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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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Damas, J., Hughes, G. M., Keough, K. C., Painter, C., Persky, N. S., Corbo, M., Hiller, M., Koepfli, K., Pfenning, A. R., Zhao, H., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.16.045302 · Cited by 98
Jung, F., Krüger‐Genge, A., Franke, R. P., Hufert, F. T., & Küpper, J. ‐. (2020) · Clinical Hemorheology and Microcirculation · doi:10.3233/ch-209007 · Cited by 97
Rossi, G. A., Sacco, O., Mancino, E., Cristiani, L., & Midulla, F. (2020) · Infection · doi:10.1007/s15010-020-01486-5 · Cited by 102
Elekofehinti, O. O., Iwaloye, O., Josiah, S. S., Lawal, A. O., Akinjiyan, M. O., & Ariyo, E. O. (2020) · Molecular Diversity · doi:10.1007/s11030-020-10151-w · Cited by 100
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Pollet, J. B. K., Chen, W., Versteeg, L., Keegan, B. P., Zhan, B., Wei, J., Liu, Z., Lee, J., Kundu, R., Adhikari, R., et al. (2021) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2021.1901545 · Cited by 94
Revzin, M. V., Raza, S., Warshawsky, R., D’Agostino, C. A., Srivastava, N. C., Bader, A. S., Malhotra, A., Patel, R. D., Chen, K., Kyriakakos, C., et al. (2020) · Radiographics · doi:10.1148/rg.2020200149 · Cited by 103
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Shuai, L., Zhong, G., Yuan, Q., Wen, Z., Wang, C., He, X., Liu, R., Wang, J., Zhao, Q., Liu, Y., et al. (2020) · National Science Review · doi:10.1093/nsr/nwaa291 · Cited by 98
Pickering, B., Smith, G. C., Pinette, M. M., Embury‐Hyatt, C., Moffat, E., Marszal, P., & Lewis, C. E. (2020) · Emerging infectious diseases · doi:10.3201/eid2701.203399 · Cited by 95
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Ballout, R. A., Sviridov, D., Bukrinsky, M., & Remaley, A. T. (2020) · The FASEB Journal · doi:10.1096/fj.202000654r · Cited by 91
Park, S. E. (2020) · Pediatric Infection & Vaccine · doi:10.14776/piv.2020.27.e9 · Cited by 102
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Atlas of ACE2 gene expression reveals novel insights into transmission of SARS-CoV-2
Sun, K., Gu, L., Ma, L., & Duan, Y. (2020) · Heliyon · doi:10.1016/j.heliyon.2020.e05850 · Cited by 97
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Chen, Y., Tong, P., Whiteman, N. B., Moghaddam, A. S., Zarghami, M., Zuiani, A., Habibi, S., Gautam, A. K., Keerti, K., Bi, C., et al. (2022) · Science Immunology · doi:10.1126/sciimmunol.abp8328 · Cited by 89
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White, J. M., Ward, A. E., Odongo, L., & Tamm, L. K. (2023) · Annual Review of Virology · doi:10.1146/annurev-virology-111821-093413 · Cited by 99
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Nadeem, M. S., Zamzami, M. A., Choudhry, H., Murtaza, B. N., Kazmi, I. A., Ahmad, H., & Shakoori, A. R. (2020) · Pathogens · doi:10.3390/pathogens9040307 · Cited by 95
Troyer, Z., Alhusaini, N., Tabler, C. O., Sweet, T. J., Carvalho, K. I., Schlatzer, D., Carias, L. L., King, C. L., Matreyek, K. A., & Tilton, J. C. (2021) · Journal of Extracellular Vesicles · doi:10.1002/jev2.12112 · Cited by 90
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Kosidło, J. W., Wolszczak-Biedrzycka, B., Matowicka-Karna, J., Dymicka-Piekarska, V., & Dorf, J. (2023) · Journal of Inflammation Research · doi:10.2147/jir.s395331 · Cited by 93
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Harbison, A. M., Fogarty, C. A., Phung, T. K., Satheesan, A., Schulz, B. L., & Fadda, E. (2021) · Chemical Science · doi:10.1039/d1sc04832e · Cited by 86
Maria, E. D., Latini, A., Borgiani, P., & Novelli, G. (2020) · Human Genomics · doi:10.1186/s40246-020-00280-6 · Cited by 93
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Keyhan, S. O., Fallahi, H. R., & Cheshmi, B. (2020) · Maxillofacial Plastic and Reconstructive Surgery · doi:10.1186/s40902-020-00254-7 · Cited by 93
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Ashhurst, A. S., Tang, A. H., Fajtová, P., Yoon, M. C., Aggarwal, A., Bedding, M. J., Stoye, A., Beretta, L., Pwee, D., Drelich, A. K., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01494 · Cited by 95
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Sencio, V., Machelart, A., Robil, C., Benech, N., Hoffmann, E., Galbert, C., Deryuter, L., Heumel, S., Hantute-Ghesquier, A., Flourens, A., et al. (2021) · Gut Microbes · doi:10.1080/19490976.2021.2018900 · Cited by 90
Buhre, J. S., Pongrácz, T., Künsting, I., Lixenfeld, A. S., Wang, W., Nouta, J., Lehrian, S., Schmelter, F., Lunding, H. B., Dühring, L., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1020844 · Cited by 90
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Patel, D. P., Punjani, N., Guo, J., Alukal, J. P., Li, P. S., & Hotaling, J. M. (2021) · Fertility and Sterility · doi:10.1016/j.fertnstert.2020.12.033 · Cited by 83
Oguntuyo, K. Y., Stevens, C. S., Hung, C.-T., Ikegame, S., Acklin, J. A., Kowdle, S., Carmichael, J. C., Chiu, H.-P., Azarm, K. D., Haas, G. D., et al. (2021) · mBio · doi:10.1128/mbio.02492-20 · Cited by 73
Choi, Y. K., Cao, Y., Frank, M., Woo, H., Park, S., Yeom, M. S., Croll, T. I., Seok, C., & Im, W. (2021) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.0c01144 · Cited by 78
Diabetes and COVID-19; A Bidirectional Interplay
Kazakou, P., Lambadiari, V., Ikonomidis, I., Kountouri, A., Panagopoulos, G. N., Athanasopoulos, S., Korompoki, E., Kalomenidis, I., Dimopoulos, M. A., & Mitrakou, A. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.780663 · Cited by 90
Jamison, D. A., Narayanan, S. A., Trovão, N. S., Guarnieri, J. W., Topper, M. J., Moraes‐Vieira, P. M., Zaksas, V., Singh, K. K., Wurtele, E. S., & Beheshti, A. (2022) · European Journal of Human Genetics · doi:10.1038/s41431-022-01108-8 · Cited by 95
SARS-CoV-2 Spike triggers barrier dysfunction and vascular leak via integrins and TGF-β signaling
Biering, S. B., de Sousa, F. T. G., Tjang, L. V., Pahmeier, F., Zhu, C., Ruan, R., Blanc, S. F., Patel, T. S., Worthington, C. M., Glasner, D. R., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34910-5 · Cited by 92
Shah, H., Khan, M. S. H., Dhurandhar, N. V., & Hegde, V. (2021) · Acta Diabetologica · doi:10.1007/s00592-020-01636-z · Cited by 80
Fight against novel coronavirus: A perspective of medicinal chemists
Amin, S. A., & Jha, T. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112559 · Cited by 83
Hirotsu, Y., Mochizuki, H., & Omata, M. (2020) · Journal of Virological Methods · doi:10.1016/j.jviromet.2020.113926 · Cited by 80
The Impact of SARS-Cov-2 Virus Infection on the Endocrine System
Somasundaram, N. P., Ranathunga, I., Ratnasamy, V., Wijewickrama, P. S. A., Dissanayake, H. A., Yogendranathan, N., Gamage, K. K. K., de Silva, N. L., Sumanatilleke, M., Katulanda, P., et al. (2020) · Journal of the Endocrine Society · doi:10.1210/jendso/bvaa082 · Cited by 84
Maio, F. D., Cascio, E. L., Babini, G., Sali, M., Longa, S. D., Tilocca, B., Roncada, P., Arcovito, A., Sanguinetti, M., Scambia, G., et al. (2020) · Microbes and Infection · doi:10.1016/j.micinf.2020.08.006 · Cited by 80
Assessing Antigen Structural Integrity through Glycosylation Analysis of the SARS-CoV-2 Viral Spike
Brun, J., Vasiljević, S., Gangadharan, B., Hensen, M., Chandran, A. V., Hill, M. L., Kiappes, J. L., Dwek, R. A., Alonzi, D. S., Struwe, W. B., et al. (2021) · ACS Central Science · doi:10.1021/acscentsci.1c00058 · Cited by 92
A review on potential of natural products in the management of COVID-19
Chakravarti, R., Singh, R., Ghosh, A., Dey, D., Sharma, P., Ravichandiran, V., Roy, S., & Ghosh, D. (2021) · RSC Advances · doi:10.1039/d1ra00644d · Cited by 81
Chen, C., Boorla, V. S., Banerjee, D., Chowdhury, R., Cavener, V. S., Nissly, R. H., Gontu, A., Boyle, N. R., Vandegrift, K. J., Nair, M. S., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2106480118 · Cited by 81
COVID-19 in Human, Animal, and Environment: A Review
Swelum, A. A., Shafi, M. E., Albaqami, N. M., El‐Saadony, M. T., Elsify, A. M., Abdo, M., Taha, A. E.-S., Abdel‐Moneim, A. E., Al-Gabri, N. A., Almaiman, A. A., et al. (2020) · Frontiers in Veterinary Science · doi:10.3389/fvets.2020.00578 · Cited by 83
Increased small particle aerosol transmission of B.1.1.7 compared with SARS-CoV-2 lineage A in vivo
Port, J. R., Yinda, C. K., Avanzato, V. A., Schulz, J. E., Holbrook, M. G., van Doremalen, N., Shaia, C., Fischer, R. J., & Munster, V. J. (2022) · Nature Microbiology · doi:10.1038/s41564-021-01047-y · Cited by 77
Self-citationStructural dynamics in the evolution of SARS-CoV-2 spike glycoprotein
Calvaresi, V., Wrobel, A. G., Toporowska, J., Hammerschmid, D., Doores, K. J., Bradshaw, R. T., Parsons, R. B., Benton, D. J., Roustan, C., Reading, E., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36745-0 · Cited by 81
Tackling COVID-19 with neutralizing monoclonal antibodies
Corti, D., Purcell, L. A., Snell, G., & Veesler, D. (2021) · Cell · doi:10.1016/j.cell.2021.07.027 · Cited by 78
“All mAbs authorized or in development are directed to the RBD, which interacts with the target receptor angiotensin-converting enzyme 2 (ACE2) (Hoffmann et al., 2020; Letko et al., 2020; Walls et al., 2020b; Zhou et al., 2020).”
TINJAUAN PUSTAKA COVID-19: VIROLOGI, PATOGENESIS, DAN MANIFESTASI KLINIS
Fitriani, N. I. (2021) · Jurnal Medika Malahayati · doi:10.33024/jmm.v4i3.3174 · Cited by 78
Replication and single-cycle delivery of SARS-CoV-2 replicons
Ricardo-Lax, I., Luna, J. M., Thao, T. T. N., Pen, J. L., Yu, Y., Hoffmann, H.-H., Schneider, W. M., Razooky, B. S., Fernández-Martínez, J., Schmidt, F., et al. (2021) · Science · doi:10.1126/science.abj8430 · Cited by 80
A Systematic Review of COVID-19 and Myocarditis
Kariyanna, P. T., Sutarjono, B., Grewal, E., Singh, K. P., Aurora, L., Smith, L., Chandrakumar, H. P., Jayarangaiah, A., Goldman, S. A., Salifu, M. O., et al. (2020) · American Journal of Medical Case Reports · doi:10.12691/ajmcr-8-9-11 · Cited by 77
Role of the early secretory pathway in SARS-CoV-2 infection
Sicari, D., Chatziioannou, A. A., Koutsandreas, T., Sitia, R., & Chevet, É. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202006005 · Cited by 76
Analysis of ACE2 genetic variants in 131 Italian SARS-CoV-2-positive patients
Novelli, A., Biancolella, M., Borgiani, P., Cocciadiferro, D., Colona, V. L., D’Apice, M. R., Rogliani, P., Zaffina, S., Leonardis, F., Campana, A., et al. (2020) · Human Genomics · doi:10.1186/s40246-020-00279-z · Cited by 76
Bowen, J. E., Park, Y., Stewart, C., Brown, J. T., Sharkey, W. K., Walls, A. C., Joshi, A., Sprouse, K. R., McCallum, M., Tortorici, M. A., et al. (2022) · Science Immunology · doi:10.1126/sciimmunol.adf1421 · Cited by 81
Advances in the design and development of SARS-CoV-2 vaccines
Peng, X., Cheng, J., Gong, H., Yuan, M.-D., Zhao, X., Li, Z., & Wei, D. (2021) · Military Medical Research · doi:10.1186/s40779-021-00360-1 · Cited by 84
Case, J. B., Chen, R. E., Cao, L., Ying, B., Winkler, E. S., Johnson, M., Goreshnik, I., Pham, M. N., Shrihari, S., Kafai, N. M., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.06.008 · Cited by 73
Megremis, S., Walker, T. D. J., He, X. T., Ollier, W., Chinoy, H., Hampson, L., HAMPSON, I. N., & Lamb, J. A. (2020) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2020-217522 · Cited by 76
Baker, D., Amor, S., Kang, A. S., Schmierer, K., & Giovannoni, G. (2020) · Multiple Sclerosis and Related Disorders · doi:10.1016/j.msard.2020.102174 · Cited by 75
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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