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Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses
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Abstract
Over the past 20 years, several coronaviruses have crossed the species barrier into humans, causing outbreaks of severe, and often fatal, respiratory illness. Since SARS-CoV was first identified in animal markets, global viromics projects have discovered thousands of coronavirus sequences in diverse animals and geographic regions. Unfortunately, there are few tools available to functionally test these viruses for their ability to infect humans, which has severely hampered efforts to predict the next zoonotic viral outbreak. Here, we developed an approach to rapidly screen lineage B betacoronaviruses, such as SARS-CoV and the recent SARS-CoV-2, for receptor usage and their ability to infect cell types from different species. We show that host protease processing during viral entry is a significant barrier for several lineage B viruses and that bypassing this barrier allows several lineage B viruses to enter human cells through an unknown receptor. We also demonstrate how different lineage B viruses can recombine to gain entry into human cells, and confirm that human ACE2 is the receptor for the recently emerging SARS-CoV-2.
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In the citing paper
“The S protein mediates binding of coronaviruses to angiotensin converting enzyme 2 (ACE2) on the surface of various cell types including epithelial cells of the pulmonary alveolus (4–6).”
From An Alphavirus -derived replicon RNA vaccine induces SARS-CoV-2 neutralizing antibody and T cell responses in mice and nonhuman primates (2020) · cites this paper as [5]
Experimental — accuracy not yet measuredIn the citing paper
“it directly interacts with the cellular receptor angiotensin converting enzyme 2 (ACE2) which mediates host cell entry”
From SARS-CoV-2 mRNA vaccination induces functionally diverse antibodies to NTD, RBD, and S2 (2021) · cites this paper as Letko et al., 2020
In the citing paper
“SARS-CoV-2 is a single-stranded RNA β-coronavirus and a member of the subgenus Sarbecovirus (beta-CoV lineage B).”
From Oral Microbiome and SARS-CoV-2: Beware of Lung Co-infection (2020) · cites this paper as Letko et al., 2020
In the citing paper
“It is the seventh member of the Coronaviridae known to infect humans so far, two of which, SARS-CoV and MERS-CoV, caused global health threats previously (Guarner, 2020; Letko et al., 2020).”
From Oral Microbiome and SARS-CoV-2: Beware of Lung Co-infection (2020) · cites this paper as Letko et al., 2020
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Cites
A pneumonia outbreak associated with a new coronavirus of probable bat origin
Zhou, P., Yang, X.-L., Wang, X.-G., Hu, B., Zhang, L., Zhang, W., Si, H.-R., Zhu, Y., Li, B., Huang, C.-L., et al. (2020) · Nature · doi:10.1038/s41586-020-2012-7 · Cited by 21,969
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
Wan, Y., Shang, J., Graham, R., Baric, R. S., & Li, F. (2020) · Journal of Virology · doi:10.1128/jvi.00127-20 · Cited by 4,341
Structure, Function, and Evolution of Coronavirus Spike Proteins
Li, F. (2016) · Annual Review of Virology · doi:10.1146/annurev-virology-110615-042301 · Cited by 2,740
Bats Are Natural Reservoirs of SARS-Like Coronaviruses
Li, W., Shi, Z., Yu, M., Ren, W., Smith, C. S., Epstein, J. H., Wang, H., Crameri, G. S., Hú, Z., Zhang, H., et al. (2005) · Science · doi:10.1126/science.1118391 · Cited by 2,571
Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC
Raj, V. S., Mou, H., Smits, S. L., Dekkers, D. H. W., Müller, M. A., Dijkman, R., Muth, D., Demmers, J. A. A., Zaki, A., Fouchier, R. A. M., et al. (2013) · Nature · doi:10.1038/nature12005 · Cited by 2,061
Structure of SARS Coronavirus Spike Receptor-Binding Domain Complexed with Receptor
Li, F., Li, W., Farzan, M., & Harrison, S. C. (2005) · Science · doi:10.1126/science.1116480 · Cited by 2,035
Isolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor
Ge, X.-Y., Li, J.-L., Yang, X.-L., Chmura, A. A., Zhu, G., Epstein, J. H., Mazet, J. K., Hu, B., Zhang, W., Peng, C., et al. (2013) · Nature · doi:10.1038/nature12711 · Cited by 1,778
Severe acute respiratory syndrome coronavirus-like virus in Chinese horseshoe bats
Lau, S. K. P., Woo, P. C. Y., Li, K. S. M., Huang, Y. P., Tsoi, H., Wong, B. H. L., Wong, S. S. Y., Leung, S.-Y., Chan, K., & Yuen, K. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506735102 · Cited by 1,561
Belouzard, S., Chu, V. C., & Whittaker, G. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809524106 · Cited by 1,076
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Klimstra, W. B., Tilston-Lunel, N. L., Nambulli, S., Boslett, J., McMillen, C. M., Gilliland, T., Dunn, M. D., Sun, C., Wheeler, S. E., Wells, A., et al. (2020) · Journal of General Virology · doi:10.1099/jgv.0.001481 · Cited by 137
Efforts at COVID-19 Vaccine Development: Challenges and Successes
Haque, A., & Pant, A. B. (2020) · Vaccines · doi:10.3390/vaccines8040739 · Cited by 141
Neerukonda, S. N., Vassell, R. A., Herrup, R., Liu, S., Wang, T. T., Takeda, K., Yang, Y., Lin, T.-L., Wang, W., & Weiss, C. D. (2021) · PLoS ONE · doi:10.1371/journal.pone.0248348 · Cited by 133
Fang, Z., Qin, H., Mao, J., Wang, Z., Zhang, N., Wang, Y., Liu, L., Nie, Y., Dong, M., & Ye, M. (2022) · Nature Communications · doi:10.1038/s41467-022-29530-y · Cited by 136
Engineered ACE2 receptor therapy overcomes mutational escape of SARS-CoV-2
Higuchi, Y., Suzuki, T., Arimori, T., Ikemura, N., Mihara, E., Kirita, Y., Ohgitani, E., Mazda, O., Motooka, D., Nakamura, S., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24013-y · Cited by 129
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Khoury, D. S., Wheatley, A. K., Ramuta, M. D., Reynaldi, A., Cromer, D., Subbarao, K., O’Connor, D. H., Kent, S. J., & Davenport, M. P. (2020) · Nature Reviews Immunology · doi:10.1038/s41577-020-00471-1 · Cited by 115
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Sefik, E., Israelow, B., Mirza, H., Zhao, J., Qu, R., Kaffe, E., Song, E., Halene, S., Meffre, E., Kluger, Y., et al. (2021) · Nature Biotechnology · doi:10.1038/s41587-021-01155-4 · Cited by 136
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Millet, J. K., Jaimes, J. A., & Whittaker, G. R. (2020) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaa057 · Cited by 137
Li, W., Chen, Y., Prévost, J., Ullah, I., Lu, M., Gong, S. Y., Tauzin, A., Gasser, R., Vézina, D., Anand, S. P., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110210 · Cited by 128
Gong, Y., Tsao, K., Hsiao, M., Huang, C., Huang, P.-N., Huang, P.-W., Lee, K.-M., Liu, Y., Yang, S.-L., Kuo, R.-L., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1782271 · Cited by 130
Wei, Y., & Shah, R. (2020) · Pharmaceuticals · doi:10.3390/ph13070155 · Cited by 140
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Mesquita, F. S., Abrami, L., Sergeeva, O. A., Turelli, P., Qing, E., Kunz, B., Raclot, C., Montoya, J. P., Abriata, L. A., Gallagher, T., et al. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.09.016 · Cited by 129
Identifying and prioritizing potential human-infecting viruses from their genome sequences
Mollentze, N., Babayan, S. A., & Streicker, D. G. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001390 · Cited by 133
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Bohan, D., Ert, H. A. V., Ruggio, N., Rogers, K. J., Badreddine, M., Aguilar-Briseño, J. A., Elliff, J. M., Chávez, R. A. R., Gao, B., Stokowy, T., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009743 · Cited by 132
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Tian, D., & Ye, Q. (2020) · Journal of Medical Virology · doi:10.1002/jmv.26036 · Cited by 129
Li, J., Li, H., Xu, J., Yang, M., Ma, C., Li, J., Zhao, S., Wang, H., Yang, Y., Yu, W., et al. (2020) · Gastroenterology · doi:10.1053/j.gastro.2020.12.001 · Cited by 127
Nanomedicine for COVID-19: the role of nanotechnology in the treatment and diagnosis of COVID-19
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Dhawan, M. K., Saied, A. A., Mitra, S., Alhumaydhi, F. A., Emran, T. B., & Wilairatana, P. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113522 · Cited by 130
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McCallum, M., Bassi, J., Marco, A. D., Chen, A., Walls, A. C., di Iulio, J., Tortorici, M. A., Navarro, M.-J., Silacci-Fregni, C., Saliba, C., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.31.437925 · Cited by 128
Li, R., Qiao, S., & Zhang, G. (2020) · Journal of Infection · doi:10.1016/j.jinf.2020.02.013 · Cited by 125
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Luan, J., Jin, X., Lu, Y., & Zhang, L. (2020) · Journal of Medical Virology · doi:10.1002/jmv.25817 · Cited by 130
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Fang, W., Jiang, J., Su, L., Shu, T., Liu, H., Lai, S., Ghiladi, R. A., & Wang, J. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.12.008 · Cited by 128
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Wang, P., Liu, L., Nair, M. S., Yin, M. T., Luo, Y., Wang, Q., Yuan, T., Mori, K., Solis, A. G., Yamashita, M., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1823890 · Cited by 122
Ashary, N., Bhide, A., Chakraborty, P., Colaco, S., Mishra, A., Chhabria, K., Jolly, M. K., & Modi, D. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00783 · Cited by 121
Butler, S. E., Crowley, A. R., Natarajan, H., Xu, S., Weiner, J. A., Bobak, C. A., Mattox, D. E., Lee, J., Wieland‐Alter, W., Connor, R. I., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.618685 · Cited by 120
Shang, J., Wang, Q., Zhang, H., Wang, X., Wan, J., Yan, Y., Gao, Y., Cheng, J., Li, Z., & Lin, J. (2020) · The American Journal of Medicine · doi:10.1016/j.amjmed.2020.05.033 · Cited by 121
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Guthmiller, J. J., Stovicek, O., Wang, J., Changrob, S., Li, L., Halfmann, P., Zheng, N., Utset, H. A., Stamper, C. T., Dugan, H. L., et al. (2021) · mBio · doi:10.1128/mbio.02940-20 · Cited by 116
The genetic structure of SARS‐CoV‐2 does not rule out a laboratory origin
Segreto, R., & Deigin, Y. (2020) · BioEssays · doi:10.1002/bies.202000240 · Cited by 126
King, R. G., Silva-Sánchez, A., Peel, J. N., Botta, D., Dickson, A. M., Pinto, A. K., Meza‐Perez, S., Allie, S. R., Schultz, M. D., Liu, M., et al. (2021) · Vaccines · doi:10.3390/vaccines9080881 · Cited by 134
Tortorici, M. A., Addetia, A., Seo, A. J., Brown, J. T., Sprouse, K., Logue, J., Clark, E., Franko, N., Chu, H. Y., & Veesler, D. (2024) · Immunity · doi:10.1016/j.immuni.2024.02.016 · Cited by 127
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Maio, F. D., Posteraro, B., Ponziani, F. R., Cattani, P., Gasbarrini, A., & Sanguinetti, M. (2020) · Biological Procedures Online · doi:10.1186/s12575-020-00131-7 · Cited by 116
Tucker, N. R., Chaffin, M. D., Bedi, K. C., Papangeli, I., Akkad, A.-D., Arduini, A., Hayat, S., Eraslan, G., Muus, C., Bhattacharyya, R. P., et al. (2020) · Circulation · doi:10.1161/circulationaha.120.047911 · Cited by 119
Gorshkov, K., Susumu, K., Chen, J., Xu, M., Pradhan, M., Zhu, W., Hu, X., Breger, J. C., Wolak, M. A., & Oh, E. (2020) · ACS Nano · doi:10.1021/acsnano.0c05975 · Cited by 116
Brendler, T., Al‐Harrasi, A., Bauer, R., Gafner, S., Hardy, M. L., Heinrich, M., Hosseinzadeh, H., Izzo, A. A., Michaelis, M., Nassiri‐Asl, M., et al. (2020) · Phytotherapy Research · doi:10.1002/ptr.7008 · Cited by 122
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Jana, I. D., Kumbhakar, P., Banerjee, S., Gowda, C. C., Kedia, N., Kuila, S. K., Banerjee, S., Das, N. C., Das, A. K., Manna, I., et al. (2020) · ACS Applied Nano Materials · doi:10.1021/acsanm.0c02713 · Cited by 129
Tan, Q., Duan, L., Ma, Y., Wu, F., Huang, Q., Mao, K., Xiao, W., Xia, H., Zhang, S., Zhou, E., et al. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104257 · Cited by 116
Pan, B., Fang, S., Zhang, J., Pan, Y., Liu, H., Wang, Y., Li, M., & Liu, L. (2020) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2020.11.010 · Cited by 116
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Liu, X., Liang, W. P., Xu, F., Zhao, F., Huang, Y., Fan, Z., Mei, S., Hu, Y., Zhai, L., Guo, J., et al. (2022) · Science Signaling · doi:10.1126/scisignal.abg8744 · Cited by 110
Thachil, J. V., & Srivastava, A. (2020) · Seminars in Thrombosis and Hemostasis · doi:10.1055/s-0040-1712155 · Cited by 111
Kaur, N., Singh, R., Dar, Z., Bijarnia, R. K., Dhingra, N., & Kaur, T. (2020) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2020.104490 · Cited by 115
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An, X., Zhang, Y., Duan, L., Jin, D., Zhao, S., Zhou, R., Duan, Y., Lian, F., & Tong, X. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111267 · Cited by 101
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Meekins, D. A., Gaudreault, N. N., & Richt, J. A. (2021) · Viruses · doi:10.3390/v13101993 · Cited by 105
Liu, Z., VanBlargan, L. A., Bloyet, L.-M., Rothlauf, P. W., Chen, R. E., Stumpf, S., Zhao, H., Errico, J. M., Theel, E. S., Liebeskind, M. J., et al. (2020) · doi:10.1101/2020.11.06.372037 · Cited by 135
Chen, L., & Hao, G. (2020) · Cardiovascular Research · doi:10.1093/cvr/cvaa093 · Cited by 104
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Gao, C., Zeng, J., Jia, N., Stavenhagen, K., Matsumoto, Y., Zhang, H., Jiang, L., Hume, A. J., Mühlberger, E., van Die, I., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.29.227462 · Cited by 105
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Ostaszewski, M., Niarakis, A., Mazein, A., Kuperstein, I., Phair, R. D., Resendiz, A. O., Singh, V., Aghamiri, S. S., Acencio, M. L., Glaab, E., et al. (2021) · Molecular Systems Biology · doi:10.15252/msb.202110387 · Cited by 104
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Martins, M., Boggiatto, P. M., Buckley, A., Cassmann, E. D., Falkenberg, S. M., Caserta, L. C., Fernandes, M. H. V., Kanipe, C. R., Lager, K. M., Palmer, M. V., et al. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010197 · Cited by 101
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Duda‐Chodak, A., Łukasiewicz, M., Zięć, G., Florkiewicz, A., & Filipiak‐Florkiewicz, A. (2020) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2020.08.020 · Cited by 105
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Shyr, Z. A., Gorshkov, K., Chen, C. Z., & Zheng, W. (2020) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.120.000123 · Cited by 98
Mehany, T., Khalifa, I., Barakat, H., Althwab, S. A., Alharbi, Y., & Sohaimy, S. A. E. (2021) · Food Bioscience · doi:10.1016/j.fbio.2021.100891 · Cited by 103
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Alenquer, M., Ferreira, F., Lousa, D., Valério, M., Medina-Lopes, M., Bergman, M., Gonçalves, J., Demengeot, J., Leite, R. B., Lilue, J., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009772 · Cited by 101
Pastorio, C., Zech, F., Noettger, S., Jung, C., Jacob, T., Sanderson, T., Sparrer, K. M. J., & Kirchhoff, F. (2022) · Cell Host & Microbe · doi:10.1016/j.chom.2022.07.006 · Cited by 95
Stamatatos, L., Czartoski, J., Wan, Y.-H., Homad, L. J., Rubin, V., Glantz, H., Neradilek, M., Seydoux, E., Jennewein, M. F., MacCamy, A. J., et al. (2021) · doi:10.1101/2021.02.05.21251182 · Cited by 559
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Fadini, G. P., Morieri, M. L., Longato, E., Bonora, B. M., Pinelli, S., Selmin, E., Voltan, G., Falaguasta, D., Tresso, S., Costantini, G., et al. (2020) · Diabetes Obesity and Metabolism · doi:10.1111/dom.14097 · Cited by 96
Metadata
- Authors
- Letko, M., Marzi, A., & Munster, V.
- Affiliations
- National Institutes of Health (US)
- National Institute of Allergy and Infectious Diseases (US)
- Corresponding author
- Letko, Michael
- Munster, Vincent
- Venue
- Nature Microbiology
- Published
- 2020-02-24
- Volume
- 5
- Issue
- 4
- Pages
- 562-569
- ISSN
- 2058-5276 (ISSN-L)
- PMC
- PMC7095430
- OpenAlex
- W3008394341
- Cited by
- 3,109
- References
- 38
- Citations by year
- 2026: 47 · 2025: 122 · 2024: 198 · 2023: 287 · 2022: 571 · 2021: 874 · 2020: 1002
- FWCI
- 89.66
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Nature Microbiology (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion)
- Funders
- Chinese Center for Disease Control and Prevention
- Chinese Academy of Medical Sciences
- Peking Union Medical College
- National Institute of Allergy and Infectious Diseases
- 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
- Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Zoonotic diseases and public health
- Keywords
- SARS-CoV-2, SARS-CoV, cell entry, ACE2 receptor, zoonotic transmission, viral recombination, cross-species infection
- MeSH terms
- Protein Domains, Betacoronavirus, Receptors, Coronavirus, Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, Animals, Cell Line, Humans, Peptidyl-Dipeptidase A, Mutation, Pneumonia, Viral, Receptors, Virus, Recombinant Fusion Proteins, Trypsin, Coronavirus Infections, Dipeptidyl Peptidase 4, CD13 Antigens, Severe acute respiratory syndrome-related coronavirus, Virus Internalization, Pandemics, Spike Glycoprotein, Coronavirus
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