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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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Walls, A. C., Park, Y.-J., Tortorici, M. A., Wall, A., McGuire, A. T., & Veesler, D. (2020) · doi:10.1101/2020.02.19.956581 · Cited by 8,586
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Lan, J., Ge, J., Yu, J., Shan, S., Zhou, H., Fan, S., Zhang, Q., Shi, X., Wang, Q., Zhang, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2180-5 · Cited by 5,983
The proximal origin of SARS-CoV-2
Andersen, K. G., Rambaut, A., Lipkin, W. I., Holmes, E. C., & Garry, R. F. (2020) · Nature Medicine · doi:10.1038/s41591-020-0820-9 · Cited by 5,081
Characteristics of SARS-CoV-2 and COVID-19
Hu, B., Guo, H., Zhou, P., & Shi, Z.-L. (2021) · Nature Reviews Microbiology · doi:10.1038/s41579-020-00459-7 · Cited by 5,291
Guo (2020) · doi:10.1186/s40779-020-00240-0 · Cited by 4,735
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
SARS-CoV-2 variants, spike mutations and immune escape
Harvey, W. T., Carabelli, A. M., Jackson, B., Gupta, R. K., Thomson, E. C., Harrison, E. M., Ludden, C., Reeve, R., Rambaut, A., COVID-19 Genomics UK (COG-UK) Consortium, et al. (2021) · Nature Reviews Microbiology · doi:10.1038/s41579-021-00573-0 · Cited by 3,528
Structural basis of receptor recognition by SARS-CoV-2
Shang, J., Ye, G., Shi, K., Wan, Y., Luo, C., Aihara, H., Geng, Q., Auerbach, A., & Li, F. (2020) · Nature · doi:10.1038/s41586-020-2179-y · Cited by 3,661
Coronavirus biology and replication: implications for SARS-CoV-2
V’kovski, P., Kratzel, A., Steiner, S., Stalder, H., & Thiel, V. (2020) · Nature Reviews Microbiology · doi:10.1038/s41579-020-00468-6 · Cited by 3,371
Cell entry mechanisms of SARS-CoV-2
Shang, J., Wan, Y., Luo, C., Ye, G., Geng, Q., Auerbach, A., & Li, F. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2003138117 · Cited by 3,142
Ziegler, C. G. K., Allon, S. J., Nyquist, S. K., Mbano, I. M., Miao, V. N., Tzouanas, C. N., Cao, Y., Yousif, A. S., Bals, J., Hauser, B. M., et al. (2020) · Cell · doi:10.1016/j.cell.2020.04.035 · Cited by 2,284
Monteil, V., Kwon, H., Prado, P., Hagelkrüys, A., Wimmer, R. A., Stahl, M., Leopoldi, A., Garreta, E., Hurtado del Pozo, C., Prosper, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.04.004 · Cited by 2,122
Starr, T. N., Greaney, A. J., Hilton, S. K., Ellis, D., Crawford, K. H. D., Dingens, A. S., Navarro, M. J., Bowen, J. E., Tortorici, M. A., Walls, A. C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.012 · Cited by 1,956
Huang, Y., Yang, C., Xu, X.-F., Xü, W., & Liu, S. (2020) · Acta Pharmacologica Sinica · doi:10.1038/s41401-020-0485-4 · Cited by 2,288
COVID-19 pathophysiology: A review
Yuki, K., Shibamura‐Fujiogi, M., & Koutsogiannaki, S. (2020) · Clinical Immunology · doi:10.1016/j.clim.2020.108427 · Cited by 2,286
SARS-CoV-2 vaccines in development
Krammer, F. (2020) · Nature · doi:10.1038/s41586-020-2798-3 · Cited by 2,098
Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2349-y · Cited by 1,885
Susceptibility of ferrets, cats, dogs, and other domesticated animals to SARS–coronavirus 2
Shi, J., Wen, Z., Zhong, G., Yang, H., Wang, C., Huang, B., Liu, R., He, X., Shuai, L., Sun, Z., et al. (2020) · Science · doi:10.1126/science.abb7015 · Cited by 1,952
A serological assay to detect SARS-CoV-2 seroconversion in humans
Amanat, F., Stadlbauer, D., Strohmeier, S., Nguyen, T. H. O., Chromikova, V., McMahon, M., Jiang, K., Arunkumar, G. A., Jurczyszak, D., Polanco, J., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-0913-5 · Cited by 1,769
Site-specific glycan analysis of the SARS-CoV-2 spike
Watanabe, Y., Allen, J. D., Wrapp, D., McLellan, J. S., & Crispin, M. (2020) · Science · doi:10.1126/science.abb9983 · Cited by 1,538
Ciotti, M., Ciccozzi, M., Terrinoni, A., Jiang, W.-C., Wang, C.-B., & Bernardini, S. (2020) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408363.2020.1783198 · Cited by 1,744
A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV
Yuan, M., Wu, N. C., Zhu, X., Lee, C.-C. D., So, R. T. Y., Lv, H., Mok, C. K. P., & Wilson, I. A. (2020) · Science · doi:10.1126/science.abb7269 · Cited by 1,429
The Impact of Mutations in SARS-CoV-2 Spike on Viral Infectivity and Antigenicity
Li, Q., Wu, J., Nie, J., Zhang, L., Hao, H., Liu, S., Zhao, C., Zhang, Q., Liu, H., Nie, L., et al. (2020) · Cell · doi:10.1016/j.cell.2020.07.012 · Cited by 1,420
Return of the Coronavirus: 2019-nCoV
Gralinski, L. E., & Menachery, V. D. (2020) · Viruses · doi:10.3390/v12020135 · Cited by 1,348
Seasonality of Respiratory Viral Infections
Moriyama, M., Hugentobler, W., & Iwasaki, A. (2020) · Annual Review of Virology · doi:10.1146/annurev-virology-012420-022445 · Cited by 1,344
Robust neutralizing antibodies to SARS-CoV-2 infection persist for months
Wajnberg, A., Amanat, F., Firpo, A., Altman, D. R., Bailey, M. J., Mansour, M., McMahon, M., Meade, P., Mendu, D. R., Muellers, K., et al. (2020) · Science · doi:10.1126/science.abd7728 · Cited by 1,195
Immune correlates analysis of the mRNA-1273 COVID-19 vaccine efficacy clinical trial
Gilbert, P. B., Montefiori, D. C., McDermott, A. B., Fong, Y., Benkeser, D., Deng, W., Zhou, H., Houchens, C. R., Martins, K., Jayashankar, L., et al. (2022) · Science · doi:10.1126/science.abm3425 · Cited by 1,137
SARS-CoV-2 Vaccines: Status Report
Amanat, F., & Krammer, F. (2020) · Immunity · doi:10.1016/j.immuni.2020.03.007 · Cited by 1,120
Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant
Yurkovetskiy, L., Wang, X., Pascal, K. E., Tomkins-Tinch, C., Nyalile, T. P., Wang, Y., Baum, A., Diehl, W. E., Dauphin, A., Carbone, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.032 · Cited by 1,025
Ahmed, S. F., Quadeer, A. A., & McKay, M. R. (2020) · Viruses · doi:10.3390/v12030254 · Cited by 1,128
N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2
McCallum, M., De Marco, A., Lempp, F. A., Tortorici, M. A., Pinto, D., Walls, A. C., Beltramello, M., Chen, A., Liu, Z., Zatta, F., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.028 · Cited by 901
“SARS-CoV-2 infects host cells through attachment of the viral transmembrane spike (S) glycoprotein to angiotensin-converting enzyme 2 (ACE2) followed by fusion of the viral and host membranes (Letko et al., 2020; Walls et al., 2020b).”
Randhawa, G. S., Soltysiak, M. P. M., El Roz, H., de Souza, C. P. E., Hill, K. A., & Kari, L. (2020) · PLOS ONE · doi:10.1371/journal.pone.0232391 · Cited by 1,023
Greaney, A. J., Starr, T. N., Gilchuk, P., Zost, S. J., Binshtein, E., Loes, A. N., Hilton, S. K., Huddleston, J., Eguia, R., Crawford, K. H. D., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2020.11.007 · Cited by 1,016
Chen, R. E., Zhang, X., Case, J. B., Winkler, E. S., Liu, Y., VanBlargan, L. A., Liu, J., Errico, J. M., Xie, X., Suryadevara, N., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01294-w · Cited by 881
TMPRSS2 and TMPRSS4 promote SARS-CoV-2 infection of human small intestinal enterocytes
Zang, R., Castro, M. F. G., McCune, B. T., Zeng, Q., Rothlauf, P. W., Sonnek, N. M., Liu, Z., Brulois, K. F., Wang, X., Greenberg, H. B., et al. (2020) · Science Immunology · doi:10.1126/sciimmunol.abc3582 · Cited by 982
Eastman, R. T., Roth, J. S., Brimacombe, K. R., Simeonov, A. M., Shen, M., Patnaik, S., & Hall, M. D. (2020) · ACS Central Science · doi:10.1021/acscentsci.0c00489 · Cited by 963
Yang, Y., Islam, M. S., Wang, J., Li, Y., & Chen, X. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.45538 · Cited by 975
Persistence of serum and saliva antibody responses to SARS-CoV-2 spike antigens in COVID-19 patients
Isho, B., Abe, K. T., Zuo, M., Jamal, A. J., Rathod, B., Wang, J. H., Li, Z., Chao, G., Rojas, O. L., Bang, Y. M., et al. (2020) · Science Immunology · doi:10.1126/sciimmunol.abe5511 · Cited by 822
SARS-CoV-2: Structure, Biology, and Structure-Based Therapeutics Development
Wang, M.-Y., Zhao, R., Gao, L.-J., Gao, X.-F., Wang, D.-P., & Cao, J.-M. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.587269 · Cited by 874
Lin, L., Lu, L., Cao, W., & Li, T. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1746199 · Cited by 922
Winkler, E. S., Bailey, A. L., Kafai, N. M., Nair, S., McCune, B. T., Yu, J., Fox, J. M., Chen, R. E., Earnest, J. T., Keeler, S. P., et al. (2020) · Nature Immunology · doi:10.1038/s41590-020-0778-2 · Cited by 901
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. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.01.014 · Cited by 725
“During viral entry into cells, the receptor-binding domain (RBD) of S1 engages the primary receptor, human angiotensin converting enzyme 2 (hACE2) (Letko et al., 2020).”
BackgroundThe presence of SARS‐CoV‐2 RNA in the feces of COVID‐19 patients
Chen, Y., Chen, L., Deng, Q., Zhang, G., Wu, K., Ni, L., Yang, Y., Liu, B., Wang, W., Wei, C., et al. (2020) · Journal of Medical Virology · doi:10.1002/jmv.25825 · Cited by 839
COVID-19: what has been learned and to be learned about the novel coronavirus disease
Ye, Y., Lagniton, P. N. P., Ye, S., Li, E., & Xu, R.-H. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.45134 · Cited by 859
Coronavirus Diseases (COVID-19) Current Status and Future Perspectives: A Narrative Review
Gennaro, F. D., Pizzol, D., Marotta, C., Antunes, M., Racalbuto, V., Veronese, N., & Smith, L. (2020) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph17082690 · Cited by 882
COVID-19 and diabetes: Knowledge in progress
Hussain, A., Bhowmik, B., & Moreira, N. C. D. V. (2020) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2020.108142 · Cited by 836
Crawford, K. H. D., Eguia, R. T., Dingens, A. S., Loes, A. N., Malone, K. D., Wolf, C. R., Chu, H. Y., Tortorici, M. A., Veesler, D., Murphy, M., et al. (2020) · Viruses · doi:10.3390/v12050513 · Cited by 744
COVID-19: Current understanding of its Pathophysiology, Clinical presentation and Treatment
Parasher, A. (2020) · Postgraduate Medical Journal · doi:10.1136/postgradmedj-2020-138577 · Cited by 810
Immune response, inflammation, and the clinical spectrum of COVID-19
García, L. F. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01441 · Cited by 739
Structural basis of a shared antibody response to SARS-CoV-2
Yuan, M., Liu, H., Wu, N. C., Lee, C.-C. D., Zhu, X., Zhao, F., Huang, D., Yu, W., Hua, Y., Tien, H., et al. (2020) · Science · doi:10.1126/science.abd2321 · Cited by 589
Hu, Y., Sun, J., Dai, Z., Deng, H., Li, X., Huang, Q., Wu, Y., Sun, L., & Xu, Y. (2020) · Journal of Clinical Virology · doi:10.1016/j.jcv.2020.104371 · Cited by 725
SARS-CoV-2 Omicron virus causes attenuated disease in mice and hamsters
Halfmann, P., Iida, S., Iwatsuki‐Horimoto, K., Maemura, T., Kiso, M., Scheaffer, S. M., Darling, T. L., Joshi, A., Loeber, S. J., Singh, G., et al. (2022) · Nature · doi:10.1038/s41586-022-04441-6 · Cited by 664
Akhmerov, A., & Marbán, E. (2020) · Circulation Research · doi:10.1161/circresaha.120.317055 · Cited by 700
Liu, Z., Xiao, X., Wei, X., Li, J., Yang, J., Tan, H., Zhu, J., Zhang, Q., Wu, J., & Liu, L. (2020) · Journal of Medical Virology · doi:10.1002/jmv.25726 · Cited by 697
A Mouse-Adapted SARS-CoV-2 Induces Acute Lung Injury and Mortality in Standard Laboratory Mice
Leist, S. R., Dinnon, K. H., Schäfer, A., Tse, L. V., Okuda, K., Hou, Y. J., West, A., Edwards, C. E., Sanders, W., Fritch, E. J., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.050 · Cited by 613
Engineering human ACE2 to optimize binding to the spike protein of SARS coronavirus 2
Chan, K. K., Dorosky, D. E., Sharma, P. A., Abbasi, S. A., Dye, J. M., Kranz, D. M., Herbert, A. S., & Procko, E. (2020) · Science · doi:10.1126/science.abc0870 · Cited by 623
Damas, J., Hughes, G. M., Keough, K. C., Painter, C. A., Persky, N. S., Corbo, M., Hiller, M., Koepfli, K.-P., Pfenning, A. R., Zhao, H., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2010146117 · Cited by 633
Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms
Tortorici, M. A., Beltramello, M., Lempp, F. A., Pinto, D., Dang, H. V., Rosen, L. E., McCallum, M., Bowen, J., Minola, A., Jaconi, S., et al. (2020) · Science · doi:10.1126/science.abe3354 · Cited by 510
Walls, A. C., Fiala, B., Schäfer, A., Wrenn, S., Pham, M. N., Murphy, M., Tse, L. V., Shehata, L., O’Connor, M. A., Chen, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.043 · Cited by 532
Sardu, C., Gambardella, J., Morelli, M. B., Wang, X., Marfella, R., & Santulli, G. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9051417 · Cited by 610
A Single-Dose Intranasal ChAd Vaccine Protects Upper and Lower Respiratory Tracts against SARS-CoV-2
Hassan, A. O., Kafai, N. M., Dmitriev, I. P., Fox, J. M., Smith, B. K., Harvey, I. B., Chen, R. E., Winkler, E. S., Wessel, A. W., Case, J. B., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.026 · Cited by 571
Acter, T., Uddin, N., Das, J., Akhter, A., Choudhury, T. R., & Kim, S. (2020) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2020.138996 · Cited by 600
Pathogenesis of SARS-CoV-2 in Transgenic Mice Expressing Human Angiotensin-Converting Enzyme 2
Jiang, R.-D., Liu, M.-Q., Chen, Y., Shan, C., Zhou, Y.-W., Shen, X.-R., Li, Q., Zhang, L., Zhu, Y., Si, H.-R., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.027 · Cited by 548
Bat-borne virus diversity, spillover and emergence
Letko, M. C., Seifert, S. N., Olival, K. J., Plowright, R. K., & Munster, V. J. (2020) · Nature Reviews Microbiology · doi:10.1038/s41579-020-0394-z · Cited by 583
Self-citationSARS-CoV-2 spike D614G change enhances replication and transmission
Zhou, B., Thao, T. T. N., Hoffmann, D., Taddeo, A., Ebert, N., Labroussaa, F., Pohlmann, A., King, J., Steiner, S., Kelly, J. N., et al. (2021) · Nature · doi:10.1038/s41586-021-03361-1 · Cited by 538
mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection
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) · Science · doi:10.1126/science.abg9175 · Cited by 557
Aerosol transmission of SARS-CoV-2? Evidence, prevention and control
Tang, S., Mao, Y., Jones, R. M., Tan, Q., Ji, J. S., Li, N., Shen, J., Lv, Y., Pan, L., Ding, P., et al. (2020) · Environment International · doi:10.1016/j.envint.2020.106039 · Cited by 552
Wrobel, A. G., Benton, D. J., Xu, P., Roustan, C., Martin, S. R., Rosenthal, P. B., Skehel, J. J., & Gamblin, S. J. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0468-7 · Cited by 544
Prevalence and impact of diabetes among people infected with SARS-CoV-2
Fadini, G. P., Morieri, M. L., Longato, E., & Avogaro, A. (2020) · Journal of Endocrinological Investigation · doi:10.1007/s40618-020-01236-2 · Cited by 550
A systematic review of SARS-CoV-2 vaccine candidates
Dong, Y., Dai, T., Wei, Y., Zhang, L., Zheng, M., & Zhou, F. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00352-y · Cited by 555
ACE2 Expression in Kidney and Testis May Cause Kidney and Testis Infection in COVID-19 Patients
Fan, C., Lu, W., Ding, Y., Lu, W., & Wang, J. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2020.563893 · Cited by 564
Trials of anti-tumour necrosis factor therapy for COVID-19 are urgently needed
Feldmann, M., Maini, R. N., Woody, J. N., Holgate, S. T., Winter, G., Rowland, M. J., Richards, D. B., & Hussell, T. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30858-8 · Cited by 537
The Impact of COVID-19 Disease on Platelets and Coagulation
Wool, G. D., & Miller, J. L. (2020) · Pathobiology · doi:10.1159/000512007 · Cited by 554
Bat coronaviruses related to SARS-CoV-2 and infectious for human cells
Temmam, S., Vongphayloth, K., Baquero, E., Munier, S., Bonomi, M., Regnault, B., Douangboubpha, B., Karami, Y., Chrétien, D., Sanamxay, D., et al. (2022) · Nature · doi:10.1038/s41586-022-04532-4 · Cited by 553
Genome-wide CRISPR Screens Reveal Host Factors Critical for SARS-CoV-2 Infection
Wei, J., Alfajaro, M. M., DeWeirdt, P. C., Hanna, R. E., Lu-Culligan, W. J., Cai, W. L., Strine, M. S., Zhang, S.-M., Graziano, V. R., Schmitz, C. O., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.028 · Cited by 572
SARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape
Starr, T. N., Czudnochowski, N., Liu, Z., Zatta, F., Park, Y., Addetia, A., Pinto, D., Beltramello, M., Hernandez, P., Greaney, A. J., et al. (2021) · Nature · doi:10.1038/s41586-021-03807-6 · Cited by 503
Davidson, A. D., Williamson, M. K., Lewis, S., Shoemark, D., Carroll, M. W., Heesom, K. J., Zambon, M., Ellis, J., Lewis, P. A., Hiscox, J. A., et al. (2020) · Genome Medicine · doi:10.1186/s13073-020-00763-0 · Cited by 457
A comprehensive review of COVID-19 characteristics
Esakandari, H., Nabi‐Afjadi, M., Afjadi, J. F., Farahmandian, N., Miresmaeili, S. M., & Bahreini, E. (2020) · Biological Procedures Online · doi:10.1186/s12575-020-00128-2 · Cited by 511
Park, S. E. (2020) · Korean Journal of Pediatrics · doi:10.3345/cep.2020.00493 · Cited by 527
COVID-19 Coronavirus Vaccine Design Using Reverse Vaccinology and Machine Learning
Ong, E., Wong, M. U., Huffman, A., & He, Y. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01581 · Cited by 499
SARS-CoV-2 infects cells after viral entry via clathrin-mediated endocytosis
Bayati, A., Kumar, R., Francis, V., & McPherson, P. S. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100306 · Cited by 499
Petabase-scale sequence alignment catalyses viral discovery
Edgar, R. C., Taylor, B., Lin, V., Altman, T., Barbera, P., Meleshko, D., Lohr, D., Novakovsky, G., Buchfink, B., Al-Shayeb, B., et al. (2022) · Nature · doi:10.1038/s41586-021-04332-2 · Cited by 495
Malik, Y. S., Sircar, S., Bhat, S., Sharun, K., Dhama, K., Dadar, M., Tiwari, R., & Chaicumpa, W. (2020) · Veterinary Quarterly · doi:10.1080/01652176.2020.1727993 · Cited by 508
A SARS-CoV-2 Infection Model in Mice Demonstrates Protection by Neutralizing Antibodies
Hassan, A. O., Case, J. B., Winkler, E. S., Thackray, L. B., Kafai, N. M., Bailey, A. L., McCune, B. T., Fox, J. M., Chen, R. E., Alsoussi, W. B., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.011 · Cited by 482
Jaimes, J. A., André, N. M., Chappie, J. S., Millet, J. K., & Whittaker, G. R. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.04.009 · Cited by 492
Case, J. B., Rothlauf, P. W., Chen, R. E., Liu, Z., Zhao, H., Kim, A. S., Bloyet, L.-M., Zeng, Q., Tahan, S., Droit, L., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.06.021 · Cited by 410
Type I Interferon Susceptibility Distinguishes SARS-CoV-2 from SARS-CoV
Lokugamage, K. G., Hage, A., de Vries, M., Valero-Jimenez, A. M., Schindewolf, C., Dittmann, M., Rajsbaum, R., & Menachery, V. D. (2020) · Journal of Virology · doi:10.1128/jvi.01410-20 · Cited by 503
ACE2: The Major Cell Entry Receptor for SARS-CoV-2
Scialo, F., Daniele, A., Amato, F., Pastore, L., Matera, M. G., Cazzola, M., Castaldo, G., & Bianco, A. (2020) · Lung · doi:10.1007/s00408-020-00408-4 · Cited by 481
Overview of Immune Response During SARS-CoV-2 Infection: Lessons From the Past
Shah, V. K., Firmal, P., Alam, A., Ganguly, D., & Chattopadhyay, S. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01949 · Cited by 476
SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern
McCallum, M., Bassi, J., De Marco, A., Chen, A., Walls, A. C., Di Iulio, J., Tortorici, M. A., Navarro, M.-J., Silacci-Fregni, C., Saliba, C., et al. (2021) · Science · doi:10.1126/science.abi7994 · Cited by 412
Syncytia formation by SARS‐CoV‐2‐infected cells
Buchrieser, J., Dufloo, J., Hubert, M., Monel, B., Planas, D., Rajah, M. M., Planchais, C., Porrot, F., Guivel‐Benhassine, F., Van der Werf, S., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2020106267 · Cited by 462
Sama, I. E., Ravera, A., Santema, B. T., van Goor, H., ter Maaten, J. M., Cleland, J. G. F., Rienstra, M., Friedrich, A. W., Samani, N. J., Ng, L. L., et al. (2020) · European Heart Journal · doi:10.1093/eurheartj/ehaa373 · Cited by 460
Role of Structural and Non-Structural Proteins and Therapeutic Targets of SARS-CoV-2 for COVID-19
Yadav, R., Chaudhary, J. K., Jain, N. K., Chaudhary, P. K., Khanra, S., Dhamija, P., Sharma, A., Kumar, A., & Handu, S. S. (2021) · Cells · doi:10.3390/cells10040821 · Cited by 486
Natural product-derived phytochemicals as potential agents against coronaviruses: A review
Mani, J. S., Johnson, J. B., Steel, J. C., Broszczak, D. A., Neilsen, P. M., Walsh, K. B., & Naiker, M. (2020) · Virus Research · doi:10.1016/j.virusres.2020.197989 · Cited by 451
The hallmarks of COVID-19 disease
Tang, D., Comish, P. B., & Kang, R. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008536 · Cited by 467
Si, L., Bai, H., Rodas, M., Cao, W., Oh, C. Y., Jiang, A., Moller, R., Hoagland, D., Oishi, K., Horiuchi, S., et al. (2021) · Nature Biomedical Engineering · doi:10.1038/s41551-021-00718-9 · Cited by 440
“The ability of SARS-CoV-2pp to efficiently infect human airway epithelial cells on-chip is consistent with our finding that these highly differentiated lung cells express high levels of its ACE2 receptor as well as TMPRSS2 (Fig.”
InfluentialSeydoux, E., Homad, L. J., MacCamy, A. J., Parks, K. R., Hurlburt, N. K., Jennewein, M. F., Akins, N. R., Stuart, A. B., Wan, Y.-H., Feng, J., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.06.001 · Cited by 364
“Like SARS-CoV, SARS-CoV-2 utilizes angiotensin-converting enzyme 2 (ACE2) as an entry receptor binding with nM affinity (Li et al., 2003; Walls et al., 2020; Wrapp et al., 2020; Hoffmann et al., 2020; Letko et al., 2020; Ou et al., 2020).”
The first 12 months of COVID-19: a timeline of immunological insights
Carvalho, T., Krammer, F., & Iwasaki, A. (2021) · Nature reviews. Immunology · doi:10.1038/s41577-021-00522-1 · Cited by 483
Mapping mutations to the SARS-CoV-2 RBD that escape binding by different classes of antibodies
Greaney, A. J., Starr, T. N., Barnes, C. O., Weisblum, Y., Schmidt, F., Caskey, M., Gaebler, C., Cho, A., Agudelo, M., Finkin, S., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24435-8 · Cited by 433
COVID-19 in Children, Pregnancy and Neonates: A Review of Epidemiologic and Clinical Features
Zimmermann, P., & Curtis, N. C. (2020) · The Pediatric Infectious Disease Journal · doi:10.1097/inf.0000000000002700 · Cited by 456
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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