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 accessAbstract
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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Cites
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Structural basis for human coronavirus attachment to sialic acid receptors
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Cited by
Correlates of protection against SARS‐CoV‐2 infection and COVID‐19 disease
Goldblatt, D., Alter, G., Crotty, S., & Plotkin, S. A. (2022) · Immunological Reviews · doi:10.1111/imr.13091 · Cited by 298
Evolution and phylogenetic distribution of endo -α-mannosidase
Sobala, Ł. F. (2023) · Glycobiology · doi:10.1093/glycob/cwad041 · Cited by 5
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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- 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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