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The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.

Sialic acid-containing glycolipids mediate binding and viral entry of SARS-CoV-2

Open access
Nguyen, Linh, McCord, Kelli A., Bui, Duong T., Bouwman, Kim M., Kitova, Elena N., Elaish, Mohamed, Kumawat, Dhanraj, Daskhan, Gour C., Tomris, Ilhan, Han, Ling, Chopra, Pradeep, Yang, Tzu-Jing, Willows, Steven D., Mason, Andrew L., Mahal, Lara K., Lowary, Todd L., West, Lori J., Hsu, Shang-Te Danny, Hobman, Tom, Tompkins, Stephen M., Boons, Geert-Jan, de Vries, Robert P., Macauley, Matthew S., Klassen, John S.·2022·Nature Chemical Biology

Abstract

Emerging evidence suggests that host glycans influence severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Here, we reveal that the receptor-binding domain (RBD) of the spike (S) protein on SARS-CoV-2 recognizes oligosaccharides containing sialic acid (Sia), with preference for monosialylated gangliosides. Gangliosides embedded within an artificial membrane also bind to the RBD. The monomeric affinities ( K d = 100–200 μM) of gangliosides for the RBD are similar to another negatively charged glycan ligand of the RBD proposed as a viral co-receptor, heparan sulfate (HS) dp2–dp6 oligosaccharides. RBD binding and infection of SARS-CoV-2 pseudotyped lentivirus to angiotensin-converting enzyme 2 (ACE2)-expressing cells is decreased following depletion of cell surface Sia levels using three approaches: sialyltransferase (ST) inhibition, genetic knockout of Sia biosynthesis, or neuraminidase treatment. These effects on RBD binding and both pseudotyped and authentic SARS-CoV-2 viral entry are recapitulated with pharmacological or genetic disruption of glycolipid biosynthesis. Together, these results suggest that sialylated glycans, specifically glycolipids, facilitate viral entry of SARS-CoV-2. Mass spectrometric profiling of a glycan library reveals that sialylated glycans, especially sialic acid-containing gangliosides, interact with the RBD of the SARS-CoV-2 spike protein and are involved in ACE2-dependent viral infection.

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Metadata

Authors
Nguyen, L., McCord, K. A., Bui, D. T., Bouwman, K. M., Kitova, E. N., Elaish, M., Kumawat, D., Daskhan, G. C., Tomris, I., Han, L., Chopra, P., Yang, T.-J., Willows, S. D., Mason, A. L., Mahal, L. K., Lowary, T. L., West, L. J., Hsu, S.-T. D., Hobman, T., Tompkins, S. M., Boons, G.-J., de Vries, R. P., Macauley, M. S., & Klassen, J. S.
Venue
Nature Chemical Biology
Published
2021-11-09
Volume
18
Issue
1
Pages
81-90
ISSN
  • 1552-4450 (ISSN-L)
  • 1552-4469
OpenAlex
W3213442916
Cited by
259
References
58
FWCI
13.99
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Sialic acid-containing glycolipids mediate binding and viral entry of SARS-CoV-2. https://app.cochat.ai/papers/10.1038/s41589-021-00924-1
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Nguyen, L., McCord, K. A., Bui, D. T., Bouwman, K. M., Kitova, E. N., Elaish, M., Kumawat, D., Daskhan, G. C., Tomris, I., Han, L., Chopra, P., Yang, T.-J., Willows, S. D., Mason, A. L., Mahal, L. K., Lowary, T. L., West, L. J., Hsu, S.-T. D., Hobman, T., . . . Klassen, J. S. (2022). Sialic acid-containing glycolipids mediate binding and viral entry of SARS-CoV-2. Nature Chemical Biology. https://doi.org/10.1038/s41589-021-00924-1

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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