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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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“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
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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“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
“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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Israelow, B., Song, E., Mao, T., Lu, P., Meir, A., Liu, F., Alfajaro, M. M., Wei, J., Dong, H., Homer, R. J., et al. (2020) · Journal of Experimental Medicine · doi:10.1084/jem.20201241 · Cited by 415
Li, J.-Y., You, Z., Wang, Q., Zhou, Z., Qiu, Y., Luo, R., & Ge, X. (2020) · Microbes and Infection · doi:10.1016/j.micinf.2020.02.002 · Cited by 450
Free fatty acid binding pocket in the locked structure of SARS-CoV-2 spike protein
Toelzer, C., Gupta, K., Yadav, S. K. N., Borucu, U., Davidson, A. D., Williamson, M. K., Shoemark, D. K., Garzoni, F., Staufer, O., Milligan, R., et al. (2020) · Science · doi:10.1126/science.abd3255 · Cited by 427
Can N95 Respirators Be Reused after Disinfection? How Many Times?
Liao, L., Wang, X., Zhao, M., Yu, X., Wang, H., Wang, Q., Chu, S., & Cui, Y. (2020) · ACS Nano · doi:10.1021/acsnano.0c03597 · Cited by 446
Katsura, H., Sontake, V., Tata, A., Kobayashi, Y., Edwards, C. E., Heaton, B. E., Konkimalla, A., Asakura, T., Mikami, Y., Fritch, E. J., et al. (2020) · Cell Stem Cell · doi:10.1016/j.stem.2020.10.005 · Cited by 416
After the pandemic: perspectives on the future trajectory of COVID-19
Telenti, A., Arvin, A. M., Corey, L., Corti, D., Diamond, M., García‐Sastre, A., Garry, R. F., Holmes, E. C., Pang, P. S., & Virgin, H. W. (2021) · Nature · doi:10.1038/s41586-021-03792-w · Cited by 450
Genetic Screens Identify Host Factors for SARS-CoV-2 and Common Cold Coronaviruses
Wang, R., Simoneau, C. R., Kulsuptrakul, J., Bouhaddou, M., Travisano, K. A., Hayashi, J. M., Carlson-Stevermer, J., Zengel, J. R., Richards, C. M., Fozouni, P., et al. (2020) · Cell · doi:10.1016/j.cell.2020.12.004 · Cited by 417
Mosaic nanoparticles elicit cross-reactive immune responses to zoonotic coronaviruses in mice
Cohen, A. A., Gnanapragasam, P. N. P., Lee, Y. E., Hoffman, P. R., Ou, S. K.-H., Kakutani, L. M., Keeffe, J. R., Wu, H., Howarth, M. R., West, A. P., et al. (2021) · Science · doi:10.1126/science.abf6840 · Cited by 396
Duan, L., Zheng, Q., Zhang, H., Niu, Y., Lou, Y., & Wang, H. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.576622 · Cited by 417
Cross-reactive Antibody Response between SARS-CoV-2 and SARS-CoV Infections
Lv, H., Wu, N. C., Tsang, O. T.-Y., Yuan, M., Perera, R. A. P. M., Leung, W.-S., So, R. T. Y., Chan, J. M. C., Yip, G. K., Chik, T. S., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107725 · Cited by 406
Emergence of SARS-CoV-2 through recombination and strong purifying selection
Li, X., Giorgi, E. E., Marichannegowda, M. H., Foley, B. T., Xiao, C., Kong, X., Chen, Y., Gnanakaran, S., Korber, B., & Gao, F. (2020) · Science Advances · doi:10.1126/sciadv.abb9153 · Cited by 407
RNA Drugs and RNA Targets for Small Molecules: Principles, Progress, and Challenges
Yu, A., Choi, Y. H., & Tu, M. (2020) · Pharmacological Reviews · doi:10.1124/pr.120.019554 · Cited by 421
Genome-Scale Identification of SARS-CoV-2 and Pan-coronavirus Host Factor Networks
Schneider, W. M., Luna, J. M., Hoffmann, H.-H., Rivera, F. J. S., Leal, A. A., Ashbrook, A. W., Pen, J. L., Ricardo-Lax, I., Michailidis, E., Peace, A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.12.006 · Cited by 397
Wang, D., Yin, Y., Hu, C., Liu, X., Zhang, X., Zhou, S., Jian, M., Xu, H., Prowle, J., Hu, B., et al. (2020) · Critical Care · doi:10.1186/s13054-020-02895-6 · Cited by 397
Diarrhoea may be underestimated: a missing link in 2019 novel coronavirus
Liang, W., Feng, Z., Rao, S., Xiao, C., Xue, X., Lin, Z., Zhang, Q., & Qi, W. (2020) · Gut · doi:10.1136/gutjnl-2020-320832 · Cited by 397
Pathophysiological mechanisms of liver injury in COVID‐19
Nardo, A. D., Schneeweiss‐Gleixner, M., Bakail, M., Dixon, E. D., Lax, S., & Trauner, M. (2020) · Liver International · doi:10.1111/liv.14730 · Cited by 400
Poh, C. M., Carissimo, G., Wang, B., Amrun, S. N., Lee, C. Y., Chee, R. S., Fong, S., Yeo, N. K., Lee, W.-H., Torres‐Ruesta, A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16638-2 · Cited by 379
COVID-19 pandemic—a focused review for clinicians
Çevik, M., Bamford, C., & Ho, A. Y. W. (2020) · Clinical Microbiology and Infection · doi:10.1016/j.cmi.2020.04.023 · Cited by 406
Molecular Diagnosis of COVID-19: Challenges and Research Needs
Feng, W., Newbigging, A. M., Le, C., Pang, B., Peng, H., Cao, Y., Wu, J., Abbas, G., Song, J., Wang, D., et al. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c02060 · Cited by 390
Hasöksüz, M., Kılıç, S., & Saraç, F. (2020) · TURKISH JOURNAL OF MEDICAL SCIENCES · doi:10.3906/sag-2004-127 · Cited by 417
Tackling COVID-19 with neutralizing monoclonal antibodies
Corti, D., Purcell, L. A., Snell, G., & Veesler, D. (2021) · Cell · doi:10.1016/j.cell.2021.05.005 · Cited by 386
Luan, J., Lu, Y., Jin, X., & Zhang, L. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.03.047 · Cited by 383
Immunopathological characteristics of coronavirus disease 2019 cases in Guangzhou, China
Shi, Y., Tan, M., Chen, X., Liu, Y., Huang, J., Ou, J., & 邓西龙 (2020) · Immunology · doi:10.1111/imm.13223 · Cited by 376
Zhao, H., Lu, L., Peng, Z., Chen, L.-L., Meng, X., Zhang, C., Ip, J. D., Chan, W.-M., Chu, A. W.-H., Chan, K.-H., et al. (2022) · Emerging Microbes & Infections · doi:10.1080/22221751.2021.2023329 · Cited by 413
COVID-19: breaking down a global health crisis
Mallah, S. I., Ghorab, O. K. H. A., Al-Salmi, S., Abdellatif, O. S., Tharmaratnam, T., Iskandar, M. M. A., Sefen, J. A. N., Sidhu, P., Atallah, B., El-Lababidi, R. M., et al. (2021) · Annals of Clinical Microbiology and Antimicrobials · doi:10.1186/s12941-021-00438-7 · Cited by 401
Schäfer, A., Muecksch, F., Lorenzi, J. C. C., Leist, S. R., Cipolla, M., Bournazos, S., Schmidt, F., Maison, R. M., Gazumyan, A., Martinez, D. R., et al. (2021) · Journal of Experimental Medicine · doi:10.1084/jem.20201993 · Cited by 305
SARS-CoV-2 genomic variations associated with mortality rate of COVID-19
Toyoshima, Y., Nemoto, K., Matsumoto, S., Nakamura, Y., & Kiyotani, K. (2020) · Journal of Human Genetics · doi:10.1038/s10038-020-0808-9 · Cited by 351
Muralidar, S., Ambi, S. V., Sekaran, S., & Krishnan, U. M. (2020) · Biochimie · doi:10.1016/j.biochi.2020.09.018 · Cited by 384
Immune-mediated approaches against COVID-19
Florindo, H. F., Kleiner, R., Vaskovich‐Koubi, D., Acúrcio, R. C., Carreira, B., Yeini, E., Tiram, G., Liubomirski, Y., & Satchi‐Fainaro, R. (2020) · Nature Nanotechnology · doi:10.1038/s41565-020-0732-3 · Cited by 356
Unadjuvanted intranasal spike vaccine elicits protective mucosal immunity against sarbecoviruses
Mao, T., Israelow, B., Peña-Hernández, M. A., Suberi, A., Zhou, L., Luyten, S., Reschke, M., Dong, H., Homer, R., Saltzman, W. M., et al. (2022) · Science · doi:10.1126/science.abo2523 · Cited by 356
Erratum To: 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. (2021) · The EMBO Journal · doi:10.15252/embj.2020107405 · Cited by 330
Racial Disparities-Associated COVID-19 Mortality among Minority Populations in the US
Alcendor, D. J. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9082442 · Cited by 348
Extra-respiratory manifestations of COVID-19
Lai, C., Ko, W., Lee, P., Jean, S., & Hsueh, P. (2020) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2020.106024 · Cited by 336
Broad and potent activity against SARS-like viruses by an engineered human monoclonal antibody
Rappazzo, C. G., Tse, L. V., Kaku, C. I., Wrapp, D., Sakharkar, M., Huang, D., Deveau, L. M., Yockachonis, T. J., Herbert, A. S., Battles, M. B., et al. (2021) · Science · doi:10.1126/science.abf4830 · Cited by 307
Han, Y., Zhang, H., Mu, S., Wei, W., Jin, C., Tong, C., Song, Z., Zha, Y., Xue, Y., & Gu, G. (2020) · Aging · doi:10.18632/aging.103372 · Cited by 315
Wang, Y., Liu, M., & Gao, J. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2008209117 · Cited by 307
ACE2: Evidence of role as entry receptor for SARS-CoV-2 and implications in comorbidities
Cuervo, N. Z., & Grandvaux, N. (2020) · eLife · doi:10.7554/elife.61390 · Cited by 313
Clinical Significance of a High SARS-CoV-2 Viral Load in the Saliva
Yoon, J. G., Yoon, J. H., Song, J. Y., Yoon, S., Lim, C. S., Cheong, H. J., Noh, J. Y., Cheong, H. J., & Kim, W. J. (2020) · Journal of Korean Medical Science · doi:10.3346/jkms.2020.35.e195 · Cited by 311
Autoinflammatory and autoimmune conditions at the crossroad of COVID-19
Rodríguez, Y., Novelli, L., Rojas, M., Santis, M. D., Acosta‐Ampudia, Y., Monsalve, D. M., Ramírez-Santana, C., Costanzo, A., Ridgway, W. M., Ansari, A. A., et al. (2020) · Journal of Autoimmunity · doi:10.1016/j.jaut.2020.102506 · Cited by 319
The COVID-19 pandemic face mask waste: A blooming threat to the marine environment
Dharmaraj, S., Ashokkumar, V., Hariharan, S., Manibharathi, A., Show, P. L., Chong, C. T., & Ngamcharussrivichai, C. (2021) · Chemosphere · doi:10.1016/j.chemosphere.2021.129601 · Cited by 316
Bryche, B., Deliot, A. S.-A., Murri, S., Lacôte, S., Pulido, C., Gouilh, M. A., Lesellier, S., Servat, A., Wasniewski, M., Meyer, E. P., et al. (2020) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2020.06.032 · Cited by 306
Zhang, H., Li, H., Lyu, J., Li, W., Li, W., Wu, G., Lyu, J., & Dai, Z.-M. (2020) · International Journal of Infectious Diseases · doi:10.1016/j.ijid.2020.04.027 · Cited by 305
K18-hACE2 mice develop respiratory disease resembling severe COVID-19
Yinda, C. K., Port, J. R., Bushmaker, T., Donkor, I. O., Purushotham, J. N., Avanzato, V. A., Fischer, R. J., Schulz, J. E., Holbrook, M. G., Hebner, M. J., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009195 · Cited by 288
Self-citationHuman ACE2 receptor polymorphisms and altered susceptibility to SARS-CoV-2
Suryamohan, K., Diwanji, D. C., Stawiski, E. W., Gupta, R. K., Miersch, S., Liu, J., Chen, C., Jiang, Y.-P., Fellouse, F. A., Sathirapongsasuti, J. F., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02030-3 · Cited by 306
Zhang, C., Zheng, W. H., Huang, X., Bell, E. W., Zhou, X., & Zhang, Y. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00129 · Cited by 301
Detection of SARS-CoV-2 in Human Retinal Biopsies of Deceased COVID-19 Patients
Casagrande, M. K., Fitzek, A., Püschel, K., Aleshcheva, G., Schultheiß, H., Berneking, L., Spitzer, M. S., & Schultheiß, M. (2020) · Ocular Immunology and Inflammation · doi:10.1080/09273948.2020.1770301 · Cited by 295
Hasan, A., Paray, B. A., Hussain, A., Qadir, F. A., Attar, F., Aziz, F. M., Sharifi, M., Derakhshankhah, H., Rasti, B., Mehrabi, M., et al. (2021) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1754293 · Cited by 293
Alanagreh, L., Alzoughool, F., & Atoum, M. F. M. (2020) · Pathogens · doi:10.3390/pathogens9050331 · Cited by 315
Genetic and structural basis for SARS-CoV-2 variant neutralization by a two-antibody cocktail
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Fodoulian, L., Tuberosa, J., Rossier, D., Boillat, M., Kan, C., Pauli, V., Egervari, K., Lobrinus, J. A., Landis, B. N., Carleton, A., et al. (2020) · doi:10.1101/2020.03.31.013268 · Cited by 286
Molecular basis of immune evasion by the Delta and Kappa SARS-CoV-2 variants
McCallum, M., Walls, A. C., Sprouse, K. R., Bowen, J. E., Rosen, L. E., Dang, H. V., Marco, A. D., Franko, N., Tilles, S. W., Logue, J. K., et al. (2021) · Science · doi:10.1126/science.abl8506 · Cited by 280
Leung, J. M., Niikura, M., Yang, C. W. T., & Sin, D. D. (2020) · European Respiratory Journal · doi:10.1183/13993003.02108-2020 · Cited by 297
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Ruiz‐Aravena, M., McKee, C., Gamble, A., Lunn, T. J., Morris, A. L., Snedden, C. E., Yinda, C. K., Port, J. R., Buchholz, D. W., Yeo, Y. Y., et al. (2021) · Nature Reviews Microbiology · doi:10.1038/s41579-021-00652-2 · Cited by 303
Self-citationSARS-CoV-2 mRNA Vaccines: Immunological Mechanism and Beyond
Bettini, E., & Locci, M. (2021) · Vaccines · doi:10.3390/vaccines9020147 · Cited by 292
COVID-19 vaccine: A recent update in pipeline vaccines, their design and development strategies
Rawat, K., Kumari, P., & Saha, L. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173751 · Cited by 282
SARS-CoV-2 mRNA vaccination induces functionally diverse antibodies to NTD, RBD, and S2
Amanat, F., Thapa, M., Lei, T., Ahmed, S. M. S., Adelsberg, D. C., Carreño, J. M., Strohmeier, S., Schmitz, A. J., Zafar, S., Zhou, J. Q., et al. (2021) · Cell · doi:10.1016/j.cell.2021.06.005 · Cited by 273
Current status of probiotic and related health benefits
Das, T. K., Pradhan, S., Chakrabarti, S., Mondal, K. C., & Ghosh, K. (2022) · Applied Food Research · doi:10.1016/j.afres.2022.100185 · Cited by 308
COVID-19 outbreak: history, mechanism, transmission, structural studies and therapeutics
Yesudhas, D., Srivastava, A., & Gromiha, M. M. (2020) · Infection · doi:10.1007/s15010-020-01516-2 · Cited by 329
Yan, Y., Shin, W. I., Pang, Y. X., Yang, M., Lai, J., You, C., Zhao, H., Lester, E. H., Wu, T., & Pang, C. H. (2020) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph17072323 · Cited by 275
Broad sarbecovirus neutralization by a human monoclonal antibody
Tortorici, M. A., Czudnochowski, N., Starr, T. N., Marzi, R., Walls, A. C., Zatta, F., Bowen, J. E., Jaconi, S., di Iulio, J., Wang, Z., et al. (2021) · Nature · doi:10.1038/s41586-021-03817-4 · Cited by 255
Susceptibility of White-Tailed Deer (Odocoileus virginianus) to SARS-CoV-2
Palmer, M. V., Martins, M., Falkenberg, S. M., Buckley, A., Caserta, L. C., Mitchell, P. K., Cassmann, E. D., Rollins, A., Zylich, N. C., Renshaw, R. W., et al. (2021) · Journal of Virology · doi:10.1128/jvi.00083-21 · Cited by 257
Mosaic RBD nanoparticles protect against challenge by diverse sarbecoviruses in animal models
Cohen, A. A., van Doremalen, N., Greaney, A. J., Andersen, H., Sharma, A., Starr, T. N., Keeffe, J. R., Fan, C., Schulz, J. E., Gnanapragasam, P. N. P., et al. (2022) · Science · doi:10.1126/science.abq0839 · Cited by 264
Self-citationAge‐related rhesus macaque models of COVID‐19
Yu, P., Qi, F., Xu, Y., Li, F., Liu, P., Liu, J., Bao, L., Deng, W., Gao, H., Xiang, Z., et al. (2020) · Animal Models and Experimental Medicine · doi:10.1002/ame2.12108 · Cited by 275
Pathophysiology of COVID-19: Mechanisms Underlying Disease Severity and Progression
Bohn, M. K., Hall, A., Sepiashvili, L., Jung, B., Steele, S., & Adeli, K. (2020) · Physiology · doi:10.1152/physiol.00019.2020 · Cited by 273
Tutunchi, H., Naeini, F., Ostadrahimi, A., & Hosseinzadeh‐Attar, M. J. (2020) · Phytotherapy Research · doi:10.1002/ptr.6781 · Cited by 270
Coronaviruses: a paradigm of new emerging zoonotic diseases
Salata, C., Calistri, A., Parolin, C., & Palù, G. (2019) · Pathogens and Disease · doi:10.1093/femspd/ftaa006 · Cited by 257
Ahmed, S. F., Quadeer, A. A., & McKay, M. R. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.03.933226 · Cited by 256
Growth, detection, quantification, and inactivation of SARS-CoV-2
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Vardhan, S., & Sahoo, S. K. (2020) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2020.103936 · Cited by 244
What to do next to control the 2019-nCoV epidemic?
Wang, F., & Zhang, C. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30300-7 · Cited by 242
Cholesterol 25-hydroxylase suppresses SARS-CoV-2 replication by blocking membrane fusion
Zang, R., Case, J. B., Yutuc, E., Ma, X., Shen, S., Gomez Castro, M. F., Liu, Z., Zeng, Q., Zhao, H., Son, J., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2012197117 · Cited by 240
Erasmus, J. H., Khandhar, A. P., O’Connor, M. A., Walls, A. C., Hemann, E. A., Murapa, P., Archer, J., Leventhal, S., Fuller, J. T., Lewis, T. B., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.abc9396 · Cited by 241
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Woo, H., Park, S., Choi, Y. K., Park, T., Tanveer, M., Cao, Y., Kern, N. R., Lee, J., Yeom, M. S., Croll, T. I., et al. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c04553 · Cited by 230
Comparison of SARS-CoV-2 detection in nasopharyngeal swab and saliva
Iwasaki, S., Fujisawa, S., Nakakubo, S., Kamada, K., Yamashita, Y., Fukumoto, T., Sato, K., Oguri, S., Taki, K., Senjo, H., et al. (2020) · Journal of Infection · doi:10.1016/j.jinf.2020.05.071 · Cited by 243
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Ibrahım, B., & Önem, E. (2021) · Gevher Nesibe Journal IESDR · doi:10.46648/gnj.200 · Cited by 251
Yao, H., Lu, X., Chen, Q., Xu, K., Chen, Y. Z., Cheng, M., Chen, K., Cheng, L., Weng, T.-H., Shi, D., et al. (2020) · Cell Discovery · doi:10.1038/s41421-020-00226-1 · Cited by 241
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Divani, A. A., Andalib, S., Napoli, M. D., Lattanzi, S., Hussain, M. S., Biller, J., McCullough, L. D., Azarpazhooh, M. R., Seletska, A., Mayer, S. A., et al. (2020) · Journal of Stroke and Cerebrovascular Diseases · doi:10.1016/j.jstrokecerebrovasdis.2020.104941 · Cited by 236
Dittmar, M., Lee, J. S., Whig, K., Segrist, E., Li, M., Kamalia, B., Castellana, L., Ayyanathan, K., Cardenas‐Diaz, F. L., Morrisey, E. E., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108959 · Cited by 230
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Rosenke, K., Meade-White, K. D., Letko, M. C., Clancy, C. S., Hansen, F., Liu, Y., Okumura, A., Tang-Huau, T.-L., Li, R., Saturday, G. A., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1858177 · Cited by 216
Self-citationPotential neurological symptoms of COVID-19
Wang, H., Li, X., Yan, Z., Sun, X.-P., Han, J., & Zhang, B.-W. (2020) · Therapeutic Advances in Neurological Disorders · doi:10.1177/1756286420917830 · Cited by 230
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Campos, E. V. R., Pereira, A. D. E. S., de Oliveira, J. L., Carvalho, L. B., Guilger‐Casagrande, M., de Lima, R., & Fraceto, L. F. (2020) · Journal of Nanobiotechnology · doi:10.1186/s12951-020-00685-4 · Cited by 234
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Zhang, H., Rostami, M. R., Leopold, P. L., Mezey, J. G., O’Beirne, S. L., Strulovici‐Barel, Y., & Crystal, R. G. (2020) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.202003-0541oc · Cited by 227
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Yong, S. J. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00793 · Cited by 243
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Yu, L., Zhang, Z., Li, Y., Lian, X., Xie, Y., Li, S., Xin, S., Cao, P., & Lu, J. (2020) · iScience · doi:10.1016/j.isci.2020.101400 · Cited by 224
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Aydillo, T., Rombauts, A., Stadlbauer, D., Aslam, S., Abelenda-Alonso, G., Escalera, A., Amanat, F., Jiang, K., Krammer, F., Carratala, J., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23977-1 · Cited by 223
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Liu, G., & Rusling, J. F. (2021) · ACS Sensors · doi:10.1021/acssensors.0c02621 · Cited by 226
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dos Santos, W. G. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110493 · Cited by 235
Dieterle, M. E., Haslwanter, D., Bortz, R. H., Wirchnianski, A. S., Lasso, G., Vergnolle, O., Abbasi, S. A., Fels, J. M., Laudermilch, E., Florez, C., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.06.020 · Cited by 206
Liu, H., Wu, N. C., Yuan, M., Bangaru, S., Torres, J. L., Caniels, T. G., van Schooten, J., Zhu, X., Lee, C.-C. D., Brouwer, P. J. M., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.10.023 · Cited by 201
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Jung, C., Kmieć, D., Koepke, L., Zech, F., Jacob, T., Sparrer, K. M. J., & Kirchhoff, F. (2022) · Journal of Virology · doi:10.1128/jvi.02077-21 · Cited by 207
Evidence for SARS-CoV-2 Infection of Animal Hosts
Abdel-Moneim, A. S., & Abdelwhab, E. M. (2020) · Pathogens · doi:10.3390/pathogens9070529 · Cited by 209
The MERS-CoV Receptor DPP4 as a Candidate Binding Target of the SARS-CoV-2 Spike
Yu, L., Zhang, Z., Li, Y., Lian, X., Xie, Y., Li, S., Xin, S., Cao, P., & Lu, J. (2020) · iScience · doi:10.1016/j.isci.2020.101160 · Cited by 218
Wu, W., Cheng, Y., Zhou, H. W., Sun, C., & Zhang, S. (2023) · Virology Journal · doi:10.1186/s12985-023-01968-6 · Cited by 234
Neurological manifestations of COVID-19: a systematic review and meta-analysis of proportions
Favas, T. T., Dev, P., Chaurasia, R. N., Chakravarty, K., Mishra, R., Joshi, D., Mishra, V. N., Kumar, A., Singh, V. K., Pandey, M., et al. (2020) · Neurological Sciences · doi:10.1007/s10072-020-04801-y · Cited by 218
The SARS-CoV-2 Spike protein has a broad tropism for mammalian ACE2 proteins
Conceicao, C., Thakur, N., Human, S., Kelly, J. T., Logan, L., Bialy, D., Bhat, S., Stevenson-Leggett, P., Zagrajek, A. K., Hollinghurst, P., et al. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3001016 · Cited by 207
COVID-19 as part of the hyperferritinemic syndromes: the role of iron depletion therapy
Perricone, C., Bartoloni, E., Bursi, R., Cafaro, G., Guidelli, G. M., Shoenfeld, Y., & Gerli, R. (2020) · Immunologic Research · doi:10.1007/s12026-020-09145-5 · Cited by 238
ACE2 binding is an ancestral and evolvable trait of sarbecoviruses
Starr, T. N., Zepeda, S. K., Walls, A. C., Greaney, A. J., Alkhovsky, S. V., Veesler, D., & Bloom, J. D. (2022) · Nature · doi:10.1038/s41586-022-04464-z · Cited by 207
Oral Microbiome and SARS-CoV-2: Beware of Lung Co-infection
Bao, L., Zhang, C., Dong, J., Zhao, L., Li, Y., & Sun, J. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01840 · Cited by 207
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Gu, Y., Cao, J., Zhang, X., Gao, H., Wang, Y., Wang, J., He, J., Jiang, X., Zhang, J., Shen, G., et al. (2021) · Cell Research · doi:10.1038/s41422-021-00595-6 · Cited by 215
Hyperglycemia, hydroxychloroquine, and the COVID‐19 pandemic
Brufsky, A. (2020) · Journal of Medical Virology · doi:10.1002/jmv.25887 · Cited by 214
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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