SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity
Open accessPublished version of a preprint
Abstract
SARS-CoV-2 variants with spike (S)-protein D614G mutations now predominate globally. We therefore compare the properties of the mutated S protein (S G614 ) with the original (S D614 ). We report here pseudoviruses carrying S G614 enter ACE2-expressing cells more efficiently than those with S D614 . This increased entry correlates with less S1-domain shedding and higher S-protein incorporation into the virion. Similar results are obtained with virus-like particles produced with SARS-CoV-2 M, N, E, and S proteins. However, D614G does not alter S-protein binding to ACE2 or neutralization sensitivity of pseudoviruses. Thus, D614G may increase infectivity by assembling more functional S protein into the virion.
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?
The B.1.1.7, B.1.351, and P.1 lineages all harbor a N501Y mutation in the RBD, which increases the affinity for the ACE2 receptor, and a D614G mutation, which increases virion spike density, infectivity, and transmissibility.
“The B.1.1.7, B.1.351, and P.1 lineages all harbor a N501Y mutation in the RBD, which increases the affinity for the ACE2 receptor (57, 58), and a D614G mutation, which increases virion spike density, infectivity, and transmissibility (59, 60).”
From mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection (2021) · cites this paper as [59]
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
1 retracted
Genome-wide variations of SARS-CoV-2 infer evolution relationship and transmission routePreprint
Zhang, L., Wang, S., Ren, Q., Yang, J., Lu, Y., Zhang, L., & Gai, Z. (2020) · medRxiv · doi:10.1101/2020.04.27.20081349 · Cited by 13 · see citing works
Self-citationRetractedA 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
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 · see citing works
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 · see citing works
Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
Lan, J., Ge, J., Yu, J., Shan, S., Zhou, H., Fan, S., Zhang, Q., Shi, X., Wang, Q., Zhang, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2180-5 · Cited by 5,983 · see citing works
Self-citationAngiotensin-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
Self-citationKorber, B., Fischer, W. M., Gnanakaran, S., Yoon, H., Theiler, J., Abfalterer, W., Hengartner, N., Giorgi, E. E., Bhattacharya, T., Foley, B., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.043 · Cited by 4,281 · see citing works
Coronaviruses: An Overview of Their Replication and Pathogenesis
Fehr, A. R., & Perlman, S. M. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2438-7_1 · Cited by 3,784 · see citing works
Structural basis of receptor recognition by SARS-CoV-2
Shang, J., Ye, G., Shi, K., Wan, Y., Luo, C., Aihara, H., Geng, Q., Auerbach, A., & Li, F. (2020) · Nature · doi:10.1038/s41586-020-2179-y · Cited by 3,661 · see citing works
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
Ou, X., Liu, Y., Lei, X., Li, P., Mi, D., Ren, L., Guo, L., Guo, R., Chen, T., Hu, J., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15562-9 · Cited by 3,097 · see citing works
Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2
Wang, Q., Zhang, Y., Wu, L., Niu, S., Song, C., Zhang, Z., Lu, G., Qiao, C., Hu, Y., Yuen, K.-Y., et al. (2020) · Cell · doi:10.1016/j.cell.2020.03.045 · Cited by 2,892 · see citing works
Ziegler, C. G. K., Allon, S. J., Nyquist, S. K., Mbano, I. M., Miao, V. N., Tzouanas, C. N., Cao, Y., Yousif, A. S., Bals, J., Hauser, B. M., et al. (2020) · Cell · doi:10.1016/j.cell.2020.04.035 · Cited by 2,284 · see citing works
Self-citationStructure 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
Self-citationHoffmann, M., Kleine-Weber, H., & Pöhlmann, S. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.04.022 · Cited by 1,852 · see citing works
Glowacka, 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
SARS-CoV-2 receptor ACE2 and TMPRSS2 are primarily expressed in bronchial transient secretory cells
Lukassen, S., Chua, R. L., Trefzer, T. B., Kahn, N. C., Schneider, M. A., Muley, T., Winter, H., Meister, M. A., Veith, C., Boots, A. W., et al. (2020) · The EMBO Journal · doi:10.15252/embj.20105114 · Cited by 1,082 · 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
Receptor and viral determinants of SARS‐coronavirus adaptation to human ACE2
Li, W., Zhang, C., Sui, J., Kuhn, J. H., Moore, M. J., Luo, S., Wong, S.-K., Huang, I., Xu, K., Vasilieva, N. Y., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600640 · Cited by 976 · see citing works
Self-citationHost 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
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
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
Self-citationShulla, A., Heald-Sargent, T. A., Subramanya, G., Zhao, J., Perlman, S. M., & Gallagher, T. (2010) · Journal of Virology · doi:10.1128/jvi.02062-10 · Cited by 686 · see citing works
SARS-CoV-2 receptor ACE2 and TMPRSS2 are primarily expressed in bronchial transient secretory cells
Lukassen, S., Chua, R. L., Trefzer, T. B., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2020105114 · Cited by 417 · see citing works
Huang, I., Bosch, B., Li, F., Li, W., Lee, K. H., Ghiran, S., Vasilieva, N. Y., Dermody, T. S., Harrison, S. C., Dormitzer, P. R., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508381200 · Cited by 373 · see citing works
Self-citationNo evidence for increased transmissibility from recurrent mutations in SARS-CoV-2
van Dorp, L., Richard, D., Tan, C. C. S., Shaw, L. P., Acman, M., & Balloux, F. (2020) · Nature Communications · doi:10.1038/s41467-020-19818-2 · Cited by 310 · see citing works
Muus, C., Luecken, M. D., Eraslan, G., Waghray, A., Heimberg, G., Sikkema, L., Kobayashi, Y., Vaishnav, E. D., Subramanian, A., Smilie, C., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.19.049254 · Cited by 245 · see citing works
Moore, M. J., Dorfman, T., Li, W., Wong, S. K., Li, Y., Kuhn, J. H., Coderre, J. A., Vasilieva, N. Y., Han, Z., Greenough, T. C., et al. (2004) · Journal of Virology · doi:10.1128/jvi.78.19.10628-10635.2004 · Cited by 236 · see citing works
Self-citationCharacterizations of SARS-CoV-2 mutational profile, spike protein stability and viral transmission
Laha, S., Chakraborty, J., Das, S., Manna, S. K., Biswas, S., & Chatterjee, R. (2020) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2020.104445 · Cited by 195 · see citing works
Structure and Properties of a Complex of α-Synuclein and a Single-Domain Camelid Antibody
Genst, E. D., Guilliams, T., Wellens, J., O’Day, E. M., Waudby, C. A., Meehan, S., Dumoulin, M., Hsu, S. D., Cremades, N., Verschueren, K. H. G., et al. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.07.001 · Cited by 185 · see citing works
Huang, Y., Yang, Z., Kong, W., & Nabel, G. J. (2004) · Journal of Virology · doi:10.1128/jvi.78.22.12557-12565.2004 · Cited by 127 · see citing works
No evidence for increased transmissibility from recurrent mutations in SARS-CoV-2Preprint
van Dorp, L., Richard, D., Tan, C. C. S., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.21.108506 · Cited by 92 · see citing works
Lokman, S. M., Rasheduzzaman, M., Salauddin, A., Barua, R., Tanzina, A. Y., Rumi, M. H., Hossain, M. I., Siddiki, A. Z., Mannan, A., & Hasan, M. M. (2020) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2020.104389 · Cited by 90 · see citing works
Laamarti, M., Alouane, T., Kartti, S., Chemao-Elfihri, M. W., Hakmi, M., Essabbar, A., Laamarti, M., Hlali, H., Bendani, H., Boumajdi, N., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0240345 · Cited by 85 · see citing works
Viral genomes reveal patterns of the SARS-CoV-2 outbreak in Washington State
Müller, N. F., Wagner, C., Frazar, C. D., Roychoudhury, P., Lee, J., Moncla, L. H., Pelle, B., Richardson, M. A., Ryke, E., Xie, H. J., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abf0202 · Cited by 66 · see citing works
The global population of SARS-CoV-2 is composed of six major subtypes
Morais, I. J., Polveiro, R. C., Souza, G. M., Bortolin, D. I., Sassaki, F. T., & Lima, A. T. M. (2020) · Scientific Reports · doi:10.1038/s41598-020-74050-8 · Cited by 62 · see citing works
The global population of SARS-CoV-2 is composed of six major subtypesPreprint
Morais, I. J., Polveiro, R. C., Souza, G. M., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.14.040782 · Cited by 25 · see citing works
Viral genomes reveal patterns of the SARS-CoV-2 outbreak in Washington StatePreprint
Müller, N. F., Wagner, C., Frazar, C. D., et al. (2020) · medRxiv · doi:10.1101/2020.09.30.20204230 · Cited by 23 · see citing works
Lokman, S. M., Rasheduzzaman, M., Salauddin, A., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.07.030924 · Cited by 20 · see citing works
Insights from the Association of SARS-CoV S-Protein with its Receptor, ACE2
Li, W., Choe, H., & Farzan, M. R. (2006) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-33012-9_36 · Cited by 15 · see citing works
Self-citationEmergence of multiple variants of SARS-CoV-2 with signature structural changesPreprint
Bhowmik, D., Pal, S., Lahiri, A., Talukdar, A., & Paul, S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.26.062471 · Cited by 13 · see citing works
Cortey, M., Li, Y., Díaz, I., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.16.099499 · Cited by 12 · see citing works
Insurgence and worldwide diffusion of genomic variants in SARS-CoV-2 genomesPreprint
Comandatore, F., Chiodi, A., Gabrieli, P., Biffignandi, G. B., Perini, M., Ricagno, S., Mascolo, E., Petazzoni, G., Ramazzotti, M., Rimoldi, S. G., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.30.071027 · Cited by 5 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Korber, B., Fischer, W. M., Gnanakaran, S., Yoon, H., Theiler, J., Abfalterer, W., Hengartner, N., Giorgi, E. E., Bhattacharya, T., Foley, B., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.043 · Cited by 4,281 · see citing works
Spike mutation D614G alters SARS-CoV-2 fitness
Plante, J. A., Liu, Y., Liu, J., Xia, H., Johnson, B. A., Lokugamage, K. G., Zhang, X., Muruato, A. E., Zou, J., Fontes-Garfias, C. R., et al. (2021) · Nature · doi:10.1038/s41586-020-2895-3 · Cited by 1,558 · 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
Self-citationEvaluating the Effects of SARS-CoV-2 Spike Mutation D614G on Transmissibility and Pathogenicity
Volz, E., Hill, V., McCrone, J. T., Price, A., Jorgensen, D., O’Toole, Á., Southgate, J., Johnson, R., Jackson, B., Nascimento, F. F., et al. (2021) · Cell · doi:10.1016/j.cell.2020.11.020 · Cited by 1,006 · see citing works
The biological and clinical significance of emerging SARS-CoV-2 variants
Tao, K., Tzou, P. L., Nouhin, J., Gupta, R. K., de Oliveira, T., Kosakovsky Pond, S. L., Fera, D., & Shafer, R. W. (2021) · Nature Reviews Genetics · doi:10.1038/s41576-021-00408-x · Cited by 1,009 · see citing works
SARS-CoV-2: Structure, Biology, and Structure-Based Therapeutics Development
Wang, M.-Y., Zhao, R., Gao, L.-J., Gao, X.-F., Wang, D.-P., & Cao, J.-M. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.587269 · Cited by 874 · see citing works
BNT162b2 vaccine induces neutralizing antibodies and poly-specific T cells in humans
Sahin, U., Muik, A., Vogler, I., Derhovanessian, E., Kranz, L. M., Vormehr, M., Quandt, J., Bidmon, N., Ulges, A., Baum, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03653-6 · Cited by 845 · see citing works
Loss of furin cleavage site attenuates SARS-CoV-2 pathogenesis
Johnson, B. A., Xie, X., Bailey, A. L., Kalveram, B., Lokugamage, K. G., Muruato, A., Zou, J., Zhang, X., Juelich, T., Smith, J. K., et al. (2021) · Nature · doi:10.1038/s41586-021-03237-4 · Cited by 694 · see citing works
Self-citationThomson, E. C., Rosen, L. E., Shepherd, J. G., Spreafico, R., da Silva Filipe, A., Wojcechowskyj, J. A., Davis, C., Piccoli, L., Pascall, D. J., Dillen, J., et al. (2021) · Cell · doi:10.1016/j.cell.2021.01.037 · Cited by 606 · 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
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 · see citing works
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
Anosmia in COVID-19: Underlying Mechanisms and Assessment of an Olfactory Route to Brain Infection
Butowt, R., & von Bartheld, C. S. (2021) · The Neuroscientist · doi:10.1177/1073858420956905 · Cited by 345 · 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
On the origin and evolution of SARS-CoV-2
Singh, D., & Yi, S. V. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00604-z · Cited by 281 · 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
Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe
Thakur, V., Bhola, S., Thakur, P., Patel, S. K. S., Kulshrestha, S., Ratho, R. K., & Kumar, P. (2022) · Infection · doi:10.1007/s15010-021-01734-2 · Cited by 210 · see citing works
“[24] reported a more efficient entry of pseudovirus SG614 with less S1 domain shedding in ACE-2 expressing cells.”
BackgroundDecline of Humoral Responses against SARS-CoV-2 Spike in Convalescent Individuals
Beaudoin-Bussières, G., Laumaea, A., Anand, S. P., Prévost, J., Gasser, R., Goyette, G., Medjahed, H., Perreault, J., Tremblay, T., Lewin, A., et al. (2020) · mBio · doi:10.1128/mbio.02590-20 · Cited by 189 · 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
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
Yang, R., Deng, Y., Huang, B., Huang, L., Lin, A., Li, Y., Wang, W., Liu, J., Lu, S., Zhan, Z., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00634-z · Cited by 130 · see citing works
Self-citationEvolution of enhanced innate immune evasion by the SARS-CoV-2 B.1.1.7 UK variant
Thorne, L. G., Bouhaddou, M., Reuschl, A.-K., Zuliani-Alvarez, L., Polacco, B., Pelin, A., Batra, J., Whelan, M. V. X., Ummadi, M., Rojc, A., et al. (2021) · doi:10.1101/2021.06.06.446826 · Cited by 91 · see citing works
Martin, D. P., Weaver, S., Tegally, H., San, E. J., Shank, S. D., Wilkinson, E., Lucaci, A. G., Giandhari, J., Naidoo, S., Pillay, Y., et al. (2021) · doi:10.1101/2021.02.23.21252268 · Cited by 291 · see citing works
Zhou, H., Dcosta, B. M., Samanovic, M. I., Mulligan, M. J., Landau, N. R., & Tada, T. (2021) · mBio · doi:10.1128/mbio.01386-21 · Cited by 68 · see citing works
Kruglova, N., Siniavin, A., Gushchin, V., & Mazurov, D. (2021) · Viruses · doi:10.3390/v13061133 · Cited by 37 · see citing works
Shooting at a Moving Target—Effectiveness and Emerging Challenges for SARS-CoV-2 Vaccine Development
Günl, F., Mecate-Zambrano, A., Rehländer, S., Hinse, S., Ludwig, S., & Brunotte, L. (2021) · Vaccines · doi:10.3390/vaccines9101052 · Cited by 27 · 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
Wang, Q., Nair, M. S., Anang, S., Zhang, S., Nguyen, H., Huang, Y., Liu, L., Ho, D. D., & Sodroski, J. G. (2021) · iScience · doi:10.1016/j.isci.2021.103393 · Cited by 15 · see citing works
An mRNA-based vaccine candidate against SARS-CoV-2 elicits stable immuno-response with single dose
Nag, K., Chandra Baray, J., Rahman Khan, M., Mahmud, A., Islam, J., Myti, S., Ali, R., Haq Sarker, E., Kumar, S., Hossain Chowdhury, M., et al. (2021) · Vaccine · doi:10.1016/j.vaccine.2021.05.035 · Cited by 13 · see citing works
Structural Analysis of Spike Protein Mutations in the SARS-CoV-2 P.3 Variant
Bascos, N. A. D., Mirano-Bascos, D., & Saloma, C. P. (2021) · doi:10.1101/2021.03.06.434059 · Cited by 11 · see citing works
Prompetchara, E., Ketloy, C., Alameh, M.-G., Tarakhet, K., Kaewpang, P., Yostrerat, N., Pitakpolrat, P., Buranapraditkun, S., Manopwisedcharoen, S., Thitithanyanont, A., et al. (2022) · doi:10.1101/2022.09.07.506878 · Cited by 1 · see citing works
- Authors
- Zhang, L., Jackson, C. B., Mou, H., Ojha, A., Peng, H., Quinlan, B. D., Rangarajan, E. S., Pan, A., Vanderheiden, A., Suthar, M. S., Li, W., Izard, T., Rader, C., Farzan, M., & Choe, H.
- Affiliations
- Scripps Research Institute (US)
- Emory University (US)
- National Institute of Biological Sciences, Beijing (CN)
- Corresponding author
- Farzan, Michael
- Choe, Hyeryun
- ORCID
- Venue
- Nature Communications
- Published
- 2020-11-26
- Volume
- 11
- Issue
- 1
- Pages
- 6013-6013
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC7693302
- OpenAlex
- W3107112434
- Cited by
- 1,387
- References
- 46
- Citations by year
- 2026: 23 · 2025: 56 · 2024: 88 · 2023: 162 · 2022: 329 · 2021: 519 · 2020: 209
- FWCI
- 40.02
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases (AI129868)
- 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, D614G mutation, viral infectivity, virus-like particles, ACE2 binding, neutralization sensitivity, pseudovirus, SARS-CoV-2 variants
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
