.
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New SARS-CoV-2 variants are found and predicted to exploit a cellular attachment-promoting factor to increase infection and transmission efficiency in ACE2 cells of the upper respiratory tract.
“The new variants are found and predicted to exploit a cellular attachment promoting factor to increase the variant’s efficiency in terms of both infection and transmission to infect ACE2 cells in the upper respiratory tract [13].”
From Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe (2022) · cites this paper as [13]
The Results (page unavailable) show that sialoside attachment promotes MERS-CoV spike-mediated entry into human airway cells. The Discussion (page unavailable) suggests that this attachment may facilitate binding to DPP4. The paper does not establish the claim about new SARS-CoV-2 variants, ACE2 cells, or increased transmission efficiency. (LLM, conf=0.87)
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“The new variants are found and predicted to exploit a cellular attachment promoting factor to increase the variant’s efficiency in terms of both infection and transmission to infect ACE2 cells in the upper respiratory tract [13].”
BackgroundWang, C., van Haperen, R., Gutiérrez-Álvarez, J., Li, W., Okba, N. M. A., Albulescu, I., Widjaja, I., van Dieren, B., Fernandez-Delgado, R., Sola, I., et al. (2020) · doi:10.1101/2020.10.20.346916 · Cited by 15 · see citing works
Self-citation
- Authors
- Park, Y.-J., Walls, A. C., Wang, Z., Sauer, M. M., Li, W., Tortorici, M. A., Bosch, B.-J., DiMaio, F., & Veesler, D.
- Affiliations
- University of Washington (US)
- Utrecht University (NL)
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Veesler, David
- ORCID
- Venue
- Nature Structural & Molecular Biology
- Published
- 2019-12
- Volume
- 26
- Issue
- 12
- Pages
- 1151-1157
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- PMC
- PMC7097669
- OpenAlex
- W2995902735
- Cited by
- 260
- References
- 69
- Citations by year
- 2026: 10 · 2025: 14 · 2024: 21 · 2023: 18 · 2022: 42 · 2021: 67 · 2020: 86 · 2019: 1
- FWCI
- 37.95
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
- Funders
- National Science Foundation
- Burroughs Wellcome Fund
- University of Washington
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
- National Institute of General Medical Sciences (R01GM120553, R01GM123089)
- National Institute of Allergy and Infectious Diseases (HHSN272201700059C)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Keywords
- MERS-CoV, spike protein, dipeptidyl peptidase IV, viral attachment, receptor specificity, α2,3-linked sialic acid, α2,6-linked sialic acid, sialyl Lewis X, N-acetylneuraminic acid, viral entry inhibitors
- MeSH terms
- Protein Domains, Binding Sites, Carbohydrate Conformation, Hemagglutination, Viral, Humans, Models, Molecular, Protein Binding, Protein Conformation, Sialic Acids, Structure-Activity Relationship, Dipeptidyl Peptidase 4, Cryoelectron Microscopy, Protein Interaction Mapping, Spike Glycoprotein, Coronavirus, Middle East Respiratory Syndrome Coronavirus
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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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