Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV
Open accessPublished version of a preprint
Abstract
Since 2002, beta coronaviruses (CoV) have caused three zoonotic outbreaks, SARS-CoV in 2002–2003, MERS-CoV in 2012, and the newly emerged SARS-CoV-2 in late 2019. However, little is currently known about the biology of SARS-CoV-2. Here, using SARS-CoV-2 S protein pseudovirus system, we confirm that human angiotensin converting enzyme 2 (hACE2) is the receptor for SARS-CoV-2, find that SARS-CoV-2 enters 293/hACE2 cells mainly through endocytosis, that PIKfyve, TPC2, and cathepsin L are critical for entry, and that SARS-CoV-2 S protein is less stable than SARS-CoV S. Polyclonal anti-SARS S1 antibodies T62 inhibit entry of SARS-CoV S but not SARS-CoV-2 S pseudovirions. Further studies using recovered SARS and COVID-19 patients’ sera show limited cross-neutralization, suggesting that recovery from one infection might not protect against the other. Our results present potential targets for development of drugs and vaccines for SARS-CoV-2.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
ACE2 serves as a SARS-CoV-2 entry route in human cells, but as this enzyme is internalized following virus binding, its enzyme function is lost.
“ACE2, independent from its enzymatic activity, serves as SARS-CoV-2 entry route in human cells, but as this enzyme is internalized following virus binding, its enzyme function is lost [6, 116].”
From Hyperactivation of P2X7 receptors as a culprit of COVID-19 neuropathology (2021) · cites this paper as [6]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
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 · see citing works
Self-citationA novel coronavirus from patients with pneumonia in China, 2019
Zhu, N., Zhang, D., Wang, W., Li, X., Yang, B., Song, J., Zhao, X., Huang, B., Shi, W., Lu, R., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2001017 · Cited by 28,244 · see citing works
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 · see citing works
Self-citationHoffmann, 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 · see citing works
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 · see citing works
Isolation of a Novel Coronavirus from a Man with Pneumonia in Saudi Arabia
Zaki, A. M., van Boheemen, S., Bestebroer, T. M., Osterhaus, A. D. M. E., & Fouchier, R. A. M. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1211721 · Cited by 5,677 · see citing works
Identification of a novel coronavirus in patients with severe acute respiratory syndrome
Drosten, C., Günther, S., Preiser, W., van der Werf, S., Brodt, H.-R., Becker, S., Rabenau, H., Panning, M., Kolesnikova, L., Fouchier, R. A. M., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa030747 · Cited by 4,574 · see citing works
A Novel Coronavirus Associated with Severe Acute Respiratory Syndrome
Tg, K., Erdman, D. D., Cs, G., Zaki, Peret, T. C. T., Emery, S. L., Tong, S., Urbani, C., Comer, J. A., Lim, W., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa030781 · Cited by 4,345 · see citing works
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 · see citing works
Guan, Y., Zheng, B., He, Y., Liu, X. L., Zhuang, Z. X., Cheung, C. L., Luo, S., Li, P. H., Zhang, L., Guan, Y., et al. (2003) · Science · doi:10.1126/science.1087139 · Cited by 2,404 · see citing works
Self-citationDipeptidyl 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 · see citing works
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 2,031 · see citing works
Identification of a novel coronavirus causing severe pneumonia in human: a descriptive study.
Ren, L.-L., Wang, Y.-M., Wu, Z.-Q., Xiang, Z.-C., Guo, L., Xu, T., Jiang, Y.-Z., Xiong, Y., Li, Y.-J., Li, X.-W., et al. (2020) · Chinese Medical Journal · doi:10.1097/cm9.0000000000000722 · Cited by 1,349 · see citing works
Self-citationGlowacka, I., Bertram, S., Müller, M. A., Allen, P. W., Soilleux, E. J., Pfefferle, S., Steffen, I., Tsegaye, T. S., He, Y., Gnirß, K., et al. (2011) · Journal of Virology · doi:10.1128/jvi.02232-10 · Cited by 1,109 · see citing works
Belouzard, S., Chu, V. C., & Whittaker, G. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809524106 · Cited by 1,073 · see citing works
Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry
Simmons, G., Gosalia, D. N., Rennekamp, A. J., Reeves, J. D., Diamond, S. L., & Bates, P. F. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505577102 · Cited by 1,041 · see citing works
The International Committee on Taxonomy of Viruses
Murphy, F. A., Fauquet, C., Bishop, D. H. L., Ghabrial, S. A., Jarvis, A. W., Martelli, G. P., Mayo, M. A., & Summers, M. D. (1995) · Springer eBooks · doi:10.1007/978-3-7091-6607-9_3 · Cited by 945 · see citing works
Matsuyama, S., Nagata, N., Shirato, K., Kawase, M., Takeda, M., & Taguchi, F. (2010) · Journal of Virology · doi:10.1128/jvi.01542-10 · Cited by 778 · see citing works
Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26
Lu, G., Hu, Y., Wang, Q., Qi, J., Gao, F., Li, Y., Zhang, Y., Zhang, W., Yuan, Y., Bao, J., et al. (2013) · Nature · doi:10.1038/nature12328 · Cited by 740 · see citing works
Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4
Wang, N., Shi, X., Jiang, L., Zhang, S., Wang, D., Tong, P., Guo, D., Fu, L., Cui, Y., Liu, X., et al. (2013) · Cell Research · doi:10.1038/cr.2013.92 · Cited by 719 · see citing works
Millet, J. K., & Whittaker, G. R. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1407087111 · Cited by 698 · see citing works
Receptor Recognition Mechanisms of Coronaviruses: a Decade of Structural Studies
Li, F. (2014) · Journal of Virology · doi:10.1128/jvi.02615-14 · Cited by 574 · see citing works
Two-pore channels control Ebola virus host cell entry and are drug targets for disease treatment
Sakurai, Y., Kolokoltsov, A. A., Chen, C., Tidwell, M. W., Bauta, W. E., Klugbauer, N., Grimm, C. M., Wahl‐Schott, C., Biel, M., & Davey, R. A. (2015) · Science · doi:10.1126/science.1258758 · Cited by 548 · see citing works
Shirato, K., Kawase, M., & Matsuyama, S. (2013) · Journal of Virology · doi:10.1128/jvi.01890-13 · Cited by 456 · see citing works
SARS-like WIV1-CoV poised for human emergence
Menachery, V. D., Yount, B. L., Sims, A. C., Debbink, K., Agnihothram, S. S., Gralinski, L. E., Graham, R. L., Scobey, T., Plante, J. A., Royal, S. R., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1517719113 · Cited by 418 · see citing works
Williams, R. K., Jiang, G. S., & Holmes, K. V. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.13.5533 · Cited by 406 · see citing works
Hulswit, R. J. G., Lang, Y., Bakkers, M. J. G., Li, W., Li, Z., Schouten, A., Ophorst, B., van Kuppeveld, F. J. M., Boons, G., Bosch, B., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1809667116 · Cited by 380 · see citing works
Bertram, S., Dijkman, R., Habjan, M., Heurich, A., Gierer, S., Glowacka, I., Welsch, K., Winkler, M., Schneider, H., Hofmann-Winkler, H., et al. (2013) · Journal of Virology · doi:10.1128/jvi.03372-12 · Cited by 341 · see citing works
Gierer, S., Bertram, S., Kaup, F. ‐., Wrensch, F., Heurich, A., Krämer-Kühl, A., Welsch, K., Winkler, M., Meyer, B., Drosten, C., et al. (2013) · Journal of Virology · doi:10.1128/jvi.00128-13 · Cited by 341 · see citing works
Bertram, S., Glowacka, I., Müller, M. A., Lavender, H., Gnirß, K., Nehlmeier, I., Niemeyer, D., He, Y., Simmons, G., Drosten, C., et al. (2011) · Journal of Virology · doi:10.1128/jvi.05300-11 · Cited by 330 · see citing works
Proteolytic processing of Middle East respiratory syndrome coronavirus spikes expands virus tropism
Park, J.-E., Li, K., Barlan, A., Fehr, A. R., Perlman, S. M., McCray, P. B., & Gallagher, T. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1608147113 · Cited by 299 · see citing works
Kubo, H., Yamada, Y. K., & Taguchi, F. (1994) · Journal of Virology · doi:10.1128/jvi.68.9.5403-5410.1994 · Cited by 286 · see citing works
Genomic characterization and infectivity of a novel SARS-like coronavirus in Chinese bats
Hu, D., Zhu, C.-Q., Ai, L.-L., He, T., Wang, Y., Ye, F., Yang, L., Ding, C., Zhu, X.-H., Lv, R., et al. (2018) · Emerging Microbes and Infections · doi:10.1038/s41426-018-0155-5 · Cited by 281 · see citing works
Rutherford, A. C., Traer, C. J., Wassmer, T., Pattni, K., Bujny, M. V., Carlton, J. G., Stenmark, H., & Cullen, P. J. (2006) · Journal of Cell Science · doi:10.1242/jcs.03153 · Cited by 279 · see citing works
Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors
Park, Y.-J., Walls, A. C., Wang, Z., Sauer, M. M., Li, W., Tortorici, M. A., Bosch, B.-J., DiMaio, F., & Veesler, D. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0334-7 · Cited by 260 · see citing works
Huang, X., Dong, W., Milewska, A., Gołda, A., Qi, Y., Zhu, Q. K., Marasco, W. A., Baric, R. S., Sims, A. M., Pyrć, K., et al. (2015) · Journal of Virology · doi:10.1128/jvi.00854-15 · Cited by 257 · see citing works
PIKfyve Regulation of Endosome‐Linked Pathways
Lartigue, J. D., Polson, H. E. J., Feldman, M. E., Shokat, K. M., Tooze, S. A., Urbé, S., & Clague, M. J. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.00915.x · Cited by 243 · see citing works
Qian, Z., Dominguez, S. R., & Holmes, K. V. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076469 · Cited by 238 · see citing works
Self-citationHuman Adaptation of Ebola Virus during the West African Outbreak
Urbanowicz, R. A., McClure, C. P., Sakuntabhai, A., Sall, A. A., Kobinger, G., Müller, M. A., Holmes, E. C., Rey, F. A., Simon‐Lorière, E., & Ball, J. K. (2016) · Cell · doi:10.1016/j.cell.2016.10.013 · Cited by 219 · see citing works
Ebola Virus Glycoprotein with Increased Infectivity Dominated the 2013–2016 Epidemic
Diehl, W. E., Lin, A. E., Grubaugh, N. D., Carvalho, L. M., Kim, K., Kyawe, P. P., McCauley, S. M., Donnard, E. R., Küçükural, A., McDonel, P. E., et al. (2016) · Cell · doi:10.1016/j.cell.2016.10.014 · Cited by 192 · see citing works
Shirogane, Y., Takeda, M., Iwasaki, M., Ishiguro, N., Takeuchi, H., Nakatsu, Y., Tahara, M., Kikuta, H., & Yanagi, Y. (2008) · Journal of Virology · doi:10.1128/jvi.00676-08 · Cited by 181 · see citing works
Lysosomal Ion Channels as Decoders of Cellular Signals
Li, P., Gu, M., & Xu, H. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.10.006 · Cited by 174 · see citing works
Self-citationEmerging zoonoses and vector-borne infections affecting humans in Europe
Vorou, R., PAPAVASSILIOU, V. G., & Tsiodras, S. (2007) · Epidemiology and Infection · doi:10.1017/s0950268807008527 · Cited by 166 · see citing works
Gunaratne, G. S., Yang, Y., Li, F., Walseth, T. F., & Marchant, J. S. (2018) · Cell Calcium · doi:10.1016/j.ceca.2018.08.003 · Cited by 121 · see citing works
Identification of the Fusion Peptide-Containing Region in Betacoronavirus Spike Glycoproteins
Ou, X., Zheng, W., Shan, Y., Mu, Z., Dominguez, S. R., Holmes, K. V., & Qian, Z. (2016) · Journal of Virology · doi:10.1128/jvi.00015-16 · Cited by 117 · see citing works
Self-citationNelson, E. A., Dyall, J., Hoenen, T., et al. (2017) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0005540 · Cited by 113 · see citing works
Ou, X., Guan, H., Qin, B., et al. (2017) · Nature Communications · doi:10.1038/ncomms15216 · Cited by 78 · see citing works
Self-citationBiochemical Basis for Increased Activity of Ebola Glycoprotein in the 2013–16 Epidemic
Wang, M. K., Lim, S.-Y., Lee, S. M., et al. (2017) · Cell Host & Microbe · doi:10.1016/j.chom.2017.02.002 · Cited by 56 · see citing works
Qian, Z., Ou, X., Góes, L. G. B., Osborne, C. M., Castano, A. M., Holmes, K. V., & Dominguez, S. R. (2015) · Journal of Virology · doi:10.1128/jvi.03737-14 · Cited by 52 · see citing works
Self-citationLi, P., Shan, Y., Zheng, W., Ou, X., Mi, D., Mu, Z., Holmes, K. V., & Qian, Z. (2018) · Journal of Virology · doi:10.1128/jvi.00209-18 · Cited by 12 · see citing works
Self-citationMi, D., Ou, X., Li, P., et al. (2019) · Journal of Virology · doi:10.1128/jvi.01046-19 · Cited by 8 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 1
- [1]Masters, P. S. & Perlman, S. In Fields Virology, Vol. 1 (eds. D. M. Knipe & P. M Howley) Ch. 28, 825–858 (Lippincott Williams & Wilkins, 2013).
Cited by
Sorted by citations
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 · see citing works
Rydyznski Moderbacher, C., Ramirez, S. I., Dan, J. M., Grifoni, A., Hastie, K. M., Weiskopf, D., Belanger, S., Abbott, R. K., Kim, C., Choi, J., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.038 · Cited by 1,790 · see citing works
“, 2020), measurements of common leukocyte types, or inflammatory proteins in blood (Giamarellos-Bourboulis et al., 2020; Laing et al., 2020; Mathew et al., 2020; Meckiff et al., 2020; Ou et al., 2020; Sekine et al., 2020) to obtain powerful information about the status of COVID-19 patients.”
SARS-CoV-2 B.1.617.2 Delta variant replication and immune evasion
Mlcochova, P., Kemp, S. A., Dhar, M. S., Papa, G., Meng, B., Ferreira, I. A. T. M., Datir, R., Collier, D. A., Albecka, A., Singh, S., et al. (2021) · Nature · doi:10.1038/s41586-021-03944-y · Cited by 1,337 · see citing works
SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity
Zhang, L., Jackson, C. B., Mou, H., Ojha, A., Peng, H., Quinlan, B. D., Rangarajan, E. S., Pan, A., Vanderheiden, A., Suthar, M. S., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19808-4 · Cited by 1,387 · see citing works
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 · see citing works
“The next day cells were transfected with a SARS-CoV-2 S glycoprotein-encoding plasmid harboring the D19 C-terminal truncation (Ou et al., 2020), anMLVGag-Pol packaging construct and the reporter vector pTG-Luc, using the X-tremeGENE HP DNA transfection reagent (Roche) according to the manufacturer’s instructions.”
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 · see citing works
Barnes, C. O., West, A. P., Huey-Tubman, K. E., Hoffmann, M. A. G., Sharaf, N. G., Hoffman, P. R., Koranda, N., Gristick, H. B., Gaebler, C., Muecksch, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.025 · Cited by 795 · see citing works
Preexisting and de novo humoral immunity to SARS-CoV-2 in humans
Ng, K. W., Faulkner, N., Cornish, G. H., Rosa, A., Harvey, R., Hussain, S., Ulferts, R., Earl, C., Wrobel, A. G., Benton, D. J., et al. (2020) · Science · doi:10.1126/science.abe1107 · Cited by 886 · see citing works
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 · see citing works
BNT162b vaccines protect rhesus macaques from SARS-CoV-2
Vogel, A. B., Kanevsky, I., Che, Y., Swanson, K. A., Muik, A., Vormehr, M., Kranz, L. M., Walzer, K. C., Hein, S., Güler, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03275-y · Cited by 694 · see citing works
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 · see citing works
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 · see citing works
Self-citationUltrapotent 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 · see citing works
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 · see citing works
Tian, J.-H., Patel, N., Haupt, R., Zhou, H., Weston, S., Hammond, H., Logue, J., Portnoff, A. D., Norton, J., Guebre-Xabier, M., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20653-8 · Cited by 508 · see citing works
Humoral and circulating follicular helper T cell responses in recovered patients with COVID-19
Juno, J. A., Tan, H.-X., Lee, W. S., Reynaldi, A., Kelly, H. G., Wragg, K., Esterbauer, R., Kent, H. E., Batten, C. J., Mordant, F. L., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-0995-0 · Cited by 437 · see citing works
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 · see citing works
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 · see citing works
Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera
Supasa, P., Zhou, D., Dejnirattisai, W., Liu, C., Mentzer, A. J., Ginn, H. M., Zhao, Y., Duyvesteyn, H. M. E., Nutalai, R., Tuekprakhon, A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.033 · Cited by 460 · see citing works
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 · see citing works
“Pseudotyped S protein-expressing viral particles faithfully reflect key aspects of native SARS-CoV-2 entry into host cells via binding to its ACE2 receptor 33 , and thus, they can be used to test potential entry inhibitors of SARS-CoV-2 20,31 .”
Seydoux, 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 · see citing works
“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).”
Shen, X., Tang, H., McDanal, C., Wagh, K., Fischer, W., Theiler, J., Yoon, H., Li, D., Haynes, B. F., Sanders, K. O., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.03.002 · Cited by 378 · see citing works
Butowt, R., & Bilinska, K. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00172 · Cited by 346 · see citing works
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 · see citing works
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 · see citing works
Self-citationCrawford, K. H. D., Dingens, A. S., Eguia, R., Wolf, C. R., Wilcox, N., Logue, J. K., Shuey, K., Casto, A. M., Fiala, B., Wrenn, S., et al. (2021) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiaa618 · Cited by 265 · see citing works
Grzelak, L., Temmam, S., Planchais, C., Demeret, C., Tondeur, L., Huon, C., Guivel-Benhassine, F., Staropoli, I., Chazal, M., Dufloo, J., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.abc3103 · Cited by 310 · see citing works
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 · see citing works
Wang, K., Long, Q.-X., Deng, H.-J., Hu, J., Gao, Q.-Z., Zhang, G.-J., He, C.-L., Huang, L.-Y., Hu, J.-L., Chen, J., et al. (2021) · Clinical Infectious Diseases · doi:10.1093/cid/ciaa1143 · Cited by 218 · see citing works
Self-citationDe 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 · see citing works
Self-citationMicrostructure, pathophysiology, and potential therapeutics of COVID‐19: A comprehensive review
Singh, S. P., Pritam, M., Pandey, B., & Yadav, T. P. (2021) · Journal of Medical Virology · doi:10.1002/jmv.26254 · Cited by 166 · see citing works
Hyperactivation of P2X7 receptors as a culprit of COVID-19 neuropathology
Ribeiro, D. E., Oliveira-Giacomelli, Á., Glaser, T., Arnaud-Sampaio, V. F., Andrejew, R., Dieckmann, L., Baranova, J., Lameu, C., Ratajczak, M. Z., & Ulrich, H. (2021) · Molecular Psychiatry · doi:10.1038/s41380-020-00965-3 · Cited by 145 · see citing works
Vogel, A. B., Kanevsky, I., Che, Y., Swanson, K. A., Muik, A., Vormehr, M., Kranz, L. M., Walzer, K. C., Hein, S., Güler, A., et al. (2020) · doi:10.1101/2020.09.08.280818 · Cited by 126 · see citing works
Klimstra, W. B., Tilston-Lunel, N. L., Nambulli, S., Boslett, J., McMillen, C. M., Gilliland, T., Dunn, M. D., Sun, C., Wheeler, S. E., Wells, A., et al. (2020) · Journal of General Virology · doi:10.1099/jgv.0.001481 · Cited by 137 · see citing works
Serologic responses to SARS-CoV-2 infection among hospital staff with mild disease in eastern France
Fafi-Kremer, S., Bruel, T., Madec, Y., Grant, R., Tondeur, L., Grzelak, L., Staropoli, I., Anna, F., Souque, P., Fernandes-Pellerin, S., et al. (2020) · eBioMedicine · doi:10.1016/j.ebiom.2020.102915 · Cited by 108 · see citing works
Tada, T., Dcosta, B. M., Samanovic-Golden, M., Herati, R. S., Cornelius, A., Mulligan, M. J., & Landau, N. R. (2021) · doi:10.1101/2021.02.05.430003 · Cited by 153 · see citing works
Identification of trypsin-degrading commensals in the large intestine
Li, Y., Watanabe, E., Kawashima, Y., Plichta, D. R., Wang, Z., Ujike, M., Ang, Q. Y., Wu, R., Furuichi, M., Takeshita, K., et al. (2022) · Nature · doi:10.1038/s41586-022-05181-3 · Cited by 106 · see citing works
Can SARS-CoV-2 infect the central nervous system via the olfactory bulb or the blood-brain barrier?
Burks, S. M., Rosas-Hernandez, H., Alejandro Ramirez-Lee, M., Cuevas, E., & Talpos, J. C. (2021) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2020.12.031 · Cited by 97 · see citing works
Martínez-Mármol, R., Giordano-Santini, R., Kaulich, E., Cho, A.-N., Przybyla, M., Riyadh, M. A., Robinson, E., Chew, K. Y., Amor, R., Meunier, F. A., et al. (2023) · Science Advances · doi:10.1126/sciadv.adg2248 · Cited by 94 · see citing works
Stamatatos, L., Czartoski, J., Wan, Y.-H., Homad, L. J., Rubin, V., Glantz, H., Neradilek, M., Seydoux, E., Jennewein, M. F., MacCamy, A. J., et al. (2021) · doi:10.1101/2021.02.05.21251182 · Cited by 559 · see citing works
COVID-19: neonatal–perinatal perspectives
On behalf of the Harvard Neonatal-Perinatal Fellowship COVID-19 Working Group, Barrero-Castillero, A., Beam, K. S., Bernardini, L. B., Ramos, E. G. C., Davenport, P. E., Duncan, A. R., Fraiman, Y. S., Frazer, L. C., Healy, H., et al. (2021) · Journal of Perinatology · doi:10.1038/s41372-020-00874-x · Cited by 92 · see citing works
SARS-CoV-2 Dissemination Through Peripheral Nerves Explains Multiple Organ Injury
Fenrich, M., Mrdenovic, S., Balog, M., Tomic, S., Zjalic, M., Roncevic, A., Mandic, D., Debeljak, Z., & Heffer, M. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00229 · Cited by 95 · see citing works
Mlcochova, P., Kemp, S., Dhar, M. S., Papa, G., Meng, B., Mishra, S., Whittaker, C., Mellan, T., Ferreira, I., Datir, R., et al. (2021) · doi:10.1101/2021.05.08.443253 · Cited by 90 · see citing works
Coronavirus entry: how we arrived at SARS-CoV-2
Whittaker, G. R., Daniel, S., & Millet, J. K. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.02.006 · Cited by 67 · see citing works
Liu, S., Hossinger, A., Heumüller, S.-E., Hornberger, A., Buravlova, O., Konstantoulea, K., Müller, S. A., Paulsen, L., Rousseau, F., Schymkowitz, J., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25855-2 · Cited by 72 · see citing works
Pentón-Rol, G., Marín-Prida, J., & McCarty, M. F. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666210408123807 · Cited by 73 · see citing works
Wang, Y., Zheng, J., Islam, M. S., Yang, Y., Hu, Y., & Chen, X. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.59534 · Cited by 71 · see citing works
Self-citationCell deaths: Involvement in the pathogenesis and intervention therapy of COVID-19
Li, X., Zhang, Z., Wang, Z., Gutiérrez-Castrellón, P., & Shi, H. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01043-6 · Cited by 67 · see citing works
Kruglova, N., Siniavin, A., Gushchin, V., & Mazurov, D. (2021) · Viruses · doi:10.3390/v13061133 · Cited by 37 · see citing works
Steffen, T. L., Stone, E. T., Hassert, M., Geerling, E., Grimberg, B. T., Espino, A. M., Pantoja, P., Climent, C., Hoft, D. F., George, S. L., et al. (2020) · doi:10.1101/2020.08.21.261727 · Cited by 25 · see citing works
Insights in Chloroquine Action: Perspectives and Implications in Malaria and <scp>COVID</scp>‐19
Pillat, M. M., Krüger, A., Guimarães, L. M. F., Lameu, C., de Souza, E. E., Wrenger, C., & Ulrich, H. (2020) · Cytometry Part A · doi:10.1002/cyto.a.24190 · Cited by 17 · see citing works
Molecular epidemiology of SARS CoV-2: a review of current data on genetic variability of the virus
Parczewski, M., & Ciechanowicz, A. (2020) · Polish Archives of Internal Medicine · doi:10.20452/pamw.15550 · Cited by 17 · see citing works
Coelho Paraguassu, E., Chen, H., Zhou, F., Xu, Z., & Wang, M. (2020) · Brazilian Journal of Implantology and Health Sciences · doi:10.36557/2674-8169.2020v2n3p96-109 · Cited by 14 · see citing works
Li, C., Yu, D., Wu, X., Liang, H., Zhou, Z., Xie, Y., Li, T., Wu, J., Lu, F., Feng, L., et al. (2021) · doi:10.1101/2021.04.05.437224 · Cited by 73 · see citing works
Piccoli, L., Park, Y.-J., Tortorici, M. A., Czudnochowski, N., Walls, A. C., Beltramello, M., Silacci-Fregni, C., Pinto, D., Rosen, L. E., Bowen, J. E., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.037 · Cited by 1,395 · see citing works
- Authors
- Ou, X., Liu, Y., Lei, X., Li, P., Mi, D., Ren, L., Guo, L., Guo, R., Chen, T., Hu, J., Xiang, Z., Mu, Z., Chen, X., Chen, J., Hu, K., Jin, Q., Wang, J., & Qian, Z.
- Affiliations
- Chinese Academy of Medical Sciences & Peking Union Medical College (CN)
- Corresponding author
- Jin, Qi
- Wang, Jianwei
- Qian, Zhaohui
- ORCID
- Venue
- Nature Communications
- Published
- 2020-03-27
- Volume
- 11
- Issue
- 1
- Pages
- 1620-1620
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC7100515
- OpenAlex
- W3013093478
- Cited by
- 3,097
- References
- 51
- Citations by year
- 2026: 42 · 2025: 104 · 2024: 189 · 2023: 303 · 2022: 609 · 2021: 973 · 2020: 870 · 2019: 1
- FWCI
- 90.70
- Type
- journal article
- Language
- en
- Update notices
- correction (2021-04-01)
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- Research Square (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Informationszentrum Lebenswissenschaften (ZB MED) (submittedVersion, cc-by)
- Funders
- National Natural Science Foundation of China (31970171, 31670164)
- 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 › Infectious Diseases › COVID-19 Clinical Research Studies
- Keywords
- SARS-CoV-2, spike protein, viral entry, endocytosis, PIKfyve, TPC2, cathepsin L, SARS-CoV, cross-neutralization, COVID-19 pandemic, vaccine targets, therapeutic target
- MeSH terms
- Protein Domains, Betacoronavirus, Broadly Neutralizing Antibodies, Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, Antibodies, Viral, Cathepsins, Cell Fusion, Cross Reactions, Endocytosis, Humans, Peptidyl-Dipeptidase A, Neutralization Tests, Pneumonia, Viral, Receptors, Virus, Trypsin, Calcium Channels, Giant Cells, Coronavirus Infections, Phosphatidylinositol 3-Kinases, Severe Acute Respiratory Syndrome, Severe acute respiratory syndrome-related coronavirus, Virus Internalization, Protein Multimerization, Cathepsin L, HEK293 Cells, Pandemics, Spike Glycoprotein, Coronavirus
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
