Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis
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Abstract
Severe acute respiratory syndrome coronavirus (SARS-CoV) emerged in 2002 as a highly transmissible pathogenic human betacoronavirus. The viral spike glycoprotein (S) utilizes angiotensin-converting enzyme 2 (ACE2) as a host protein receptor and mediates fusion of the viral and host membranes, making S essential to viral entry into host cells and host species tropism. As SARS-CoV enters host cells, the viral S is believed to undergo a number of conformational transitions as it is cleaved by host proteases and binds to host receptors. We recently developed stabilizing mutations for coronavirus spikes that prevent the transition from the pre-fusion to post-fusion states. Here, we present cryo-EM analyses of a stabilized trimeric SARS-CoV S, as well as the trypsin-cleaved, stabilized S, and its interactions with ACE2. Neither binding to ACE2 nor cleavage by trypsin at the S1/S2 cleavage site impart large conformational changes within stabilized SARS-CoV S or expose the secondary cleavage site, S2′.
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Both vaccines encode the same full-length, pre-fusion stabilized SARS-CoV-2 spike protein and are encapsulated in lipid nanoparticles with identical composition.
“Both vaccines encode the same full-length, pre-fusion stabilized severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) spike protein13,14 and are encapsulated in lipid nanoparticles (LNPs) with identical composition.”
From Optimization of non-coding regions for a non-modified mRNA COVID-19 vaccine (2022) · cites this paper as [14]
The Introduction (page unavailable) describes prefusion stabilization of coronavirus spike proteins using two proline mutations, and the Results examine a stabilized SARS-CoV spike ectodomain. The cited paper does not establish that both vaccines encode the same full-length SARS-CoV-2 spike protein. The LNP-composition clause follows the citations and is not judged as attributed to this source. (LLM, conf=0.87)
Experimental — accuracy not yet measuredStabilizing coronavirus spike proteins by substituting two prolines at the top of heptad repeat 1 prevents structural rearrangements of the fusion (S2) subunit.
“Stabilizing coronavirus spike proteins by substituting two prolines at the top of heptad repeat 1 prevents structural rearrangements of the fusion (S2) subunit.”
From An mRNA Vaccine against SARS-CoV-2 — Preliminary Report (2020) · cites this paper as [26]
The Methods describe two proline substitutions, and the Results report that the stabilized SARS-CoV spike retains its prefusion conformation without large changes in S2 after receptor binding. But the Results also observe a subtle rearrangement in the S2 central helix and say only that the mutations may block further propagation. The claim’s unqualified statement that they prevent S2 rearrangements overstates the evidence; page numbers are unavailable in our copy. (LLM, conf=0.88)
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Cites
<i>Coot</i> : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571 · see citing works
<i>PHENIX</i> : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716 · see citing works
MotionCor2 - anisotropic correction of beam-induced motion for improved cryo-electron microscopy
Zheng, S., Palovcak, E. J., Armache, J., Verba, K., Cheng, Y.-F., & Agard, D. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,678 · see citing works
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334 · 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
SARS and MERS: recent insights into emerging coronaviruses
de Wit, E., van Doremalen, N., Falzarano, D., & Munster, V. J. (2016) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.81 · Cited by 3,510 · see citing works
Gctf: Real-time CTF determination and correction
Zhang, K. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.11.003 · Cited by 3,372 · 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
Automated molecular microscopy: The new Leginon system
Suloway, C. J. M., Pulokas, J., Fellmann, D., Cheng, A., Guerra, F., Quispe, J. D., Stagg, S. M., Potter, C. S., & Carragher, B. O. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.03.010 · Cited by 1,681 · see citing works
Structure of influenza haemagglutinin at the pH of membrane fusion
Bullough, P. A., Hughson, F. M., Skehel, J. J., & Wiley, D. C. (1994) · Nature · doi:10.1038/371037a0 · Cited by 1,564 · see citing works
Bosch, B. J., van der Zee, R., de Haan, C. A. M., & Rottier, P. J. M. (2003) · Journal of Virology · doi:10.1128/jvi.77.16.8801-8811.2003 · Cited by 1,489 · see citing works
Mechanisms of Coronavirus Cell Entry Mediated by the Viral Spike Protein
Belouzard, S., Millet, J. K., Licitra, B. N., & Whittaker, G. R. (2012) · Viruses · doi:10.3390/v4061011 · Cited by 1,368 · 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
Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen
Pallesen, J., Wang, N., Corbett, K. S., Wrapp, D., Kirchdoerfer, R. N., Turner, H. L., Cottrell, C. A., Becker, M. M., Wang, L., Shi, W., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707304114 · Cited by 1,073 · see citing works
Self-citationInhibitors 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
Hu, B., Zeng, L., Yang, X., Ge, X.-Y., Zhang, W., Li, B., Xie, J., Shen, X.-R., Zhang, Y.-Z., Wang, N., et al. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006698 · Cited by 956 · see citing works
Self-citationSanders, R. W., Derking, R., Cupo, A., Julien, J., Yasmeen, A., de Val, N., Kim, H. J., Blattner, C., de la Peña, A. T., Korzun, J., et al. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003618 · Cited by 937 · see citing works
Self-citationAccelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2
Kimanius, D., Forsberg, B. O., Scheres, S. H. W., & Lindahl, E. R. (2016) · eLife · doi:10.7554/elife.18722 · Cited by 903 · see citing works
Host cell proteases: Critical determinants of coronavirus tropism and pathogenesis
Millet, J. K., & Whittaker, G. R. (2014) · Virus Research · doi:10.1016/j.virusres.2014.11.021 · Cited by 887 · see citing works
Appion: An integrated, database-driven pipeline to facilitate EM image processing
Lander, G. C., Stagg, S. M., Voss, N. R., Cheng, A., Fellmann, D., Pulokas, J., Yoshioka, C., Irving, C., Mulder, A. M., Lau, P., et al. (2009) · Journal of Structural Biology · doi:10.1016/j.jsb.2009.01.002 · Cited by 836 · see citing works
Molecular architecture of native HIV-1 gp120 trimers
Liu, J., Bartesaghi, A., Borgnia, M. J., Sapiro, G., & Subramaniam, S. (2008) · Nature · doi:10.1038/nature07159 · Cited by 815 · 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
Pre-fusion structure of a human coronavirus spike protein
Kirchdoerfer, R. N., Cottrell, C. A., Wang, N., Pallesen, J., Yassine, H. M., Turner, H. L., Corbett, K. S., Graham, B. S., McLellan, J. S., & Ward, A. B. (2016) · Nature · doi:10.1038/nature17200 · Cited by 765 · see citing works
Self-citationYuan, Y., Cao, D., Zhang, Y., Ma, J., Qi, J., Wang, Q., Lu, G., Wu, Y., Yan, J., Shi, Y., et al. (2017) · Nature Communications · doi:10.1038/ncomms15092 · Cited by 761 · see citing works
Sievers, F., & Higgins, D. G. (2014) · Current Protocols in Bioinformatics · doi:10.1002/0471250953.bi0313s48 · Cited by 760 · see citing works
Graham, R. L., & Baric, R. S. (2009) · Journal of Virology · doi:10.1128/jvi.01394-09 · Cited by 738 · see citing works
Wong, S. K., Li, W., Moore, M. J., Choe, H., & Farzan, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c300520200 · Cited by 690 · see citing works
Gui, M., Song, W., Zhou, H., Xu, J., Chen, S., Xiang, Y., & Wang, X. (2016) · Cell Research · doi:10.1038/cr.2016.152 · Cited by 577 · see citing works
Voss, N. R., Yoshioka, C., Radermacher, M., Potter, C. S., & Carragher, B. O. (2009) · Journal of Structural Biology · doi:10.1016/j.jsb.2009.01.004 · Cited by 571 · see citing works
Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer
Walls, A. C., Tortorici, M. A., Bosch, B., Frenz, B., Rottier, P. J. M., DiMaio, F., Rey, F. A., & Veesler, D. (2016) · Nature · doi:10.1038/nature16988 · Cited by 539 · see citing works
Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion
Walls, A. C., Tortorici, M. A., Snijder, J., Xiong, X., Bosch, B., Rey, F. A., & Veesler, D. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708727114 · Cited by 539 · see citing works
Sanders, R. W., Vesanen, M., Schülke, N., Master, A., Schiffner, L., Kalyanaraman, R., Paluch, M. T., Berkhout, B., Maddon, P. J., Olson, W. C., et al. (2002) · Journal of Virology · doi:10.1128/jvi.76.17.8875-8889.2002 · Cited by 441 · 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
Walls, A. C., Tortorici, M. A., Frenz, B., Snijder, J., Li, W., Rey, F. A., DiMaio, F., Bosch, B., & Veesler, D. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3293 · Cited by 407 · see citing works
Protease-mediated enhancement of severe acute respiratory syndrome coronavirus infection
Matsuyama, S., Ujike, M., Morikawa, S., Tashiro, M., & Taguchi, F. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503203102 · Cited by 314 · see citing works
Gong, X., Qian, H., Zhou, X., Wu, J., Wan, T., Cao, P., Huang, W., Zhao, X., Wang, X., Wang, P., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.022 · Cited by 314 · see citing works
DiMaio, F., Song, Y., Li, X., Brunner, M. J., Xu, C., Conticello, V. P., Egelman, E. H., Marlovits, T. C., Cheng, Y., & Baker, D. A. (2015) · Nature Methods · doi:10.1038/nmeth.3286 · Cited by 309 · 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
Ebola Viral Glycoprotein Bound to Its Endosomal Receptor Niemann-Pick C1
Wang, H., Shi, Y., Song, J. G., Qi, J., Lu, G., Yan, J., & Gao, G. F. (2016) · Cell · doi:10.1016/j.cell.2015.12.044 · Cited by 292 · see citing works
Physiological and molecular triggers for SARS-CoV membrane fusion and entry into host cells
Millet, J. K., & Whittaker, G. R. (2017) · Virology · doi:10.1016/j.virol.2017.12.015 · Cited by 291 · see citing works
Open and closed structures reveal allostery and pliability in the HIV-1 envelope spike
Ozorowski, G., Pallesen, J., de Val, N., Lyumkis, D., Cottrell, C. A., Torres, J. L., Copps, J., Stanfield, R. L., Cupo, A., Pugach, P., et al. (2017) · Nature · doi:10.1038/nature23010 · Cited by 237 · see citing works
Self-citationLai, A. L., Millet, J. K., Daniel, S., Freed, J. H., & Whittaker, G. R. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.10.017 · Cited by 192 · see citing works
Millhauser, G. L. (1995) · Biochemistry · doi:10.1021/bi00012a001 · Cited by 185 · see citing works
Harris, A. K., Borgnia, M. J., Shi, D., Bartesaghi, A., He, H., Pejchal, R., Kang, Y., Depetris, R. S., Marozsan, A. J., Sanders, R. W., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1101414108 · Cited by 161 · see citing works
Xiong, X., Tortorici, M. A., Snijder, J., Yoshioka, C., Walls, A. C., Li, W., McGuire, A. T., Rey, F. A., Bosch, B., & Veesler, D. (2017) · Journal of Virology · doi:10.1128/jvi.01628-17 · Cited by 155 · see citing works
Cryo-Electron Microscopy Structure of Porcine Deltacoronavirus Spike Protein in the Prefusion State
Shang, J., Zheng, Y., Yang, Y., Liu, C., Geng, Q., Tai, W., Du, L., Zhou, Y., Zhang, W., & Li, F. (2017) · Journal of Virology · doi:10.1128/jvi.01556-17 · Cited by 139 · see citing works
Fukushi, S., Mizutani, T., Saijo, M., Matsuyama, S., Miyajima, N., Taguchi, F., Itamura, S., Kurane, I., & Morikawa, S. (2005) · Journal of General Virology · doi:10.1099/vir.0.80955-0 · Cited by 132 · see citing works
310 helices in channels and other membrane proteins
Vieira-Pires, R. S., & Morais-Cabral, J. H. (2010) · The Journal of General Physiology · doi:10.1085/jgp.201010508 · Cited by 101 · see citing works
Matsuyama, S., & Taguchi, F. (2009) · Journal of Virology · doi:10.1128/jvi.00959-09 · Cited by 96 · see citing works
Structural Characterization of Cleaved, Soluble HIV-1 Envelope Glycoprotein Trimers
Khayat, R., Lee, J. H., Julien, J., et al. (2013) · Journal of Virology · doi:10.1128/jvi.01222-13 · Cited by 73 · see citing works
SARS Immunity and Vaccination.
Minsheng, Z. (2004) · PubMed · Cited by 72 · see citing works
Park, J.-E., Cruz, D. J. M., & Shin, H. (2011) · Archives of Virology · doi:10.1007/s00705-011-1044-6 · Cited by 63 · see citing works
Miura, H. S., Nakagaki, K., & Taguchi, F. (2003) · Journal of Virology · doi:10.1128/jvi.78.1.216-223.2004 · Cited by 45 · see citing works
EMHP: an accurate automated hole masking algorithm for single-particle cryo-EM image processing
Berndsen, Z. T., Bowman, C., Jang, H., et al. (2017) · Bioinformatics · doi:10.1093/bioinformatics/btx500 · Cited by 22 · see citing works
Grindeanu, A. (1971) · PubMed · Cited by 5 · see citing works
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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 · see citing works
Self-citationStructure, 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 · see citing works
An mRNA Vaccine against SARS-CoV-2 — Preliminary Report
Jackson, L. A., Anderson, E. J., Rouphael, N. G., Roberts, P. C., Makhene, M., Coler, R. N., McCullough, M. P., Chappell, J. D., Denison, M. R., Stevens, L. J., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2022483 · Cited by 3,237 · see citing works
Self-citationHuman neutralizing antibodies elicited by SARS-CoV-2 infection
Ju, B., Zhang, Q., Ge, J., Wang, R., Sun, J., Ge, X., Yu, J., Shan, S., Zhou, B., Song, S., et al. (2020) · Nature · doi:10.1038/s41586-020-2380-z · Cited by 1,667 · see citing works
Distinct conformational states of SARS-CoV-2 spike protein
Cai, Y., Zhang, J., Xiao, T., Peng, H., Sterling, S. M., Walsh, R. M., Rawson, S., Rits-Volloch, S., & Chen, B. (2020) · Science · doi:10.1126/science.abd4251 · Cited by 1,221 · see citing works
Molecular Architecture of the SARS-CoV-2 Virus
Yao, H., Song, Y., Chen, Y., Wu, N., Xu, J., Sun, C., Zhang, J., Weng, T., Zhang, Z., Wu, Z., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.018 · Cited by 1,060 · see citing works
“Activation of S requires cleavage of S1/S2 by furin-like protease and undergoes a conformational change from prefusion to postfusion (Belouzard et al., 2009; Kirchdoerfer et al., 2018; Simmons et al., 2004, 2013; Song et al., 2018).”
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
Structural insights into coronavirus entry
(2019) · Advances in Virus Research · doi:10.1016/bs.aivir.2019.08.002 · Cited by 769 · 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
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 · see citing works
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 · see citing works
Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion
Walls, A. C., Xiong, X., Park, Y.-J., Tortorici, M. A., Snijder, J., Quispe, J., Cameroni, E., Gopal, R., Dai, M., Lanzavecchia, A., et al. (2019) · Cell · doi:10.1016/j.cell.2018.12.028 · Cited by 582 · see citing works
McKay, P. F., Hu, K., Blakney, A. K., Samnuan, K., Brown, J. C., Penn, R., Zhou, J., Bouton, C. R., Rogers, P., Polra, K., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17409-9 · Cited by 462 · see citing works
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
“High-resolution structures of the SARS-CoV-2 prefusion-stabilized spike (S) ectodomain revealed that it adopts multiple conformations with either one receptor-binding domain (RBD) in the ‘‘up’’ or ‘‘open’’ conformation or all RBDs in the ‘‘down’’ or ‘‘closed’’ conformation, similar to previous reports on both SARS-CoV…”
D614G Spike Mutation Increases SARS CoV-2 Susceptibility to Neutralization
Weissman, D., Alameh, M.-G., de Silva, T., Collini, P., Hornsby, H., Brown, R., LaBranche, C. C., Edwards, R. J., Sutherland, L., Santra, S., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2020.11.012 · Cited by 324 · see citing works
A thermostable, closed SARS-CoV-2 spike protein trimer
Xiong, X., Qu, K., Ciazynska, K. A., Hosmillo, M., Carter, A. P., Ebrahimi, S., Ke, Z., Scheres, S. H. W., Bergamaschi, L., Grice, G. L., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0478-5 · Cited by 313 · 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
The SARS-CoV-2 Spike variant D614G favors an open conformational state
Mansbach, R. A., Chakraborty, S., Nguyen, K., Montefiori, D. C., Korber, B., & Gnanakaran, S. (2021) · Science Advances · doi:10.1126/sciadv.abf3671 · Cited by 206 · see citing works
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 · see citing works
Rauch, S., Roth, N., Schwendt, K., Fotin-Mleczek, M., Mueller, S. O., & Petsch, B. (2021) · npj Vaccines · doi:10.1038/s41541-021-00311-w · Cited by 165 · see citing works
An engineered decoy receptor for SARS-CoV-2 broadly binds protein S sequence variants
Chan, K. K., Tan, T. J. C., Narayanan, K. K., & Procko, E. (2021) · Science Advances · doi:10.1126/sciadv.abf1738 · Cited by 152 · 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
Optimization of non-coding regions for a non-modified mRNA COVID-19 vaccine
Gebre, M. S., Rauch, S., Roth, N., Yu, J., Chandrashekar, A., Mercado, N. B., He, X., Liu, J., McMahan, K., Martinot, A., et al. (2022) · Nature · doi:10.1038/s41586-021-04231-6 · Cited by 127 · see citing works
Approaches and Challenges in SARS-CoV-2 Vaccine Development
Dagotto, G., Yu, J., & Barouch, D. H. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.08.002 · Cited by 103 · 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
Roth, N., Schön, J., Hoffmann, D., Thran, M., Thess, A., Mueller, S. O., Petsch, B., & Rauch, S. (2022) · Vaccines · doi:10.3390/vaccines10081251 · Cited by 22 · see citing works
Wang, C., van Haperen, R., Gutiérrez-Álvarez, J., Li, W., Okba, N. M. A., Albulescu, I., Widjaja, I., van Dieren, B., Fernandez-Delgado, R., Sola, I., et al. (2020) · doi:10.1101/2020.10.20.346916 · Cited by 15 · see citing works
Roth, N., Schön, J., Hoffmann, D., Thran, M., Thess, A., Mueller, S. O., Petsch, B., & Rauch, S. (2021) · doi:10.1101/2021.05.13.443734 · Cited by 18 · see citing works
Gebre, M. S., Rauch, S., Roth, N., Yu, J., Chandrashekar, A., Mercado, N. B., He, X., Liu, J., McMahan, K., Martinot, A., et al. (2021) · doi:10.1101/2021.08.13.456316 · Cited by 8 · 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
- Kirchdoerfer, R. N., Wang, N., Pallesen, J., Wrapp, D., Turner, H. L., Cottrell, C. A., Corbett, K. S., Graham, B. S., McLellan, J. S., & Ward, A. B.
- Affiliations
- Scripps Research Institute (US)
- Dartmouth College (US)
- National Institute of Allergy and Infectious Diseases (US)
- Corresponding author
- Ward, Andrew B.
- ORCID
- Venue
- Scientific Reports
- Published
- 2018-10-24
- Volume
- 8
- Issue
- 1
- Pages
- 15701-15701
- ISSN
- 2045-2322 (ISSN-L)
- PMC
- PMC6200764
- OpenAlex
- W2896109093
- Cited by
- 466
- References
- 55
- Citations by year
- 2026: 7 · 2025: 10 · 2024: 33 · 2023: 43 · 2022: 75 · 2021: 123 · 2020: 164 · 2019: 10
- FWCI
- 55.94
- Type
- journal article
- Language
- en
- Update notices
- correction (2018-12-10)
- Open access
- gold
- doi.org
- Locations
- Scientific Reports (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- U.S. Department of Health & Human Services | National Institutes of Health (AI123498, AI127521, OD021634)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- SARS-CoV, spike protein, ACE2 receptor, trypsin cleavage, S1/S2 cleavage site, S2' cleavage site, receptor binding, viral entry, host proteases
- MeSH terms
- Angiotensin-Converting Enzyme 2, Binding Sites, Glycosylation, Humans, Peptidyl-Dipeptidase A, Mutation, Peptide Hydrolases, Proline, Receptors, Virus, Trypsin, Protein Structure, Secondary, Cryoelectron Microscopy, Severe acute respiratory syndrome-related coronavirus, Virus Internalization, Protein Stability, Viral Tropism, HEK293 Cells, Proteolysis, Spike Glycoprotein, Coronavirus
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