D614G Spike Mutation Increases SARS CoV-2 Susceptibility to Neutralization
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Abstract
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein acquired a D614G mutation early in the pandemic that confers greater infectivity and is now the globally dominant form. To determine whether D614G might also mediate neutralization escape that could compromise vaccine efficacy, sera from spike-immunized mice, nonhuman primates, and humans were evaluated for neutralization of pseudoviruses bearing either D614 or G614 spike. In all cases, the G614 pseudovirus was moderately more susceptible to neutralization. The G614 pseudovirus also was more susceptible to neutralization by receptor-binding domain (RBD) monoclonal antibodies and convalescent sera from people infected with either form of the virus. Negative stain electron microscopy revealed a higher percentage of the 1-RBD "up" conformation in the G614 spike, suggesting increased epitope exposure as a mechanism of enhanced vulnerability to neutralization. Based on these findings, the D614G mutation is not expected to be an obstacle for current vaccine development.
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Pseudovirus neutralization titers to D614G were threefold higher than to WA1.
“Similar to previous studies from our group (15) and others (18), pseudovirus neutralization titers to D614G were threefold higher than to WA1 (Fig. 2G).”
From Durability of mRNA-1273 vaccine–induced antibodies against SARS-CoV-2 variants (2021) · cites this paper as [18]
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R: A Language and Environment for Statistical Computing
R Core Team (2000) · doi:10.32614/r.manuals · Cited by 355,706 · see citing works
UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,260 · 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
In Vivo Gene Delivery and Stable Transduction of Nondividing Cells by a Lentiviral Vector
Naldini, L., Blömer, U., Gallay, P., Ory, D., Mulligan, R., Gage, F. H., Verma, I. M., & Trono, D. (1996) · Science · doi:10.1126/science.272.5259.263 · Cited by 4,903 · see citing works
mRNA vaccines — a new era in vaccinology
Pardi, N., Hogan, M. J., Porter, F. W., & Weissman, D. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.243 · Cited by 4,667 · 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
Self-citationAn 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 · cited 4× · see citing works
“This is the immunogen being employed in the Moderna vaccine in phase 3 clinical trials (mRNA1273, NCT04470427) (Jackson et al., 2020).”
InfluentialCOVID-19 vaccine BNT162b1 elicits human antibody and TH1 T cell responses
Sahin, U., Muik, A., Derhovanessian, E., Vogler, I., Kranz, L. M., Vormehr, M., Baum, A., Pascal, K., Quandt, J., Maurus, D., et al. (2020) · Nature · doi:10.1038/s41586-020-2814-7 · Cited by 1,977 · see citing works
Self-citationCross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2349-y · Cited by 1,885 · see citing works
Human 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
SARS-CoV-2 mRNA Vaccine Design Enabled by Prototype Pathogen Preparedness
Corbett, K. S., Edwards, D. K., Leist, S. R., Abiona, O. M., Boyoglu-Barnum, S., Gillespie, R. A., Himansu, S., Schäfer, A., Ziwawo, C. T., DiPiazza, A. T., et al. (2020) · Nature · doi:10.1038/s41586-020-2622-0 · Cited by 1,615 · see citing works
Mulligan, M. J., Lyke, K. E., Kitchin, N., Absalon, J., Gurtman, A., Lockhart, S., Neuzil, K., Raabe, V., Bailey, R., Swanson, K. A., et al. (2020) · doi:10.1101/2020.06.30.20142570 · Cited by 1,569 · see citing works
Self-citationDeveloping Covid-19 Vaccines at Pandemic Speed
Lurie, N., Saville, M., Hatchett, R., & Halton, J. (2020) · New England Journal of Medicine · doi:10.1056/nejmp2005630 · Cited by 1,557 · see citing works
A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV
Yuan, M., Wu, N. C., Zhu, X., Lee, C.-C. D., So, R. T. Y., Lv, H., Mok, C. K. P., & Wilson, I. A. (2020) · Science · doi:10.1126/science.abb7269 · Cited by 1,405 · 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
Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike
Liu, L., Wang, P., Nair, M. S., Yu, J., Rapp, M., Wang, Q., Luo, Y., Chan, J. F.-W., Sahi, V., Figueroa, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2571-7 · Cited by 1,349 · see citing works
A human neutralizing antibody targets the receptor-binding site of SARS-CoV-2
Shi, R., Shan, C., Duan, X., Chen, Z., Liu, P., Song, J., Song, T., Bi, X., Han, C., Wu, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2381-y · Cited by 1,286 · see citing works
Potent neutralizing antibodies from COVID-19 patients define multiple targets of vulnerability
Brouwer, P. J. M., Caniels, T. G., van der Straten, K., Snitselaar, J. L., Aldon, Y., Bangaru, S., Torres, J. L., Okba, N. M. A., Claireaux, M., Kerster, G., et al. (2020) · Science · doi:10.1126/science.abc5902 · Cited by 1,140 · 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
Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant
Yurkovetskiy, L., Wang, X., Pascal, K. E., Tomkins-Tinch, C., Nyalile, T. P., Wang, Y., Baum, A., Diehl, W. E., Dauphin, A., Carbone, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.032 · Cited by 1,025 · see citing works
Rapid Decay of Anti–SARS-CoV-2 Antibodies in Persons with Mild Covid-19
Ibarrondo, F. J., Fulcher, J. A., Goodman-Meza, D., Elliott, J., Hofmann, C., Hausner, M. A., Ferbas, K. G., Tobin, N. H., Aldrovandi, G. M., & Yang, O. O. (2020) · New England Journal of Medicine · doi:10.1056/nejmc2025179 · Cited by 1,021 · see citing works
Pardi, N., Tuyishime, S., Muramatsu, H., Kariko, K., Mui, B. L., Tam, Y. K., Madden, T. D., Hope, M. J., & Weissman, D. (2015) · Journal of Controlled Release · doi:10.1016/j.jconrel.2015.08.007 · Cited by 1,014 · see citing works
Self-citationWu, Y., Wang, F., Shen, C., Peng, W., Li, D., Zhao, C., Li, Z., Li, S., Bi, Y., Yang, Y., et al. (2020) · Science · doi:10.1126/science.abc2241 · Cited by 955 · see citing works
SARS-CoV-2 D614G variant exhibits efficient replication ex vivo and transmission in vivo
Hou, Y. J., Chiba, S., Halfmann, P., Ehre, C., Kuroda, M., Dinnon, K. H., Leist, S. R., Schäfer, A., Nakajima, N., Takahashi, K., et al. (2020) · Science · doi:10.1126/science.abe8499 · Cited by 900 · see citing works
A Bayesian View on Cryo-EM Structure Determination
Scheres, S. H. W. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.11.010 · Cited by 875 · 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
ter Meulen, J., van den Brink, E. N., Poon, L. L. M., Marissen, W. E., Leung, C. S.-W., Cox, F., Cheung, C. Y., Bakker, A. Q., Bogaards, J. A., van Deventer, E., et al. (2006) · PLoS Medicine · doi:10.1371/journal.pmed.0030237 · Cited by 599 · see citing works
Geographic and Genomic Distribution of SARS-CoV-2 Mutations
Mercatelli, D., & Giorgi, F. M. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01800 · Cited by 589 · see citing works
The D614G mutation in the SARS-CoV-2 spike protein reduces S1 shedding and increases infectivityPreprint
Zhang, L., Jackson, C. B., Mou, H., et al. (2020) · bioRxiv · doi:10.1101/2020.06.12.148726 · Cited by 576 · see citing works
Measuring SARS-CoV-2 neutralizing antibody activity using pseudotyped and chimeric viruses
Schmidt, F., Weisblum, Y., Muecksch, F., Hoffmann, H.-H., Michailidis, E., Lorenzi, J. C. C., Mendoza, P., Rutkowska, M., Bednarski, E., Gaebler, C., et al. (2020) · Journal of Experimental Medicine · doi:10.1084/jem.20201181 · Cited by 572 · see citing works
A facile method for the removal of dsRNA contaminant from in vitro-transcribed mRNA
Baiersdörfer, M., Boros, G., Muramatsu, H., Mahiny, A., Vlatkovic, I., Sahin, U., & Karikó, K. (2019) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2019.02.018 · Cited by 569 · see citing works
Self-citationProcessing of Structurally Heterogeneous Cryo-EM Data in RELION
Scheres, S. H. W. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.04.012 · Cited by 550 · see citing works
Pardi, N., Hogan, M. J., Naradikian, M. S., Parkhouse, K., Cain, D. W., Jones, L., Moody, M. A., Verkerke, H. P., Myles, A., Willis, E., et al. (2018) · Journal of Experimental Medicine · doi:10.1084/jem.20171450 · Cited by 530 · see citing works
Self-citationVariant analysis of SARS-CoV-2 genomes
Koyama, T., Platt, D. E., & Parida, L. (2020) · Bulletin of the World Health Organization · doi:10.2471/blt.20.253591 · Cited by 527 · see citing works
Broad neutralization of SARS-related viruses by human monoclonal antibodies
Wec, A. Z., Wrapp, D., Herbert, A. S., Maurer, D. P., Haslwanter, D., Sakharkar, M., Jangra, R. K., Dieterle, M. E., Lilov, A., Huang, D., et al. (2020) · Science · doi:10.1126/science.abc7424 · Cited by 520 · see citing works
Spike mutation pipeline reveals the emergence of a more transmissible form of SARS-CoV-2Preprint
Korber, B., Fischer, W., Gnanakaran, S., et al. (2020) · bioRxiv · doi:10.1101/2020.04.29.069054 · Cited by 473 · see citing works
Self-citationKirchdoerfer, 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. (2018) · Scientific Reports · doi:10.1038/s41598-018-34171-7 · Cited by 466 · see citing works
Controlling the SARS-CoV-2 spike glycoprotein conformation
Henderson, R. C., Edwards, R. J., Mansouri, K., Janowska, K., Stalls, V., Gobeil, S., Kopp, M., Li, D., Parks, R., Hsu, A. L., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0479-4 · Cited by 409 · see citing works
Self-citationLaczko, D. I., Hogan, M. J., Toulmin, S. A., Hicks, P. D., Lederer, K., Gaudette, B. T., Castaño, D., Amanat, F., Muramatsu, H., Oguin, T. H., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.07.019 · Cited by 366 · see citing works
Self-citationGobeil, 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 320 · see citing works
Self-citationFreyn, A. W., Ramos da Silva, J., Rosado, V. C., Bliss, C. M., Pine, M., Mui, B. L., Tam, Y. K., Madden, T. D., de Souza Ferreira, L. C., Weissman, D., et al. (2020) · Molecular Therapy · doi:10.1016/j.ymthe.2020.04.018 · Cited by 299 · see citing works
Self-citationEmergence of Drift Variants That May Affect COVID-19 Vaccine Development and Antibody Treatment
Koyama, T., Weeraratne, D., Snowdon, J. L., & Parida, L. (2020) · Pathogens · doi:10.3390/pathogens9050324 · Cited by 223 · see citing works
The SARS-CoV-2 Spike Variant D614G Favors an Open Conformational StatePreprint
Mansbach, R., Chakraborty, S., Nguyen, K., Montefiori, D., Korber, B., & Gnanakaran, G. (2020) · bioRxiv · doi:10.1101/2020.07.26.219741 · Cited by 207 · see citing works
Self-citationThe 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
Self-citationPilson, D., & Decker, K. (2002) · Ecology · doi:10.1890/0012-9658(2002)083[3097:cfhiws]2.0.co;2 · Cited by 201 · see citing works
Isabel, S., Graña-Miraglia, L., Gutierrez, J. M., Bundalovic-Torma, C., Groves, H. E., Isabel, M. R., Eshaghi, A., Patel, S. N., Gubbay, J. B., Poutanen, T., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-70827-z · Cited by 197 · see citing works
Very Fast Folding and Association of a Trimerization Domain from Bacteriophage T4 Fibritin
Güthe, S., Kapinos, L. E., Möglich, A., Meier, S., Grzesiek, S., & Kiefhaber, T. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.020 · Cited by 138 · see citing works
Gong, Y., Tsao, K., Hsiao, M., Huang, C., Huang, P.-N., Huang, P.-W., Lee, K.-M., Liu, Y., Yang, S.-L., Kuo, R.-L., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1782271 · Cited by 129 · see citing works
Lin, P. J. C., Tam, Y. Y. C., Hafez, I. M., Sandhu, A. P., Chen, S., Ciufolini, M. A., Nabi, I. R., & Cullis, P. R. (2012) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2012.05.019 · Cited by 101 · see citing works
Self-citationMessenger RNA-Based Vaccines Against Infectious Diseases
Alameh, M.-G., Weissman, D., & Pardi, N. (2020) · Current Topics in Microbiology and Immunology · doi:10.1007/82_2020_202 · Cited by 96 · see citing works
Self-citationBiswas, N. K., & Majumder, P. P. (2020) · The Indian Journal of Medical Research · doi:10.4103/ijmr.ijmr_1125_20 · Cited by 78 · see citing works
Concurrent human antibody and T H 1 type T-cell responses elicited by a COVID-19 RNA vaccinePreprint
Şahin, U., Muik, A., Derhovanessian, E., et al. (2020) · medRxiv · doi:10.1101/2020.07.17.20140533 · Cited by 67 · see citing works
Self-citationEmergence of European and North American mutant variants of SARS‐CoV‐2 in South‐East Asia
Islam, O. K., Al‐Emran, H. M., Hasan, M. S., Anwar, A., Jahid, I. K., & Hossain, M. A. (2020) · Transboundary and Emerging Diseases · doi:10.1111/tbed.13748 · Cited by 53 · see citing works
Stabilized HIV-1 envelope glycoprotein trimers for vaccine use
Medina-Ramírez, M., Sanders, R. W., & Sattentau, Q. J. (2017) · Current Opinion in HIV and AIDS · doi:10.1097/coh.0000000000000363 · Cited by 37 · see citing works
Gobeil, S., Janowska, K., McDowell, S., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.11.335299 · Cited by 29 · see citing works
Self-citationThe Resolution Revolution: Recent Advances In cryoEM
(2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(16)x0011-0 · Cited by 28 · see citing works
Emergence of European and North American mutant variants of SARS-CoV-2 in Southeast AsiaPreprint
Islam, O. K., emran, H. A., Hasan, M. S., et al. (2020) · doi:10.22541/au.159112172.23549094 · Cited by 19 · see citing works
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SARS-CoV-2 variants, spike mutations and immune escape
Harvey, W. T., Carabelli, A. M., Jackson, B., Gupta, R. K., Thomson, E. C., Harrison, E. M., Ludden, C., Reeve, R., Rambaut, A., COVID-19 Genomics UK (COG-UK) Consortium, et al. (2021) · Nature Reviews Microbiology · doi:10.1038/s41579-021-00573-0 · Cited by 3,528 · see citing works
Mechanisms of SARS-CoV-2 entry into cells
Jackson, C. B., Farzan, M., Chen, B., & Choe, H. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00418-x · Cited by 3,082 · see citing works
Greaney, A. J., Starr, T. N., Gilchuk, P., Zost, S. J., Binshtein, E., Loes, A. N., Hilton, S. K., Huddleston, J., Eguia, R., Crawford, K. H. D., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2020.11.007 · Cited by 1,016 · 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 variants B.1.351 and P.1 escape from neutralizing antibodies
Hoffmann, M., Arora, P., Groß, R., Seidel, A., Hörnich, B. F., Hahn, A. S., Krüger, N., Graichen, L., Hofmann-Winkler, H., Kempf, A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.036 · Cited by 897 · see citing works
SARS-CoV-2 D614G variant exhibits efficient replication ex vivo and transmission in vivo
Hou, Y. J., Chiba, S., Halfmann, P., Ehre, C., Kuroda, M., Dinnon, K. H., Leist, S. R., Schäfer, A., Nakajima, N., Takahashi, K., et al. (2020) · Science · doi:10.1126/science.abe8499 · Cited by 900 · see citing works
Alameh, M.-G., Tombácz, I., Bettini, E., Lederer, K., Ndeupen, S., Sittplangkoon, C., Wilmore, J. R., Gaudette, B. T., Soliman, O. Y., Pine, M., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.11.001 · Cited by 775 · see citing works
Self-citationSensitivity of infectious SARS-CoV-2 B.1.1.7 and B.1.351 variants to neutralizing antibodies
Planas, D., Bruel, T., Grzelak, L., Guivel-Benhassine, F., Staropoli, I., Porrot, F., Planchais, C., Buchrieser, J., Rajah, M. M., Bishop, E., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01318-5 · Cited by 697 · see citing works
Thomson, 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
Genetic Variants of SARS-CoV-2—What Do They Mean?
Lauring, A. S., & Hodcroft, E. B. (2021) · JAMA · doi:10.1001/jama.2020.27124 · Cited by 604 · see citing works
Durability of mRNA-1273 vaccine–induced antibodies against SARS-CoV-2 variants
Pegu, A., O’Connell, S. E., Schmidt, S. D., O’Dell, S., Talana, C. A., Lai, L., Albert, J., Anderson, E., Bennett, H., Corbett, K. S., et al. (2021) · Science · doi:10.1126/science.abj4176 · Cited by 527 · see citing works
Structural impact on SARS-CoV-2 spike protein by D614G substitution
Zhang, J., Cai, Y., Xiao, T., Lu, J., Peng, H., Sterling, S. M., Walsh, R. M., Rits‐Volloch, S., Zhu, H., Woosley, A. N., et al. (2021) · Science · doi:10.1126/science.abf2303 · Cited by 402 · see citing works
Ella, R., Vadrevu, K. M., Jogdand, H., Prasad, S., Reddy, S., Sarangi, V., Ganneru, B., Sapkal, G., Yadav, P., Abraham, P., et al. (2021) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(20)30942-7 · Cited by 424 · see citing works
Duan, L., Zheng, Q., Zhang, H., Niu, Y., Lou, Y., & Wang, H. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.576622 · Cited by 403 · 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
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
Self-citationSARS-CoV-2 501Y.V2 variants lack higher infectivity but do have immune escape
Li, Q., Nie, J., Wu, J., Zhang, L., Ding, R., Wang, H., Zhang, Y., Li, T., Liu, S., Zhang, M., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.042 · Cited by 341 · see citing works
Dispinseri, S., Secchi, M., Pirillo, M. F., Tolazzi, M., Borghi, M., Brigatti, C., Angelis, M. L. D., Baratella, M., Bazzigaluppi, E., Venturi, G., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22958-8 · Cited by 334 · see citing works
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 320 · see citing works
Self-citationAdjuvanting a subunit COVID-19 vaccine to induce protective immunity
Arunachalam, P. S., Walls, A. C., Golden, N., Atyeo, C. G., Fischinger, S., Li, C., Aye, P. P., Navarro, M. J., Lai, L., Edara, V. V., et al. (2021) · Nature · doi:10.1038/s41586-021-03530-2 · Cited by 326 · see citing works
Self-citationQu, P., Evans, J. P., Faraone, J. N., Zheng, Y.-M., Carlin, C., Anghelina, M. I., Stevens, P., Fernández, S., Jones, D. M., Lozanski, G., et al. (2022) · Cell Host & Microbe · doi:10.1016/j.chom.2022.11.012 · Cited by 296 · see citing works
Wang, R., Zhang, Q., Ge, J., Ren, W., Zhang, R., Lan, J., Ju, B., Su, B., Yu, F., Chen, P., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.06.003 · Cited by 240 · 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
Self-citationSARS-CoV-2 Mutations and their Viral Variants
Coşar, B., KARAGÜLLEOĞLU, Z. Y., ÜNAL, S., İnce, A. T., Uncuoglu, D. B., Tuncer, G., Kilinc, B. R., Ozkan, Y. E., Ozkoc, H. C., Demir, I. N., et al. (2021) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2021.06.001 · Cited by 199 · see citing works
Recognition of the SARS-CoV-2 receptor binding domain by neutralizing antibodies
Yuan, M., Liu, H., Wu, N. C., & Wilson, I. A. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.10.012 · Cited by 181 · see citing works
Proteolytic activation of SARS‐CoV‐2 spike protein
Takeda, M. (2021) · Microbiology and Immunology · doi:10.1111/1348-0421.12945 · Cited by 182 · see citing works
Effects of SARS-CoV-2 variants on vaccine efficacy and response strategies
Bian, L., Gao, F., Zhang, J., He, Q., Mao, Q., Xu, M., & Liang, Z. (2021) · Expert Review of Vaccines · doi:10.1080/14760584.2021.1903879 · Cited by 181 · see citing works
Kinetics and correlates of the neutralizing antibody response to SARS-CoV-2 infection in humans
Vanshylla, K., Di Cristanziano, V., Kleipass, F., Dewald, F., Schommers, P., Gieselmann, L., Gruell, H., Schlotz, M., Ercanoglu, M. S., Stumpf, R., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.04.015 · Cited by 153 · see citing works
Immune Responses Induced by mRNA Vaccination in Mice, Monkeys and Humans
Cagigi, A., & Loré, K. (2021) · Vaccines · doi:10.3390/vaccines9010061 · Cited by 153 · see citing works
The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2
Benton, D. J., Wrobel, A. G., Roustan, C., Borg, A., Xu, P., Martin, S. R., Rosenthal, P. B., Skehel, J. J., & Gamblin, S. J. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2022586118 · Cited by 153 · see citing works
Anti-SARS-CoV-2 neutralizing monoclonal antibodies: clinical pipeline
Tuccori, M., Ferraro, S., Convertino, I., Cappello, E., Valdiserra, G., Blandizzi, C., Maggi, F., & Focosi, D. (2020) · mAbs · doi:10.1080/19420862.2020.1854149 · Cited by 155 · see citing works
SARS-CoV-2 one year on: evidence for ongoing viral adaptation
Peacock, T. P., Penrice-Randal, R., Hiscox, J. A., & Barclay, W. (2021) · Journal of General Virology · doi:10.1099/jgv.0.001584 · Cited by 149 · see citing works
Graham, C., Seow, J., Huettner, I., Khan, H., Kouphou, N., Acors, S., Winstone, H., Pickering, S., Galão, R. P., Dupont, L., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.03.023 · Cited by 130 · see citing works
Focosi, D., & Maggi, F. (2021) · Reviews in Medical Virology · doi:10.1002/rmv.2231 · Cited by 148 · see citing works
Mapping SARS-CoV-2 antigenic relationships and serological responses
Wilks, S. H., Mühlemann, B., Shen, X., Türeli, S., LeGresley, E. B., Netzl, A., Caniza, M. A., Chacaltana-Huarcaya, J. N., Corman, V. M., Daniell, X. G., et al. (2023) · Science · doi:10.1126/science.adj0070 · Cited by 134 · see citing works
Self-citationEvolutionary trajectory of SARS-CoV-2 and emerging variants
Singh, J., Pandit, P., McArthur, A. G., Banerjee, A., & Mossman, K. L. (2021) · Virology Journal · doi:10.1186/s12985-021-01633-w · Cited by 144 · see citing works
SARS-CoV-2 Neutralizing Antibodies for COVID-19 Prevention and Treatment
Li, D., Sempowski, G. D., Saunders, K. O., Acharya, P., & Haynes, B. F. (2021) · Annual Review of Medicine · doi:10.1146/annurev-med-042420-113838 · Cited by 132 · see citing works
Self-citationSpike deep mutational scanning helps predict success of SARS-CoV-2 clades
Dadonaite, B., Brown, J. T., McMahon, T. E., Farrell, A. G., Figgins, M. D., Asarnow, D. E., Stewart, C., Lee, J., Logue, J., Bedford, T., et al. (2024) · Nature · doi:10.1038/s41586-024-07636-1 · Cited by 141 · see citing works
Sokal, A., Spaeth, G. B., Fernández, I., Broketa, M., Azzaoui, I., Selle, A. D. L., Vandenberghe, A., Fourati, S., Roeser, A., Meola, A., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.09.011 · Cited by 128 · see citing works
Groves, D. C., Rowland‐Jones, S., & Angyal, A. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.10.109 · Cited by 130 · see citing works
Gorman, M. J., Patel, N., Guebre‐Xabier, M., Zhu, A. L., Atyeo, C. G., Pullen, K. M., Loos, C., Goez-Gazi, Y., Carrion, R., Tian, J.-H., et al. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100405 · Cited by 121 · see citing works
Self-citationEmerging SARS-CoV-2 Variants of Concern (VOCs): An Impending Global Crisis
Thye, A. Y.-K., Law, J. W., Pusparajah, P., Letchumanan, V., Chan, K., & Lee, L. (2021) · Biomedicines · doi:10.3390/biomedicines9101303 · Cited by 116 · see citing works
Therapeutic targets and interventional strategies in COVID-19: mechanisms and clinical studies
Zhou, Y., Xie, Y., Tang, L., Pu, D., Zhu, Y., Liu, J., & Ma, X. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00733-x · Cited by 115 · see citing works
SARS-CoV-2 spike protein: pathogenesis, vaccines, and potential therapies
Almehdi, A. M., Khoder, G., Alchakee, A., Alsayyid, A. T., Sarg, N. H., & Soliman, S. S. M. (2021) · Infection · doi:10.1007/s15010-021-01677-8 · Cited by 113 · see citing works
Hypoxic and Pharmacological Activation of HIF Inhibits SARS-CoV-2 Infection of Lung Epithelial Cells
Wing, P. A. C., Keeley, T. P., Zhuang, X., Lee, Y. S., Prange‐Barczynska, M., Tsukuda, S., Morgan, S. B., Harding, A. C., Argles, I. L. A., Kurlekar, S., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2021.109020 · Cited by 107 · see citing works
HIV-1 and SARS-CoV-2: Patterns in the evolution of two pandemic pathogens
Fischer, W., Giorgi, E. E., Chakraborty, S., Nguyen, K., Tanmoy Bhattacharya, A., Theiler, J. P., Goloboff, P. A., Yoon, H., Abfalterer, W., Foley, B. T., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.05.012 · Cited by 106 · see citing works
Self-citationEvaluation of Cell-Based and Surrogate SARS-CoV-2 Neutralization Assays
Sholukh, A. M., Fiore-Gartland, A. J., Ford, E. S., Miner, M. D., Hou, Y. J., Tse, L. V., Kaiser, H., Zhu, H., Lu, J., Madarampalli, B., et al. (2021) · Journal of Clinical Microbiology · doi:10.1128/jcm.00527-21 · Cited by 119 · see citing works
Self-citationTroyer, Z., Alhusaini, N., Tabler, C. O., Sweet, T. J., Carvalho, K. I., Schlatzer, D., Carias, L. L., King, C. L., Matreyek, K. A., & Tilton, J. C. (2021) · Journal of Extracellular Vesicles · doi:10.1002/jev2.12112 · Cited by 86 · see citing works
Conformational dynamics and allosteric modulation of the SARS-CoV-2 spike
Díaz-Salinas, M. A., Li, Q., Ejemel, M., Yurkovetskiy, L., Luban, J., Shen, K., Wang, Y., & Munro, J. B. (2022) · eLife · doi:10.7554/elife.75433 · Cited by 80 · see citing works
Functional importance of the D614G mutation in the SARS-CoV-2 spike protein
Jackson, C. B., Zhang, L., Farzan, M., & Choe, H. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.11.026 · Cited by 90 · see citing works
Neidleman, J. A., Luo, X., McGregor, M. M., Xie, G., Murray, V., Greene, W. C., Lee, S. A., & Roan, N. R. (2021) · eLife · doi:10.7554/elife.72619 · Cited by 88 · see citing works
Tian, J., Sun, J., Li, D., Wang, N., Wang, L., Zhang, C., Meng, X., Ji, X., Suchard, M. A., Zhang, X., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110969 · Cited by 90 · see citing works
Will Mutations in the Spike Protein of SARS-CoV-2 Lead to the Failure of COVID-19 Vaccines?
Jia, Z.-X., & Gong, W. (2021) · Journal of Korean medical science · doi:10.3346/jkms.2021.36.e124 · Cited by 87 · see citing works
A multivalent mRNA-LNP vaccine protects against Clostridioides difficile infection
Alameh, M., Semon, A., Bayard, N. U., Pan, Y., Dwivedi, G., Knox, J. J., Glover, R. C., Rangel, P. C., Tanes, C., Bittinger, K. L., et al. (2024) · Science · doi:10.1126/science.adn4955 · Cited by 85 · see citing works
Self-citationRational design of anti‐inflammatory lipid nanoparticles for mRNA delivery
Zhang, H., Han, X., Alameh, M., Shepherd, S. J., Padilla, M. S., Xue, L., Butowska, K., Weissman, D., & Mitchell, M. J. (2022) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.37356 · Cited by 82 · see citing works
Self-citationEmerging SARS-CoV-2 Variants: Genetic Variability and Clinical Implications
Dubey, A., Choudhary, S., Kumar, P., & Tomar, S. (2021) · Current Microbiology · doi:10.1007/s00284-021-02724-1 · Cited by 79 · see citing works
Development and deployment of COVID-19 vaccines for those most vulnerable
Koff, W. C., Schenkelberg, T., Williams, T. M., Baric, R. S., McDermott, A. B., Cameron, C., Cameron, M. J., Frieman, M. B., Neumann, G., Kawaoka, Y., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abd1525 · Cited by 78 · see citing works
Chen, C., Boorla, V. S., Banerjee, D., Chowdhury, R., Cavener, V. S., Nissly, R. H., Gontu, A., Boyle, N. R., Vandegrift, K. J., Nair, M. S., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2106480118 · Cited by 79 · see citing works
Lipid Nanoparticle Delivery Systems to Enable mRNA-Based Therapeutics
Semple, S. C., Leone, R. D., Barbosa, C., Tam, Y. K., & Lin, P. J. C. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14020398 · Cited by 80 · see citing works
Self-citationMonitoring of SARS‐CoV‐2 infection in mustelids
Boklund, A., Gortázar, C., Pasquali, P., Roberts, H., Nielsen, S., Ståhl, K., Stegeman, A., Baldinelli, F., Broglia, A., der Stede, Y. V., et al. (2021) · EFSA journal. European Food Safety Authority · doi:10.2903/j.efsa.2021.6459 · Cited by 82 · see citing works
Shastri, J. S., Parikh, S., Aggarwal, V., Agrawal, S. R., Chatterjee, N., Shah, R. J., Devi, P., Mehta, P., & Pandey, R. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.737007 · Cited by 78 · see citing works
Rotondo, J. C., Martini, F., Maritati, M., Mazziotta, C., Mauro, G. D., Lanzillotti, C., Barp, N., Gallerani, A., Tognon, M. G., & Contini, C. (2021) · Viruses · doi:10.3390/v13091687 · Cited by 78 · see citing works
Tao, K., Tzou, P. L., Pond, S. L. K., Ioannidis, J. P. A., & Shafer, R. W. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.00926-22 · Cited by 80 · see citing works
Pino, M., Abid, T., Ribeiro, S. P., Edara, V. V., Floyd, K. A., Smith, J. C., Latif, M. B., Sánchez, G. P., Dutta, D., Wang, S., et al. (2021) · Science Immunology · doi:10.1126/sciimmunol.abh3634 · Cited by 77 · see citing works
Self-citationSARS-CoV-2 Omicron sublineages exhibit distinct antibody escape patterns
Gruell, H., Vanshylla, K., Korenkov, M., Tober‐Lau, P., Zehner, M., Münn, F., Janicki, H., Augustin, M., Schommers, P., Sander, L. E., et al. (2022) · Cell Host & Microbe · doi:10.1016/j.chom.2022.07.002 · Cited by 75 · see citing works
Bowen, J. E., Park, Y., Stewart, C., Brown, J. T., Sharkey, W. K., Walls, A. C., Joshi, A., Sprouse, K. R., McCallum, M., Tortorici, M. A., et al. (2022) · Science Immunology · doi:10.1126/sciimmunol.adf1421 · Cited by 81 · see citing works
mRNA Vaccines against SARS-CoV-2: Advantages and Caveats
Echaide, M., Chocarro, L., Bocanegra, A., Blanco, E., Kochan, G. T., & Escors, D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065944 · Cited by 82 · see citing works
Ilmjärv, S., Abdul, F., Acosta‐Gutiérrez, S., Estarellas, C., Galdadas, I., Casimir, M., Alessandrini, M., Gervasio, F. L., & Krause, K. (2021) · Scientific Reports · doi:10.1038/s41598-021-91662-w · Cited by 73 · see citing works
Immunogenicity and efficacy of one and two doses of Ad26.COV2.S COVID vaccine in adult and aged NHP
Solforosi, L., Kuipers, H., Jongeneelen, M. A. C., Huber, S. K. R., van der Lubbe, J. E. M., Dekking, L., Czapska-Casey, D. N., Gil, A. I., Baert, M. R. M., Drijver, J., et al. (2021) · The Journal of Experimental Medicine · doi:10.1084/jem.20202756 · Cited by 71 · see citing works
Mutations in SARS-CoV-2 structural proteins: a global analysis
Abavisani, M., Rahimian, K., Mahdavi, B., Tokhanbigli, S., Sisakht, M. M., Farhadi, A., Kodori, M., Mahmanzar, M., & Meshkat, Z. (2022) · Virology Journal · doi:10.1186/s12985-022-01951-7 · Cited by 69 · see citing works
Noori, M., Nejadghaderi, S. A., Arshi, S., Carson‐Chahhoud, K., Ansarin, K., Kolahi, A., & Safiri, S. (2021) · Reviews in Medical Virology · doi:10.1002/rmv.2277 · Cited by 64 · see citing works
SARS-CoV-2 variants and effectiveness of vaccines: a review of current evidence
Tatsi, E., Filippatos, F., & Michos, A. G. (2021) · Epidemiology and Infection · doi:10.1017/s0950268821002430 · Cited by 63 · see citing works
Appelberg, S., John, L., Pardi, N., Végvári, Á., Bereczky, S., Ahlén, G., Monteil, V., Abdurahman, S., Mikaeloff, F., Beattie, M., et al. (2021) · Journal of Virology · doi:10.1128/jvi.01568-21 · Cited by 66 · see citing works
Self-citationStructures of Omicron spike complexes and implications for neutralizing antibody development
Guo, H., Gao, Y., Li, T., Li, T., Lu, Y., Zheng, L., Liu, Y., Yang, T., Luo, F., Song, S., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110770 · Cited by 59 · see citing works
Zhang, Z., Zeng, E., Zhang, L., Wang, W., Jin, Y., Sun, J., Huang, S., Yin, W., Dai, J., Zhuang, Z., et al. (2021) · Cell Discovery · doi:10.1038/s41421-021-00302-0 · Cited by 59 · see citing works
von Bartheld, C. S., Hagen, M. M., & Butowt, R. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00542 · Cited by 60 · see citing works
Onodera, T., Kita, S., Adachi, Y., Moriyama, S., Sato, A., Nomura, T., Sakakibara, S., Inoue, T., Tadokoro, T., Anraku, Y., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.08.025 · Cited by 56 · see citing works
Banach, B. B., Cerutti, G., Fahad, A. S., Shen, C., de Souza, M. O., Katsamba, P. S., Tsybovsky, Y., Wang, P., Nair, M. S., Huang, Y., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2021.109771 · Cited by 56 · see citing works
Valdés-Balbín, Y., Santana-Mederos, D., Paquet, F., Fernández-Castillo, S., Climent, Y., Chiodo, F., Rodríguez, L., Ramírez, B. S., León, K., Hernández, T., et al. (2021) · ACS Central Science · doi:10.1021/acscentsci.1c00216 · Cited by 53 · see citing works
Valenzuela, G., Jara, R., Watterson, D., Modhiran, N., Amarilla, A. A., Himelreichs, J., Khromykh, A. A., Salinas-Rebolledo, C., Pinto, T., Cheuquemilla, Y., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-82833-w · Cited by 52 · see citing works
Kang, Y., Sun, C., Sun, J., Xie, C., Zhuang, Z., Xu, H.-Q., Liu, Z., Liu, Y., Peng, S., Yuan, R., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30222-w · Cited by 56 · see citing works
Moubarak, M., Kasozi, K. I., Hetta, . F., Shaheen, H. M., Rauf, A., Al-Kuraishy, H. M., Qusti, S. Y., Alshammari, E. M., Ayikobua, E. T., Ssempijja, F., et al. (2021) · Life · doi:10.3390/life11080734 · Cited by 55 · see citing works
Understanding the Secret of SARS-CoV-2 Variants of Concern/Interest and Immune Escape
Lou, F., Li, M., Pang, Z., Jiang, L., Guan, L., Tian, L., Hu, J., Fan, J., & Fan, H. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.744242 · Cited by 53 · see citing works
The way of SARS-CoV-2 vaccine development: success and challenges
Dong, Y., Dai, T., Wang, B., Zhang, L., Zeng, L., Huang, J., Yan, H., Zhang, L., & Zhou, F. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00796-w · Cited by 53 · see citing works
D614G mutation and SARS-CoV-2: impact on S-protein structure, function, infectivity, and immunity
Bhattacharya, M., Chatterjee, S., Sharma, A. R., Agoramoorthy, G., & Chakraborty, C. (2021) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-021-11676-2 · Cited by 50 · see citing works
High‐Precision Synthesis of RNA‐Loaded Lipid Nanoparticles for Biomedical Applications
Seo, H., Jeon, L., Kwon, J., & Lee, H. (2023) · Advanced Healthcare Materials · doi:10.1002/adhm.202203033 · Cited by 51 · see citing works
An Overview of Vaccines against SARS-CoV-2 in the COVID-19 Pandemic Era
Pascual‐Iglesias, A., Cantón, J., Ortega‐Prieto, A. M., Jiménez-Guardeño, J. M., & Regla-Nava, J. Á. (2021) · Pathogens · doi:10.3390/pathogens10081030 · Cited by 48 · see citing works
Xu, K., Dai, L., & Gao, G. F. (2021) · International Immunology · doi:10.1093/intimm/dxab061 · Cited by 48 · see citing works
Immunity to SARS-CoV-2: Lessons Learned
FERGIE, J. E., & Srivastava, A. K. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.654165 · Cited by 45 · see citing works
The Genetic Variant of SARS-CoV-2: Would it matter for Controlling the Devastating Pandemic?
Guo, S., Liu, K., & Zheng, J. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.59137 · Cited by 46 · see citing works
Intranasal gene therapy to prevent infection by SARS-CoV-2 variants
Sims, J. J., Greig, J. A., Michalson, K. T., Lian, S., Martino, R. A., Meggersee, R., Turner, K. B., Nambiar, K., Dyer, C., Hinderer, C. J., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009544 · Cited by 42 · see citing works
Schulze, H., Hoffmann, D., & Bayer, W. (2022) · Frontiers in Virology · doi:10.3389/fviro.2022.880707 · Cited by 45 · see citing works
Molecular insights into the adaptive evolution of SARS-CoV-2 spike protein
Yao, Z., Zhang, L., Duan, Y., Tang, X., & Lü, J. (2024) · Journal of Infection · doi:10.1016/j.jinf.2024.106121 · Cited by 46 · see citing works
Ali, M. A., Hu, C., Zhang, F., Jahan, S., Yuan, B., Saleh, M. S., Gao, S., & Panat, R. P. (2022) · Journal of Medical Virology · doi:10.1002/jmv.27591 · Cited by 46 · see citing works
Schuurs, Z. P., Hammond, E., Elli, S., Rudd, T. R., Mycroft‐West, C. J., de Lima, M. A., Skidmore, M. A., Karlsson, R. T. G., Chen, Y., Bagdonaite, I., et al. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.05.002 · Cited by 43 · see citing works
Ding, C., He, J., Zhang, X., Jiang, C., Sun, Y. C., Zhang, Y., Chen, Q., He, H., Li, W., Xie, J., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.693775 · Cited by 45 · see citing works
Moghaddar, M., Radman, R., & Macreadie, I. G. (2021) · Microorganisms · doi:10.3390/microorganisms9102167 · Cited by 45 · see citing works
The impact of Spike mutations on SARS-CoV-2 neutralizationPreprint
Rees-Spear, C., Muir, L., Griffith, S. A., Heaney, J., Aldon, Y., Snitselaar, J. L., Pataillot-Meakin, T., Graham, C., Seow, J., Lee, N., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.15.426849 · Cited by 45 · see citing works
Whole-genome sequencing of SARS-CoV-2 reveals the detection of G614 variant in Pakistan
Umair, M., Ikram, A., Salman, M., Khurshid, A., Alam, M., Badar, N., Suleman, R., Tahir, F., Sharif, S., Montgomery, J. M., et al. (2021) · PLoS ONE · doi:10.1371/journal.pone.0248371 · Cited by 42 · see citing works
SARS-CoV-2 genomic characterization and clinical manifestation of the COVID-19 outbreak in Uruguay
Elizondo, V., Harkins, G. W., Mabvakure, B. M., Smidt, S., Zappile, P., Marier, C., Maurano, M. T., Perez, V., Mazza, N., Beloso, C., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1863747 · Cited by 41 · see citing works
- Authors
- Weissman, D., Alameh, M.-G., de Silva, T., Collini, P., Hornsby, H., Brown, R., LaBranche, C. C., Edwards, R. J., Sutherland, L., Santra, S., Mansouri, K., Gobeil, S., McDanal, C., Pardi, N., Hengartner, N., Lin, P. J. C., Tam, Y., Shaw, P. A., Lewis, M. G., Boesler, C., Şahin, U., Acharya, P., Haynes, B. F., Korber, B., & Montefiori, D. C.
- Affiliations
- University of Pennsylvania (US)
- Sheffield Teaching Hospitals NHS Foundation Trust (GB)
- University of Sheffield (GB)
- Duke University (US)
- Beth Israel Deaconess Medical Center (US)
- Acuitas Therapeutics (Canada) (CA)
- Bioqual (US)
- BioNTech (Germany) (DE)
- Los Alamos National Laboratory (US)
- Corresponding author
- Weissman, Drew
- ORCID
- Weissman, Drew
- Alameh, Mohamad-Gabriel
- Collini, Paul
- Hornsby, Hailey
- Brown, Rebecca
- LaBranche, Celia C.
- Edwards, Robert J.
- Sutherland, Laura
- Santra, Sampa
- Mansouri, Katayoun
- Gobeil, Sophie
- McDanal, Charlene
- Pardi, Norbert
- Lin, Paulo J.C.
- Tam, Ying
- Shaw, Pamela A.
- Lewis, Mark G.
- Boesler, Carsten
- Şahin, Uğur
- Acharya, Priyamvada
- Haynes, Barton F.
- Korber, Bette
- Montefiori, David C.
- Venue
- Cell Host & Microbe
- Publisher
- Elsevier BV
- Published
- 2021-01
- Volume
- 29
- Issue
- 1
- Pages
- 23-31.e4
- ISSN
- 1931-3128 (ISSN-L)
- PMC
- PMC7707640
- OpenAlex
- W3108737416
- Cited by
- 324
- References
- 57
- Citations by year
- 2026: 6 · 2025: 7 · 2024: 17 · 2023: 33 · 2022: 72 · 2021: 173 · 2020: 16
- FWCI
- 9.59
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Host & Microbe (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- National Institutes of Health (75N93019C00050, HHSN272201800004C, R01 - AI145687)
- Wellcome Trust (110058/Z/15/Z)
- National Institute of Allergy and Infectious Diseases (AI142596, AI124429, R01AI123738, 1R01AI146101)
- University of Pennsylvania
- National Institute for Health Research
- Laboratory Directed Research and Development (20200706ER)
- Bill and Melinda Gates Foundation (OPP1146996)
- UK Research and Innovation
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Keywords
- SARS-CoV-2, spike protein, D614G mutation, neutralizing antibodies, neutralization escape, receptor binding domain, monoclonal antibodies, convalescent sera, epitope exposure, vaccine efficacy, pseudovirus
- MeSH terms
- COVID-19, SARS-CoV-2, COVID-19 Vaccines, COVID-19 Serotherapy, Adolescent, Adult, Animals, Antibodies, Monoclonal, Binding Sites, Female, Humans, Immunization, Passive, Macaca mulatta, Male, Mice, Inbred BALB C, Middle Aged, Mutation, Neutralization Tests, Mice, Young Adult, HEK293 Cells, 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.
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