The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2
Open accessAbstract
We show that SARS-CoV-2 spike protein interacts with both cellular heparan sulfate and angiotensin-converting enzyme 2 (ACE2) through its receptor-binding domain (RBD). Docking studies suggest a heparin/heparan sulfate-binding site adjacent to the ACE2-binding site. Both ACE2 and heparin can bind independently to spike protein in vitro, and a ternary complex can be generated using heparin as a scaffold. Electron micrographs of spike protein suggests that heparin enhances the open conformation of the RBD that binds ACE2. On cells, spike protein binding depends on both heparan sulfate and ACE2. Unfractionated heparin, non-anticoagulant heparin, heparin lyases, and lung heparan sulfate potently block spike protein binding and/or infection by pseudotyped virus and authentic SARS-CoV-2 virus. We suggest a model in which viral attachment and infection involves heparan sulfate-dependent enhancement of binding to ACE2. Manipulation of heparan sulfate or inhibition of viral adhesion by exogenous heparin presents new therapeutic opportunities.
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Cites
Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., Graham, B. S., & McLellan, J. S. (2020) · Science · doi:10.1126/science.abb2507 · Cited by 8,897
Self-citationRemdesivir for the Treatment of Covid-19 — Final Report
Beigel, J. H., Tomashek, K. M., Dodd, L. E., Mehta, A. K., Zingman, B. S., Kalil, A. C., Hohmann, E., Chu, H. Y., Luetkemeyer, A., Kline, S., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2007764 · Cited by 7,267
Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
Li, W., Moore, M. J., Vasilieva, N., Sui, J., Wong, S. K., Berne, M. A., Somasundaran, M., Sullivan, J. L., Luzuriaga, K., Greenough, T. C., et al. (2003) · Nature · doi:10.1038/nature02145 · Cited by 5,923
RELION: Implementation of a Bayesian approach to cryo-EM structure determination
Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446
Order Out of Chaos: Assembly of Ligand Binding Sites in Heparan Sulfate
Esko, J. D., & Selleck, S. B. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.110601.135458 · Cited by 1,495
Self-citationLoss of Bcl-6-Expressing T Follicular Helper Cells and Germinal Centers in COVID-19
Kaneko, N., Kuo, H.-H., Boucau, J., Farmer, J. R., Allard-Chamard, H., Mahajan, V. S., Piechocka-Trocha, A., Lefteri, K., Osborn, M., Bals, J., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.025 · Cited by 734
Self-citationThe versatile heparin in COVID-19
Thachil, J. (2020) · Journal of Thrombosis and Haemostasis · doi:10.1111/jth.14821 · Cited by 404
Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors
Park, Y.-J., Walls, A. C., Wang, Z., Sauer, M. M., Li, W., Tortorici, M. A., Bosch, B.-J., DiMaio, F., & Veesler, D. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0334-7 · Cited by 260
Cited by
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“SARS-CoV-2 S also engages cell-surface heparan-sulfates (Clausen et al., 2020), neuropilin-1 (Cantuti-Castelvetri et al.”
COVID-19, immunothrombosis and venous thromboembolism: biological mechanisms
Loo, J., Spittle, D. A., & Newnham, M. (2021) · Thorax · doi:10.1136/thoraxjnl-2020-216243 · Cited by 341
Baker, A. N., Richards, S.-J., Guy, C. S., Congdon, T. R., Hasan, M., Zwetsloot, A. J., Gallo, A., Lewandowski, J. R., Stansfeld, P. J., Straube, A., et al. (2020) · ACS Central Science · doi:10.1021/acscentsci.0c00855 · Cited by 303
SARS-CoV-2 escape in vitro from a highly neutralizing COVID-19 convalescent plasma
Andreano, E., Piccini, G., Licastro, D., Casalino, L., Johnson, N. V., Paciello, I., Monego, S. D., Pantano, E., Manganaro, N., Manenti, A., et al. (2020) · doi:10.1101/2020.12.28.424451
Adverse effects of COVID-19 mRNA vaccines: the spike hypothesis
Trougakos, I. P., Terpos, E., Alexopoulos, H., Politou, M., Paraskevis, D., Scorilas, A., Kastritis, E., Andreakos, E., & Dimopoulos, M. A. (2022) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2022.04.007 · Cited by 273
Metadata
- Authors
- Clausen, T. M., Sandoval, D. R., Spliid, C. B., Pihl, J., Perrett, H. R., Painter, C. D., Narayanan, A., Majowicz, S. A., Kwong, E. M., McVicar, R. N., Thacker, B. E., Glass, C. A., Yang, Z., Torres, J. L., Golden, G. J., Bartels, P. L., Porell, R. N., Garretson, A. F., Laubach, L., Feldman, J., Yin, X., Pu, Y., Hauser, B. M., Caradonna, T. M., Kellman, B. P., Martino, C., Gordts, P. L. S. M., Chanda, S. K., Schmidt, A. G., Godula, K., Leibel, S. L., Jose, J., Corbett, K. D., Ward, A. B., Carlin, A. F., & Esko, J. D.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2020-11
- Volume
- 183
- Issue
- 4
- Pages
- 1043-1057.e15
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W3085153423
- Cited by
- 1,136
- References
- 8
- FWCI
- 24.32
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Clausen, T. M., Sandoval, D. R., Spliid, C. B., Pihl, J., Perrett, H. R., Painter, C. D., Narayanan, A., Majowicz, S. A., Kwong, E. M., McVicar, R. N., Thacker, B. E., Glass, C. A., Yang, Z., Torres, J. L., Golden, G. J., Bartels, P. L., Porell, R. N., Garretson, A. F., Laubach, L., . . . Esko, J. D. (2020). SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2. Cell. https://doi.org/10.1016/j.cell.2020.09.033
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
