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Cell entry mechanisms of SARS-CoV-2
Open accessAbstract
Significance: A key to curbing SARS-CoV-2 is to understand how it enters cells. SARS-CoV-2 and SARS-CoV both use human ACE2 as entry receptor and human proteases as entry activators. Using biochemical and pseudovirus entry assays and SARS-CoV as a comparison, we have identified key cell entry mechanisms of SARS-CoV-2 that potentially contribute to the immune evasion, cell infectivity, and wide spread of the virus. This study also clarifies conflicting reports from recent studies on cell entry of SARS-CoV-2. Finally, by highlighting the potency and the evasiveness of SARS-CoV-2, the study provides insight into intervention strategies that target its cell entry mechanisms.
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“The spike protein binds to its receptor on the host cell surface, angiotensin-converting enzyme 2 (ref.118).”
From mRNA vaccines for infectious diseases: principles, delivery and clinical translation (2021) · cites this paper as [118]
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“The attached spike protein is then cut open by the cell’s transmembrane serine protease 2, which induces a conformational change that exposes the spike protein’s fusion peptide and facilitates fusion with the cell or endosomal membrane118.”
From mRNA vaccines for infectious diseases: principles, delivery and clinical translation (2021) · cites this paper as [118]
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Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China
Huang, C., Wang, Y., Li, X., Ren, L., Zhao, J., Hu, Y., Zhang, L., Fan, G., Xu, J., Gu, X., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30183-5 · Cited by 48,884
Zhou, F., Yu, T., Du, R., Fan, G., Liu, Y., Liu, Z., Xiang, J., Wang, Y., Song, B., Gu, X., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30566-3 · Cited by 27,263
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
Hoffmann, M., Kleine-Weber, H., Schroeder, S., Krüger, N., Herrler, T., Erichsen, S., Schiergens, T. S., Herrler, G., Wu, N.-H., Nitsche, A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.02.052 · Cited by 20,286
Early transmission dynamics in Wuhan, China, of novel coronavirus-infected pneumonia
Li, Q., Guan, X., Wu, P., Wang, X., Zhou, L., Tong, Y., Ren, R., Leung, K. S. M., Lau, E. H. Y., Wong, J. Y., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2001316 · Cited by 16,575
Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., Graham, B. S., & McLellan, J. S. (2020) · Science · doi:10.1126/science.abb2507 · Cited by 8,897
Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein
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
Virological assessment of hospitalized patients with COVID-2019
Wölfel, R., Corman, V. M., Guggemos, W., Seilmaier, M., Zange, S., Müller, M. A., Niemeyer, D., Jones, T. C., Vollmar, P., Rothe, C., et al. (2020) · Nature · doi:10.1038/s41586-020-2196-x · Cited by 6,661
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
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- R. Woelfel . Clinical presentation and virological assessment of hospitalized cases of coronavirus disease 2019 in a travel-associated transmission cluster. medRxiv:2020.2003.2005.20030502 (8 March 2020).
- 10.1016/j.cell.2020.02.058 · DOI · Paper page
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Chi, X., Yan, R., Zhang, J., Zhang, G., Zhang, Y., Hao, M., Zhang, Z., Fan, P., Dong, Y., Yang, Y., et al. (2020) · Science · doi:10.1126/science.abc6952 · Cited by 1,385
Neuropilin-1 is a host factor for SARS-CoV-2 infection
Daly, J. L., Simonetti, B., Klein, K., Chen, K.-E., Williamson, M. K., Antón-Plágaro, C., Shoemark, D. K., Simón-Gracia, L., Bauer, M., Hollandi, R., et al. (2020) · Science · doi:10.1126/science.abd3072 · Cited by 1,251
Mechanisms of SARS-CoV-2 Transmission and Pathogenesis
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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
COVID-19 and comorbidities: Deleterious impact on infected patients
Ejaz, H., Alsrhani, A., Zafar, A., Javed, H., Junaid, K., Abdalla, A. E., Abosalif, K. O. A., Ahmed, Z., & Younas, S. (2020) · Journal of Infection and Public Health · doi:10.1016/j.jiph.2020.07.014 · Cited by 1,035
A dynamic COVID-19 immune signature includes associations with poor prognosis
Laing, A. G., Lorenc, A., del Molino del Barrio, I., Das, A., Fish, M., Monin, L., Muñoz-Ruiz, M., McKenzie, D. R., Hayday, T. S., Francos-Quijorna, I., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-1038-6 · Cited by 946
The furin cleavage site in the SARS-CoV-2 spike protein is required for transmission in ferrets
Peacock, T. P., Goldhill, D. H., Zhou, J., Baillon, L., Frise, R., Swann, O. C., Kugathasan, R., Penn, R., Brown, J. C., Sanchez-David, R. Y., et al. (2021) · Nature Microbiology · doi:10.1038/s41564-021-00908-w · Cited by 802
COVID-19 and the human innate immune system
Schultze, J. L., & Aschenbrenner, A. C. (2021) · Cell · doi:10.1016/j.cell.2021.02.029 · Cited by 714
Effects of COVID-19 on the Nervous System
Iadecola, C., Anrather, J., & Kamel, H. (2020) · Cell · doi:10.1016/j.cell.2020.08.028 · Cited by 674
Circular RNA Vaccines against SARS-CoV-2 and Emerging Variants
Qu, L., Yi, Z., Shen, Y., Lin, L., Chen, F., Xu, Y., Wu, Z., Tang, H., Zhang, X., Tian, F., et al. (2021) · doi:10.1101/2021.03.16.435594 · Cited by 636
Yang, L., Han, Y., Nilsson-Payant, B. E., Gupta, V., Wang, P., Duan, X., Tang, X., Zhu, J., Zhao, Z., Jaffré, F., et al. (2020) · Cell stem cell · doi:10.1016/j.stem.2020.06.015 · Cited by 645
Immunity, endothelial injury and complement-induced coagulopathy in COVID-19
Perico, L., Benigni, A., Casiraghi, F., Ng, L. F. P., Rénia, L., & Remuzzi, G. (2020) · Nature Reviews Nephrology · doi:10.1038/s41581-020-00357-4 · Cited by 616
Enhanced fusogenicity and pathogenicity of SARS-CoV-2 Delta P681R mutation
Saito, A., Irie, T., Suzuki, R., Maemura, T., Nasser, H., Uriu, K., Kosugi, Y., Shirakawa, K., Sadamasu, K., Kimura, I., et al. (2021) · Nature · doi:10.1038/s41586-021-04266-9 · Cited by 613
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
Malone, B. F., Urakova, N., Snijder, E. J., & Campbell, E. A. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00432-z · Cited by 583
Identification of SARS-CoV-2 inhibitors using lung and colonic organoids
Han, Y., Duan, X., Yang, L., Nilsson-Payant, B. E., Wang, P., Duan, F., Tang, X., Yaron, T. M., Zhang, T., Uhl, S., et al. (2021) · Nature · doi:10.1038/s41586-020-2901-9 · Cited by 530
SARS-CoV-2 D614G spike mutation increases entry efficiency with enhanced ACE2-binding affinity
Ozono, S., Zhang, Y., Ode, H., Sano, K., Tan, T. S., Imai, K., Miyoshi, K., Kishigami, S., Ueno, T., Iwatani, Y., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21118-2 · Cited by 522
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Hartenian, E., Nandakumar, D., Lari, A., Ly, M., Tucker, J. M., & Glaunsinger, B. A. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.013930 · Cited by 544
Regional and global contributions of air pollution to risk of death from COVID-19
Pozzer, A., Dominici, F., Haines, A., Witt, C., Münzel, T., & Lelieveld, J. (2020) · Cardiovascular Research · doi:10.1093/cvr/cvaa288 · Cited by 463
Jacob, F., Pather, S. R., Huang, W., Zhang, F., Wong, S. Z. H., Zhou, H., Cubitt, B., Fan, W., Chen, C. Z., Xu, M., et al. (2020) · Cell stem cell · doi:10.1016/j.stem.2020.09.016 · Cited by 443
Klein, S. L., Pekosz, A. S., Park, H.-S., Ursin, R. L., Shapiro, J. R., Benner, S. E., Littlefield, K. E., Kumar, S., Naik, H. M., Betenbaugh, M. J., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci142004 · Cited by 432
Colmenero, I., Santonja, C., Alonso, M., Noguera‐Morel, L., Hernández‐Martín, A., Martínez, D. A., Wiesner, T., Rodriguez-Peralto, J., Requena, L., & Torrelo, A. (2020) · British Journal of Dermatology · doi:10.1111/bjd.19327 · Cited by 422
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
Sacco, M. D., Ma, C., Lagarias, P. I., Gao, A., Townsend, J. A., Meng, X., Dube, P. H., Zhang, X., Hu, Y., Kitamura, N., et al. (2020) · Science Advances · doi:10.1126/sciadv.abe0751 · Cited by 405
Xu, C., Wang, Y., Liu, C., Zhang, C., Han, W., Hong, X., Wang, Y., Qin, H., Wang, S., Zhao, Q., et al. (2020) · Science Advances · doi:10.1126/sciadv.abe5575 · Cited by 380
Song, W., Hui, C., Hull, J. H., Birring, S. S., McGarvey, L. P., Mazzone, S. B., & Chung, K. F. (2021) · The Lancet Respiratory Medicine · doi:10.1016/s2213-2600(21)00125-9 · Cited by 386
COVID-19 vaccines: The status and perspectives in delivery points of view
Chung, J. Y., Thone, M. N., & Kwon, Y. J. (2021) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.12.011 · Cited by 375
Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity
Gobeil, S., Janowska, K., McDowell, S., Mansouri, K., Parks, R., Stalls, V., Kopp, M., Manne, K., Li, D., Wiehe, K. J., et al. (2021) · Science · doi:10.1126/science.abi6226 · Cited by 385
COVID-19: Virology, biology and novel laboratory diagnosis
Mohamadian, M., Chiti, H., Shoghli, A., Biglari, S., Parsamanesh, N., & Esmaeilzadeh, A. (2021) · The Journal of Gene Medicine · doi:10.1002/jgm.3303 · Cited by 371
Miao, G., Zhao, H., Li, Y., Ji, M., Chen, Y., Shi, Y., Bi, Y., Wang, P., & Zhang, H. (2021) · Developmental Cell · doi:10.1016/j.devcel.2020.12.010 · Cited by 354
TMPRSS2 expression dictates the entry route used by SARS‐CoV‐2 to infect host cells
Koch, J., Uckeley, Z. M., Doldan, P., Stanifer, M. L., Boulant, S., & Lozach, P. (2021) · The EMBO Journal · doi:10.15252/embj.2021107821 · Cited by 365
Ali, M. A., Hu, C., Jahan, S., Yuan, B., Saleh, M. S., Ju, E., Gao, S., & Panat, R. P. (2020) · Advanced Materials · doi:10.1002/adma.202006647 · Cited by 347
Bienvenu, L. A., Noonan, J. E., Wang, X., & Peter, K. (2020) · Cardiovascular Research · doi:10.1093/cvr/cvaa284 · Cited by 349
COVID-19 and the Chemical Senses: Supporting Players Take Center Stage
Cooper, K. W., Brann, D. H., Farruggia, M. C., Bhutani, S., Pellegrino, R., Tsukahara, T., Weinreb, C., Joseph, P. V., Larson, E. D., Parma, V., et al. (2020) · Neuron · doi:10.1016/j.neuron.2020.06.032 · Cited by 341
Huang, J., Hume, A. J., Abo, K. M., Werder, R. B., Villacorta-Martín, C., Alysandratos, K., Beermann, M. L., Simone-Roach, C., Lindstrom-Vautrin, J., Olejnik, J., et al. (2020) · Cell stem cell · doi:10.1016/j.stem.2020.09.013 · Cited by 334
An alpaca nanobody neutralizes SARS-CoV-2 by blocking receptor interaction
Hanke, L., Vidakovics, L. P., Sheward, D. J., Das, H., Schulte, T., Moliner-Morro, A., Corcoran, M., Achour, A., Hedestam, G. B. K., Hällberg, B. M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18174-5 · Cited by 334
Furin cleavage of SARS-CoV-2 Spike promotes but is not essential for infection and cell-cell fusion
Papa, G., Mallery, D. L., Albecka, A., Welch, L. G., Cattin‐Ortolá, J., Lupták, J., Paul, D., McMahon, H. T., Goodfellow, I., Carter, A. P., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009246 · Cited by 321
Senolytics reduce coronavirus-related mortality in old mice
Camell, C. D., Yousefzadeh, M. J., Zhu, Y., Prata, L. G. P. L., Huggins, M. A., Pierson, M., Zhang, L., O’Kelly, R. D., Pirtskhalava, T., Xun, P., et al. (2021) · Science · doi:10.1126/science.abe4832 · Cited by 320
Gobeil, S., Janowska, K., McDowell, S., Mansouri, K., Parks, R., Manne, K., Stalls, V., Kopp, M., Henderson, R. C., Edwards, R. J., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108630 · Cited by 324
The SARS-CoV-2 RNA–protein interactome in infected human cells
Schmidt, N., Lareau, C. A., Keshishian, H., Ganskih, S., Schneider, C., Hennig, T., Melanson, R., Werner, S., Wei, Y., Zimmer, M., et al. (2020) · Nature Microbiology · doi:10.1038/s41564-020-00846-z · Cited by 319
COVID-19 Transmission, Current Treatment, and Future Therapeutic Strategies
Salian, V. S., Wright, J. A., Vedell, P. T., Nair, S. A., Li, C., Kandimalla, M., Tang, X., Carmona, E. M., Kalari, K. R., & Kandimalla, K. K. (2021) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.0c00608 · Cited by 343
A genome-wide CRISPR screen identifies host factors that regulate SARS-CoV-2 entry
Zhu, Y., Feng, F., Hu, G., Wang, Y., Yin, Y., Zhu, Y., Xü, W., Cai, X., Sun, Z., Han, W., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21213-4 · Cited by 307
A materials-science perspective on tackling COVID-19
Tang, Z., Kong, N., Zhang, X., Liu, Y., Hu, P., Mou, S., Liljeström, P., Shi, J., Tan, W., Kim, J. S., et al. (2020) · Nature Reviews Materials · doi:10.1038/s41578-020-00247-y · Cited by 306
Rahman, S., Montero, M. T. V., Rowe, K., Kirton, R., & Kunik, F. (2021) · Expert Review of Clinical Pharmacology · doi:10.1080/17512433.2021.1902303 · Cited by 315
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
COVID-19: A review of therapeutic strategies and vaccine candidates
Izda, V., Jeffries, M. A., & Sawalha, A. H. (2020) · Clinical Immunology · doi:10.1016/j.clim.2020.108634 · Cited by 292
Zimmerman, M. I., Porter, J. R., Ward, M. D., Singh, S., Vithani, N., Meller, A., Mallimadugula, U. L., Kuhn, C. E., Borowsky, J. H., Wiewiora, R., et al. (2021) · Nature Chemistry · doi:10.1038/s41557-021-00707-0 · Cited by 288
Membrane fusion and immune evasion by the spike protein of SARS-CoV-2 Delta variant
Zhang, J., Xiao, T., Cai, Y., Lavine, C. L., Peng, H., Zhu, H., Anand, K., Tong, P., Gautam, A. K., Mayer, M. L., et al. (2021) · Science · doi:10.1126/science.abl9463 · Cited by 288
Yamamoto, M., Kiso, M., Sakai‐Tagawa, Y., Iwatsuki‐Horimoto, K., Imai, M., Takeda, M., Kinoshita, N., Ohmagari, N., Gohda, J., Semba, K., et al. (2020) · Viruses · doi:10.3390/v12060629 · Cited by 283
Ma, C., Hu, Y., Townsend, J. A., Lagarias, P. I., Marty, M. T., Kolocouris, A., & Wang, J. (2020) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.0c00130 · Cited by 276
Yeung, M. L., Teng, J. L. L., Jia, L., Zhang, C., Huang, C., Cai, J., Zhou, R., Chan, K., Zhao, H., Zhu, L., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.053 · Cited by 276
An infectivity-enhancing site on the SARS-CoV-2 spike protein targeted by antibodies
Liu, Y., Soh, W. T., Kishikawa, J.-I., Hirose, M., Nakayama, E. E., Li, S., Sasai, M., Suzuki, T., Tada, A., Arakawa, A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.05.032 · Cited by 277
Monocytes and Macrophages in COVID-19
Knoll, R., Schultze, J. L., & Schulte-Schrepping, J. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.720109 · Cited by 279
Richmond, P., Hatchuel, L., Dong, M., Ma, B., Hu, B. T., Smolenov, I. V., Li, P., Liang, P., Han, H. H., Liang, J. G., et al. (2021) · The Lancet · doi:10.1016/s0140-6736(21)00241-5 · Cited by 265
The SARS‐CoV‐2 main protease (M pro ): Structure, function, and emerging therapies for COVID‐19
Hu, Q., Xiong, Y., Zhu, G., Zhang, Y., Zhang, Y., Huang, P. C., & Ge, G. (2022) · MedComm · doi:10.1002/mco2.151 · Cited by 270
Ravindra, N. G., Alfajaro, M. M., Gasque, V., Huston, N. C., Wan, H., Szigeti-Buck, K., Yasumoto, Y., Greaney, A. M., Habet, V., Chow, R. D., et al. (2021) · PLOS Biology · doi:10.1371/journal.pbio.3001143 · Cited by 258
mRNA vaccines in disease prevention and treatment
Zhang, G., Tang, T., Chen, Y., Huang, X., & Liang, T. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01579-1 · Cited by 273
SARS-CoV-2 spreads through cell-to-cell transmission
Zeng, C., Evans, J. P., King, T., Zheng, Y.-M., Oltz, E. M., Whelan, S. P. J., Saif, L. J., Peeples, M. E., & Liu, S.-L. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2111400119 · Cited by 246
Heparan sulfate assists SARS-CoV-2 in cell entry and can be targeted by approved drugs in vitro
Zhang, Q., Chen, C. Z., Swaroop, M., Xu, M., Wang, L., Lee, J., Wang, A. Q., Pradhan, M., Hagen, N. R., Chen, L., et al. (2020) · Cell Discovery · doi:10.1038/s41421-020-00222-5 · Cited by 249
A TMPRSS2 inhibitor acts as a pan-SARS-CoV-2 prophylactic and therapeutic
Shapira, T., Monreal, I. A., Dion, S. P., Buchholz, D. W., Imbiakha, B., Olmstead, A. D., Jager, M. C., Désilets, A., Gao, G., Martins, M., et al. (2022) · Nature · doi:10.1038/s41586-022-04661-w · Cited by 248
Opposing activities of IFITM proteins in SARS‐CoV‐2 infection
Shi, G., Kenney, A. D., Kudryashova, E., Zani, A., Zhang, L., Lai, K. K., Hall‐Stoodley, L., Robinson, R., Kudryashov, D. S., Compton, A. A., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2020106501 · Cited by 235
Long-COVID postural tachycardia syndrome: an American Autonomic Society statement
Raj, S. R., Arnold, A. C., Barboi, A., Claydon, V. E., Limberg, J. K., Lucci, V.-E. M., Numan, M., Peltier, A., Snapper, H., Vernino, S., et al. (2021) · Clinical Autonomic Research · doi:10.1007/s10286-021-00798-2 · Cited by 227
Establishment of an African green monkey model for COVID-19 and protection against re-infection
Woolsey, C. B., Borisevich, V., Prasad, A. N., Agans, K. N., Deer, D. J., Dobias, N. S., Heymann, J. C., Foster, S. L., Levine, C. B., Medina, L. O., et al. (2020) · Nature Immunology · doi:10.1038/s41590-020-00835-8 · Cited by 232
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
Accelerating antiviral drug discovery: lessons from COVID-19
von Delft, A., Hall, M. D., Kwong, A. D., Purcell, L. A., Saikatendu, K. S., Schmitz, U., Tallarico, J. A., & Lee, A. A. (2023) · Nature Reviews Drug Discovery · doi:10.1038/s41573-023-00692-8 · Cited by 230
Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2): a Systemic Infection
Synowiec, A., Szczepański, A., Barreto-Durán, E., Lie, L. K., & Pyrć, K. (2021) · Clinical Microbiology Reviews · doi:10.1128/cmr.00133-20 · Cited by 228
Impact of the delta variant on vaccine efficacy and response strategies
Bian, L., Gao, Q., Gao, F., Wang, Q., He, Q., Wu, X., Mao, Q., Xu, M., & Liang, Z. (2021) · Expert Review of Vaccines · doi:10.1080/14760584.2021.1976153 · Cited by 219
COVID-19 and pulmonary fibrosis: a potential role for lung epithelial cells and fibroblasts
John, A. E., Joseph, C., Jenkins, G., & Tatler, A. L. (2021) · Immunological Reviews · doi:10.1111/imr.12977 · Cited by 219
Enzyme Therapy: Current Challenges and Future Perspectives
de la Fuente, M., Lombardero, L., Gómez-González, A., Solari, C., Angulo‐Barturen, Í., Acera, A., Vecino, E., Astigarraga, E., & Barreda‐Gómez, G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179181 · Cited by 217
De novo design of potent and resilient hACE2 decoys to neutralize SARS-CoV-2
Linsky, T. W., Vergara, R., Codina, N., Nelson, J. W., Walker, M. J., Su, W., Barnes, C. O., Hsiang, T.-Y., Esser-Nobis, K., Yu, K., et al. (2020) · Science · doi:10.1126/science.abe0075 · Cited by 216
SARS-COV-2 Variants: Differences and Potential of Immune Evasion
Hirabara, S. M., Serdan, T. D. A., Gorjão, R., Masi, L. N., Pithon‐Curi, T. C., Covas, D. T., Curi, R., & Durigon, E. L. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.781429 · Cited by 220
Genome-wide CRISPR screening identifies TMEM106B as a proviral host factor for SARS-CoV-2
Baggen, J., Persoons, L., Vanstreels, E., Jansen, S., Looveren, D. V., Boeckx, B., Geudens, V., Man, J. D., Jochmans, D., Wauters, J., et al. (2021) · Nature Genetics · doi:10.1038/s41588-021-00805-2 · Cited by 215
SARS-CoV-2 requires cholesterol for viral entry and pathological syncytia formation
Sanders, D. W., Jumper, C. C., Ackerman, P. J., Bracha, D., Donlic, A., Kim, H., Kenney, D., Castello-Serrano, I., Suzuki, S., Tamura, T., et al. (2021) · eLife · doi:10.7554/elife.65962 · Cited by 224
Structural features of coronavirus SARS-CoV-2 spike protein: Targets for vaccination
Sternberg, A., & Naujokat, C. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118056 · Cited by 223
Fignani, D., Licata, G., Brusco, N., Nigi, L., Grieco, G. E., Marselli, L., Overbergh, L., Gysemans, C. A., Colli, M. L., Marchetti, P., et al. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.596898 · Cited by 219
Host genetic factors determining COVID-19 susceptibility and severity
Velavan, T. P., Pallerla, S. R., Rüter, J., Augustin, Y. S., Kremsner, P. G., Krishna, S., & Meyer, C. G. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103629 · Cited by 222
Wu, W., Cheng, Y., Zhou, H. W., Sun, C., & Zhang, S. (2023) · Virology Journal · doi:10.1186/s12985-023-01968-6 · Cited by 234
Lu-Culligan, A., Chavan, A. R., Vijayakumar, P., Irshaid, L., Courchaine, E. M., Milano, K. M., Tang, Z., Pope, S. D., Song, E., Vogels, C. B. F., et al. (2021) · Med · doi:10.1016/j.medj.2021.04.016 · Cited by 212
An overview on the seven pathogenic human coronaviruses
Kesheh, M. M., Hosseini, P., Soltani, S., & Zandi, M. (2021) · Reviews in Medical Virology · doi:10.1002/rmv.2282 · Cited by 212
The glycosylation in SARS-CoV-2 and its receptor ACE2
Gong, Y., Qin, S., Dai, L., & Tian, Z. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00809-8 · Cited by 226
Diagnosis of COVID-19 for controlling the pandemic: A review of the state-of-the-art
Taleghani, N., & Taghipour, F. (2020) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2020.112830 · Cited by 212
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
IFITM proteins promote SARS-CoV-2 infection and are targets for virus inhibition in vitro
Bozzo, C. P., Nchioua, R., Volčič, M., Koepke, L., Krüger, J., Schütz, D., Heller, S., Stürzel, C. M., Kmieć, D., Conzelmann, C., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24817-y · Cited by 207
Kremsner, P., Mann, P., Bosch, J., Fendel, R., Gabor, J. J., Kreidenweiss, A., Kroidl, A., Leroux-Roels, I., Leroux-Roels, G., Schindler, C., et al. (2020) · doi:10.1101/2020.11.09.20228551 · Cited by 199
Idili, A., Parolo, C., Álvarez-Diduk, R., & Merkoçi, A. (2021) · ACS Sensors · doi:10.1021/acssensors.1c01222 · Cited by 198
ORF3a of SARS-CoV-2 promotes lysosomal exocytosis-mediated viral egress
Chen, D., Zheng, Q., Sun, L., Ji, M.-M., Li, Y., Deng, H., & Zhang, H. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.10.006 · Cited by 210
Inhibition of SARS-CoV-2 viral entry upon blocking N- and O-glycan elaboration
Yang, Q., Hughes, T. A., Kelkar, A., Yu, X., Cheng, K., Park, S., Huang, W., Lovell, J. F., & Neelamegham, S. (2020) · eLife · doi:10.7554/elife.61552 · Cited by 199
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
Luan, B., Wang, H., & Huynh, T. (2021) · FEBS Letters · doi:10.1002/1873-3468.14076 · Cited by 199
SARS-CoV-2 infection induces beta cell transdifferentiation
Tang, X., Uhl, S. A., Zhang, T., Xue, D., Li, B., Vandana, J. J., Acklin, J. A., Bonnycastle, L. L., Narisu, N., Erdos, M. R., et al. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.05.015 · Cited by 196
The Global Epidemic of the SARS-CoV-2 Delta Variant, Key Spike Mutations and Immune Escape
Tian, D., Sun, Y., Zhou, J., & Ye, Q. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.751778 · Cited by 201
Lee, J.-H., Choi, M., Jung, Y., Lee, S. K., Lee, C., Kim, J., Kim, J.-W., Kim, N. H., Kim, B., & Kim, H. G. (2020) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2020.112715 · Cited by 195
Laurent, Q., Martinent, R., Lim, B., Pham, A., Kato, T., López‐Andarias, J., Sakai, N., & Matile, S. (2021) · JACS Au · doi:10.1021/jacsau.1c00128 · Cited by 191
TLR3 and TLR7 RNA Sensor Activation during SARS-CoV-2 Infection
Bortolotti, D., Gentili, V., Rizzo, S., Schiuma, G., Beltrami, S., Strazzabosco, G., Fernández, M., Caccuri, F., Caruso, A., & Rizzo, R. (2021) · Microorganisms · doi:10.3390/microorganisms9091820 · Cited by 190
Metadata
- Authors
- Shang, J., Wan, Y., Luo, C., Ye, G., Geng, Q., Auerbach, A., & Li, F.
- Affiliations
- University of Minnesota (US)
- Corresponding author
- Li, Fang
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2020-05-06
- Volume
- 117
- Issue
- 21
- Pages
- 11727-11734
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC7260975
- OpenAlex
- W3022435472
- Cited by
- 3,142
- References
- 48
- Citations by year
- 2026: 78 · 2025: 171 · 2024: 257 · 2023: 444 · 2022: 746 · 2021: 993 · 2020: 450
- FWCI
- 87.09
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Division of Intramural Research, National Institute of Allergy and Infectious Diseases (R01AI089728, R01AI110700)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Health Sciences › Medicine › Infectious Diseases › COVID-19 Clinical Research Studies
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Keywords
- SARS-CoV-2, COVID-19 pandemic, viral entry, spike protein, receptor binding domain, ACE2 receptor, furin protease, proteolytic activation, SARS-CoV, receptor binding affinity, immune evasion, pseudovirus entry
- MeSH terms
- Protein Domains, Receptors, Coronavirus, Angiotensin-Converting Enzyme 2, Cell Line, Humans, Peptidyl-Dipeptidase A, Receptors, Virus, Virus Activation, Severe acute respiratory syndrome-related coronavirus, Virus Internalization, Immune Evasion, Spike Glycoprotein, Coronavirus
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