Identification of SARS-CoV-2 spike mutations that attenuate monoclonal and serum antibody neutralization
Open accessAbstract
Neutralizing antibodies against the SARS-CoV-2 spike (S) protein are a goal of COVID-19 vaccines and have received emergency use authorization as therapeutics. However, viral escape mutants could compromise efficacy. To define immune-selected mutations in the S protein, we exposed a VSV-eGFP-SARS-CoV-2-S chimeric virus, in which the VSV glycoprotein is replaced with the S protein, to 19 neutralizing monoclonal antibodies (mAbs) against the receptor-binding domain (RBD) and generated 50 different escape mutants. Each mAb had a unique resistance profile, although many shared residues within an epitope of the RBD. Some variants (e.g., S477N) were resistant to neutralization by multiple mAbs, whereas others (e.g., E484K) escaped neutralization by convalescent sera. Additionally, sequential selection identified mutants that escape neutralization by antibody cocktails. Comparing these antibody-mediated mutations with sequence variation in circulating SARS-CoV-2 revealed substitutions that may attenuate neutralizing immune responses in some humans and thus warrant further investigation.
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?
F490S helps Lambda escape convalescent sera and neutralizing antibodies from CoronaVac and reduces in vitro susceptibility to neutralization.
“F490S mutation helps the Lambda variant to escape convalescent sera and neutralizing antibodies from the CoronaVac vaccine and also reduced in vitro susceptibility to neutralization [54].”
From Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe (2022) · cites this paper as [54]
The Results section reports that F490S resisted neutralization by three convalescent sera in a VSV-SARS-CoV-2 assay, supporting reduced in vitro susceptibility for that mutation. The cited paper does not establish this result for the Lambda variant or for antibodies elicited by CoronaVac. (LLM, conf=0.90)
Experimental — accuracy not yet measuredSeveral Omicron RBD mutations were previously shown to modulate ACE2 binding and/or antibody evasion.
“several were previously shown to modulate ACE2 binding and/or antibody evasion”
From The Omicron variant is highly resistant against antibody-mediated neutralization: Implications for control of the COVID-19 pandemic (2022) · cites this paper as Liu et al., 2021
E484K substitution is a vulnerability for multiple neutralizing mAbs.
“Our results establishing the E484K substitution as a vulnerability for multiple neutralizing mAbs are consistent with deep mutational scanning or VSV-SARS-CoV-2-based neutralization escape screening campaigns31,33,34.”
From Resistance of SARS-CoV-2 variants to neutralization by monoclonal and serum-derived polyclonal antibodies (2021) · cites this paper as [34]
E484K has resulted in 3-fold to 10-fold reduced susceptibility to about 30% and >10-fold reduced susceptibility to about 10% of convalescent plasma samples.
“E484K has resulted in 3-fold to 10-fold reduced susceptibility to about 30% and >10-fold reduced susceptibility to about 10% of convalescent plasma samples”
From The biological and clinical significance of emerging SARS-CoV-2 variants (2021) · cites this paper as [160]
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
Hoffmann, M., Kleine-Weber, H., Schroeder, S., Krüger, N., Herrler, T., Erichsen, S., Schiergens, T. S., Herrler, G., Wu, N.-H., Nitsche, A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.02.052 · Cited by 20,286 · cited 1× · see citing works
“Processing of S by host cell proteases, typically TMPRSS2, TMPRSS4, or endosomal cathepsins, facilitates the S2-dependent fusion of viral and host-cell membranes (Hoffmann et al., 2020; Zang et al., 2020).”
BackgroundA new coronavirus associated with human respiratory disease in China
Wu, F., Zhao, S., Yu, B., Chen, Y.-M., Wang, W., Song, Z.-G., Hu, Y., Tao, Z.-W., Tian, J.-H., Pei, Y.-Y., et al. (2020) · Nature · doi:10.1038/s41586-020-2008-3 · Cited by 11,688 · 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 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 · cited 1× · see citing works
“The impact of SARS-CoV-2 adaptation for infection of other hosts including mice (Dinnon et al., 2020; Gu et al., 2020), mink (Oude Munnink et al., 2021), and domesticated animals (Halfmann et al., 2020; Shi et al., 2020) could also contribute to selection of new variants.”
BackgroundStructural 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 · cited 1× · see citing works
“Residue F486 is located on the top of the hACE2 contact loop of RBD, and the presence of a large hydrophobic residue facilitates efficient receptor engagement (Lan et al., 2020; Shang et al., 2020).”
BackgroundLetko, M., Marzi, A., & Munster, V. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0688-y · Cited by 3,109 · cited 2× · see citing works
“During viral entry into cells, the receptor-binding domain (RBD) of S1 engages the primary receptor, human angiotensin converting enzyme 2 (hACE2) (Letko et al., 2020).”
BackgroundTegally, H., Wilkinson, E., Giovanetti, M., Iranzadeh, A., Fonseca, V., Giandhari, J., Doolabh, D., Pillay, S., San, E. J., Msomi, N., et al. (2020) · doi:10.1101/2020.12.21.20248640 · Cited by 2,535 · cited 1× · see citing works
“a combination of at least two neutralizing antibodies (Baum et al., 2020; Du et al., 2020; 316 Greaney et al., 2020; Group et al., 2020; Li et al., 2020; Weisblum et al., 2020).”
BackgroundDetection of a SARS-CoV-2 variant of concern in South Africa
Tegally, H., Wilkinson, E., Giovanetti, M., Iranzadeh, A., Fonseca, V., Giandhari, J., Doolabh, D., Pillay, S., San, E. J., Msomi, N., et al. (2021) · Nature · doi:10.1038/s41586-021-03402-9 · Cited by 2,510 · see citing works
Monteil, V., Kwon, H., Prado, P., Hagelkrüys, A., Wimmer, R. A., Stahl, M., Leopoldi, A., Garreta, E., Hurtado del Pozo, C., Prosper, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.04.004 · Cited by 2,122 · see citing works
Starr, T. N., Greaney, A. J., Hilton, S. K., Ellis, D., Crawford, K. H. D., Dingens, A. S., Navarro, M. J., Bowen, J. E., Tortorici, M. A., Walls, A. C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.012 · Cited by 1,956 · see citing works
Susceptibility of ferrets, cats, dogs, and other domesticated animals to SARS–coronavirus 2
Shi, J., Wen, Z., Zhong, G., Yang, H., Wang, C., Huang, B., Liu, R., He, X., Shuai, L., Sun, Z., et al. (2020) · Science · doi:10.1126/science.abb7015 · Cited by 1,908 · see citing works
REGN-COV2, a Neutralizing Antibody Cocktail, in Outpatients with Covid-19
Weinreich, D. M., Sivapalasingam, S., Norton, T., Ali, S., Gao, H., Bhore, R., Musser, B. J., Soo, Y., Rofail, D., Im, J., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmoa2035002 · Cited by 1,642 · see citing works
The Impact of Mutations in SARS-CoV-2 Spike on Viral Infectivity and Antigenicity
Li, Q., Wu, J., Nie, J., Zhang, L., Hao, H., Liu, S., Zhao, C., Zhang, Q., Liu, H., Nie, L., et al. (2020) · Cell · doi:10.1016/j.cell.2020.07.012 · Cited by 1,420 · cited 2× · see citing works
“The relatively low genetic barrier to resistance combined with knowledge of the presence of relevant substitutions in clinical isolates suggests that effective mAb therapy will likely require a combination of at least two neutralizing antibodies (ACTIV-3/ TICO LY-CoV555 Study Group, 2020; Baum et al., 2020; Du et al.,…”
BackgroundEscape from neutralizing antibodies by SARS-CoV-2 spike protein variants
Weisblum, Y., Schmidt, F., Zhang, F., DaSilva, J., Poston, D., Lorenzi, J. C., Muecksch, F., Rutkowska, M., Hoffmann, H.-H., Michailidis, E., et al. (2020) · eLife · doi:10.7554/elife.61312 · Cited by 1,308 · see citing works
SARS-CoV-2 Neutralizing Antibody LY-CoV555 in Outpatients with Covid-19
Chen, P., Nirula, A., Heller, B., Gottlieb, R. L., Boscia, J., Morris, J., Huhn, G., Cardona, J., Mocherla, B., Stosor, V., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmoa2029849 · Cited by 1,282 · cited 1× · see citing works
“Therapeutic candidates that have received emergency use authorization (EUA) or are in development include several monoclonal antibodies (mAbs) (ACTIV-3/TICO LY-CoV555 Study Group, 2020; Chen et al., 2021; Weinreich et al., 2021) that recognize the SARS-CoV-2 spike (S) protein, which decorates the virion surface (Ke et…”
BackgroundBaum, A., Fulton, B. O., Wloga, E., Copin, R., Pascal, K. E., Russo, V., Giordano, S., Lanza, K., Negron, N., Ni, M., et al. (2020) · Science · doi:10.1126/science.abd0831 · Cited by 1,253 · see citing works
Sanjuán, R., Nebot, M. R., Chirico, N., Mansky, L. M., & Belshaw, R. D. (2010) · Journal of Virology · doi:10.1128/jvi.00694-10 · Cited by 1,247 · cited 1× · see citing works
“The intrinsically high error rates of viral RNA-dependent RNA polymerases (RdRp) result in the stochastic introduction of mutations during viral genome replication with substitutions approaching a nucleotide change per genome for each round of replication (Sanjuán et al., 2010).”
BackgroundRogers, T. F., Zhao, F., Huang, D., Beutler, N., Burns, A., He, W.-T., Limbo, O., Smith, C., Song, G., Woehl, J., et al. (2020) · Science · doi:10.1126/science.abc7520 · Cited by 1,230 · 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
Structures and distributions of SARS-CoV-2 spike proteins on intact virions
Ke, Z., Otón, J., Qu, K., Cortese, M., Žíla, V., McKeane, L., Nakane, T., Zivanov, J., Neufeldt, C. J., Cerikan, B., et al. (2020) · Nature · doi:10.1038/s41586-020-2665-2 · Cited by 1,113 · see citing works
Transmission of SARS-CoV-2 on mink farms between humans and mink and back to humans
Munnink, B. B. O., Sikkema, R. S., Nieuwenhuijse, D. F., Molenaar, R. J., Münger, E., Molenkamp, R., van der Spek, A. N., Tolsma, P., Rietveld, A., Brouwer, M., et al. (2020) · Science · doi:10.1126/science.abe5901 · Cited by 1,087 · see citing works
Potently neutralizing and protective human antibodies against SARS-CoV-2
Zost, S. J., Gilchuk, P., Case, J. B., Binshtein, E., Chen, R. E., Nkolola, J. P., Schäfer, A., Reidy, J. X., Trivette, A., Nargi, R. S., et al. (2020) · Nature · doi:10.1038/s41586-020-2548-6 · Cited by 1,041 · see citing works
Self-citationGreaney, 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
Self-citationDomingo, E., Sheldon, J., & Perales, C. (2012) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.05023-11 · Cited by 1,009 · cited 1× · see citing works
“We did not directly address the fitness of the mutants generated in this study, and any studies of the fitness of the VSVSARS-CoV-2 variants would pertain to their relative replicative fitness measured in cell culture (Domingo et al., 2012).”
BackgroundTMPRSS2 and TMPRSS4 promote SARS-CoV-2 infection of human small intestinal enterocytes
Zang, R., Castro, M. F. G., McCune, B. T., Zeng, Q., Rothlauf, P. W., Sonnek, N. M., Liu, Z., Brulois, K. F., Wang, X., Greenberg, H. B., et al. (2020) · Science Immunology · doi:10.1126/sciimmunol.abc3582 · Cited by 982 · see citing works
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
Adaptation of SARS-CoV-2 in BALB/c mice for testing vaccine efficacy
Gu, H., Chen, Q., Yang, G., He, L., Fan, H., Deng, Y.-Q., Wang, Y., Teng, Y., Zhao, Z., Cui, Y., et al. (2020) · Science · doi:10.1126/science.abc4730 · Cited by 762 · see citing works
A mouse-adapted model of SARS-CoV-2 to test COVID-19 countermeasures
Dinnon, K. H., Leist, S. R., Schäfer, A., Edwards, C. E., Martinez, D. R., Montgomery, S. A., West, A., Yount, B. L., Hou, Y. J., Adams, L. E., et al. (2020) · Nature · doi:10.1038/s41586-020-2708-8 · Cited by 675 · see citing works
Engineering human ACE2 to optimize binding to the spike protein of SARS coronavirus 2
Chan, K. K., Dorosky, D. E., Sharma, P. A., Abbasi, S. A., Dye, J. M., Kranz, D. M., Herbert, A. S., & Procko, E. (2020) · Science · doi:10.1126/science.abc0870 · Cited by 613 · see citing works
Transmission of SARS-CoV-2 in Domestic Cats
Halfmann, P., Hatta, M., Chiba, S., Maemura, T., Fan, S., Takeda, M., Kinoshita, N., Hattori, S.-I., Sakai‐Tagawa, Y., Iwatsuki‐Horimoto, K., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmc2013400 · Cited by 465 · cited 1× · see citing works
“, 2021), and domesticated animals (Halfmann et al., 2020; Shi et al., 2020) could also contribute to selection of new variants.”
BackgroundA Neutralizing Monoclonal Antibody for Hospitalized Patients with Covid-19
ACTIV-3/TICO LY-CoV555 Study Group (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2033130 · Cited by 433 · see citing works
Smith, E. C., Blanc, H., Vignuzzi, M., & Denison, M. R. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003565 · Cited by 428 · cited 1× · see citing works
“As a result of ExoN activity, the frequency of escape from antibody neutralization by coronaviruses is less than for other RNA viruses lacking such an enzyme (Smith et al., 2013).”
BackgroundCase, J. B., Rothlauf, P. W., Chen, R. E., Liu, Z., Zhao, H., Kim, A. S., Bloyet, L.-M., Zeng, Q., Tahan, S., Droit, L., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.06.021 · Cited by 410 · see citing works
Self-citationBroadly protective human antibodies that target the active site of influenza virus neuraminidase
Stadlbauer, D., Zhu, X., McMahon, M., Turner, J. S., Wohlbold, T. J., Schmitz, A. J., Strohmeier, S., Yu, W., Nachbagauer, R., Mudd, P. A., et al. (2019) · Science · doi:10.1126/science.aay0678 · Cited by 261 · see citing works
Self-citationDu, S., Cao, Y., Zhu, Q., Yü, P., Qi, F., Wang, G., Du, X., Bao, L., Deng, W., Zhu, H., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.035 · Cited by 238 · see citing works
A Potently Neutralizing Antibody Protects Mice against SARS-CoV-2 Infection
Alsoussi, W. B., Turner, J. S., Case, J. B., Zhao, H., Schmitz, A. J., Zhou, J. Q., Chen, R. E., Lei, T., Rizk, A. A., McIntire, K. M., et al. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.2000583 · Cited by 181 · see citing works
Self-citationCoronaviruses as DNA Wannabes: A New Model for the Regulation of RNA Virus Replication Fidelity
Smith, E. C., & Denison, M. R. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003760 · Cited by 107 · cited 10× · see citing works
“See Figures S1 and S2. ll Article (Figure S2).”
BackgroundInfluentialMapping the Evolutionary Potential of RNA Viruses
Dolan, P., Whitfield, Z. J., & Andino, R. (2018) · Cell Host & Microbe · doi:10.1016/j.chom.2018.03.012 · Cited by 91 · cited 2× · see citing works
“RNA viruses exist as a swarm or ‘‘quasispecies’’ of genome sequences around a core consensus sequence (Dolan et al., 2018).”
Background
Flagged first, then by citations
Cited by
Sorted by citations
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
Detection of a SARS-CoV-2 variant of concern in South Africa
Tegally, H., Wilkinson, E., Giovanetti, M., Iranzadeh, A., Fonseca, V., Giandhari, J., Doolabh, D., Pillay, S., San, E. J., Msomi, N., et al. (2021) · Nature · doi:10.1038/s41586-021-03402-9 · Cited by 2,510 · see citing works
Greaney, A. J., Loes, A. N., Crawford, K. H. D., Starr, T. N., Malone, K. D., Chu, H. Y., & Bloom, J. D. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.02.003 · Cited by 1,178 · see citing works
Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift
Cameroni, E., Bowen, J. E., Rosen, L. E., Saliba, C., Zepeda, S. K., Culap, K., Pinto, D., VanBlargan, L. A., Marco, A. D., di Iulio, J., et al. (2021) · Nature · doi:10.1038/s41586-021-04386-2 · Cited by 1,043 · see citing works
Self-citationN-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2
McCallum, M., De Marco, A., Lempp, F. A., Tortorici, M. A., Pinto, D., Walls, A. C., Beltramello, M., Chen, A., Liu, Z., Zatta, F., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.028 · Cited by 901 · see citing works
Self-citationChen, R. E., Zhang, X., Case, J. B., Winkler, E. S., Liu, Y., VanBlargan, L. A., Liu, J., Errico, J. M., Xie, X., Suryadevara, N., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01294-w · Cited by 881 · see citing works
Self-citationThe 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
Hoffmann, M., Krüger, N., Schulz, S., Cossmann, A., Rocha, C., Kempf, A., Nehlmeier, I., Graichen, L., Moldenhauer, A.-S., Winkler, M. S., et al. (2022) · Cell · doi:10.1016/j.cell.2021.12.032 · Cited by 889 · see citing works
“Another 15 mutations are found in the RBD (Figure 1C-E), of which G339D, S371L, S373P and S375F are unique, and several were previously shown to modulate ACE2 binding and/or antibody evasion (Harvey et al., 2021b; Li et al., 2021b; Liu et al., 2021; Wang et al., 2021; Wheatley et al., 2021).”
InfluentialSARS-CoV-2 mRNA vaccines induce persistent human germinal centre responses
Turner, J. S., O’Halloran, J. A., Kalaidina, E., Kim, W., Schmitz, A. J., Zhou, J. Q., Lei, T., Thapa, M., Chen, R. E., Case, J. B., et al. (2021) · Nature · doi:10.1038/s41586-021-03738-2 · Cited by 831 · see citing works
Self-citationNeutralizing monoclonal antibodies for treatment of COVID-19
Taylor, P. C., Adams, A. C., Hufford, M. M., de la Torre, I., Winthrop, K., & Gottlieb, R. L. (2021) · Nature Reviews Immunology · doi:10.1038/s41577-021-00542-x · Cited by 732 · see citing works
SARS-CoV-2 Omicron is an immune escape variant with an altered cell entry pathway
Willett, B. J., Grove, J., MacLean, O. A., Wilkie, C., De Lorenzo, G., Furnon, W., Cantoni, D., Scott, S., Logan, N., Ashraf, S., et al. (2022) · Nature Microbiology · doi:10.1038/s41564-022-01143-7 · Cited by 785 · see citing works
Sensitivity 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
Cherian, S., Potdar, V. A., Jadhav, S., Yadav, P. D., Gupta, N., Das, M., Rakshit, P., Singh, S. K., Abraham, P., Panda, S., et al. (2021) · Microorganisms · doi:10.3390/microorganisms9071542 · Cited by 706 · see citing works
VanBlargan, L. A., Errico, J. M., Halfmann, P., Zost, S. J., Crowe, J. E., Purcell, L. A., Kawaoka, Y., Corti, D., Fremont, D. H., & Diamond, M. (2022) · Nature Medicine · doi:10.1038/s41591-021-01678-y · Cited by 676 · see citing works
Self-citationDeng, X., Garcia-Knight, M. A., Khalid, M. M., Servellita, V., Wang, C., Morris, M. K., Sotomayor-González, A., Glasner, D. R., Reyes, K. R., Gliwa, A. S., et al. (2021) · doi:10.1101/2021.03.07.21252647 · Cited by 651 · see citing works
Escape of SARS-CoV-2 501Y.V2 from neutralization by convalescent plasma
Network for Genomic Surveillance in South Africa, Cele, S., COMMIT-KZN Team, Gazy, I., Jackson, L., Hwa, S.-H., Tegally, H., Lustig, G., Giandhari, J., Pillay, S., et al. (2021) · Nature · doi:10.1038/s41586-021-03471-w · Cited by 651 · 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
SARS-CoV-2 spike L452R variant evades cellular immunity and increases infectivity
Motozono, C., Toyoda, M., Zahradnik, J., Saito, A., Nasser, H., Tan, T. S., Ngare, I., Kimura, I., Uriu, K., Kosugi, Y., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.06.006 · Cited by 586 · see citing works
Transmission, infectivity, and neutralization of a spike L452R SARS-CoV-2 variant
Deng, X., Garcia-Knight, M. A., Khalid, M. M., Servellita, V., Wang, C., Morris, M. K., Sotomayor-González, A., Glasner, D. R., Reyes, K. R., Gliwa, A. S., et al. (2021) · Cell · doi:10.1016/j.cell.2021.04.025 · Cited by 651 · see citing works
Starr, T. N., Greaney, A. J., Dingens, A. S., & Bloom, J. D. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100255 · Cited by 470 · see citing works
SARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape
Starr, T. N., Czudnochowski, N., Liu, Z., Zatta, F., Park, Y., Addetia, A., Pinto, D., Beltramello, M., Hernandez, P., Greaney, A. J., et al. (2021) · Nature · doi:10.1038/s41586-021-03807-6 · Cited by 495 · see citing works
Self-citationSARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern
McCallum, M., Bassi, J., De Marco, A., Chen, A., Walls, A. C., Di Iulio, J., Tortorici, M. A., Navarro, M.-J., Silacci-Fregni, C., Saliba, C., et al. (2021) · Science · doi:10.1126/science.abi7994 · Cited by 412 · see citing works
Mapping mutations to the SARS-CoV-2 RBD that escape binding by different classes of antibodies
Greaney, A. J., Starr, T. N., Barnes, C. O., Weisblum, Y., Schmidt, F., Caskey, M., Gaebler, C., Cho, A., Agudelo, M., Finkin, S., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24435-8 · Cited by 433 · see citing works
Effect of Immunosuppression on the Immunogenicity of mRNA Vaccines to SARS-CoV-2
Deepak, P., Kim, W., Paley, M., Yang, M. M., Carvidi, A. B., Demissie, E., El‐Qunni, A. A., Haile, A., Huang, K., Kinnett, B., et al. (2021) · Annals of Internal Medicine · doi:10.7326/m21-1757 · Cited by 416 · see citing works
“Neutralization assays on sera to determine the magnitude of functional S-specific antibodies that prevent the in vitro infectivity of virus were performed using a fluorescencebasedplatform,which leveraged a chimeric vesicular stomatitis virus (VSV) pseudotyped with the common variant strain (D614G) of the S protein of…”
MethodSelf-citationLY-CoV1404 (bebtelovimab) potently neutralizes SARS-CoV-2 variants
Westendorf, K., Žentelis, S., Wang, L., Foster, D., Vaillancourt, P., Wiggin, M., Lovett, E., van der Lee, R., Hendle, J., Pustilnik, A., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110812 · Cited by 398 · see citing works
Lu, L., Mok, B. W.-Y., Chen, L. L., Chan, J. M. C., Tsang, O. T. Y., Lam, B. H. S., Chuang, V. W., Chu, A. W., Chan, W. M., Ip, J. D., et al. (2021) · Clinical Infectious Diseases · doi:10.1093/cid/ciab1041 · Cited by 390 · see citing works
SARS-CoV-2 infection in free-ranging white-tailed deer
Hale, V. L., Dennis, P. M., McBride, D. S., Nolting, J. M., Madden, C. C., Huey, D. D., Ehrlich, M., Grieser, J. M., Winston, J. A., Lombardi, D., et al. (2021) · Nature · doi:10.1038/s41586-021-04353-x · Cited by 404 · see citing works
Broad betacoronavirus neutralization by a stem helix–specific human antibody
Pinto, D., Sauer, M. M., Czudnochowski, N., Low, J. S., Tortorici, M. A., Housley, M. P., Noack, J., Walls, A. C., Bowen, J. E., Guarino, B., et al. (2021) · Science · doi:10.1126/science.abj3321 · Cited by 381 · see citing works
Tackling COVID-19 with neutralizing monoclonal antibodies
Corti, D., Purcell, L. A., Snell, G., & Veesler, D. (2021) · Cell · doi:10.1016/j.cell.2021.05.005 · Cited by 375 · see citing works
Ai, J., Zhang, H., Zhang, Y., Lin, K., Zhang, Y., Wu, J., Wan, Y., Huang, Y., Song, J., Fu, Z., et al. (2022) · Emerging Microbes & Infections · doi:10.1080/22221751.2021.2022440 · Cited by 339 · see citing works
“[10] Liu Z, VanBlargan LA, Bloyet LM, et al.”
BackgroundSARS-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
Germinal centre-driven maturation of B cell response to mRNA vaccination
Kim, W., Zhou, J. Q., Horvath, S. C., Schmitz, A. J., Sturtz, A. J., Lei, T., Liu, Z., Kalaidina, E., Thapa, M., Alsoussi, W. B., et al. (2022) · Nature · doi:10.1038/s41586-022-04527-1 · Cited by 345 · see citing works
Self-citationNovel SARS-CoV-2 variants: the pandemics within the pandemic
Boehm, E., Kronig, I., Neher, R. A., Eckerle, I., Vetter, P., & Kaiser, L. (2021) · Clinical Microbiology and Infection · doi:10.1016/j.cmi.2021.05.022 · Cited by 341 · see citing works
The variant gambit: COVID-19’s next move
Plante, J. A., Mitchell, B. M., Plante, K. S., Debbink, K., Weaver, S. C., & Menachery, V. D. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.02.020 · Cited by 328 · see citing works
Infection and Vaccine-Induced Neutralizing-Antibody Responses to the SARS-CoV-2 B.1.617 Variants
Edara, V.-V., Pinsky, B. A., Suthar, M. S., Lai, L., Davis-Gardner, M. E., Floyd, K., Flowers, M. W., Wrammert, J., Hussaini, L., Ciric, C. R., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmc2107799 · Cited by 328 · see citing works
de Puig, H., Lee, R. A., Najjar, D., Tan, X. J., Soenksen, L. R., Angenent-Mari, N. M., Donghia, N. M., Weckman, N. E., Ory, A. L. H., Ng, C. F., et al. (2021) · Science Advances · doi:10.1126/sciadv.abh2944 · Cited by 326 · see citing works
Defining variant-resistant epitopes targeted by SARS-CoV-2 antibodies: A global consortium study
Hastie, K. M., Li, H., Bedinger, D., Schendel, S. L., Dennison, S. M., Li, K., Rayaprolu, V., Yu, X., Mann, C. J., Zandonatti, M. A., et al. (2021) · Science · doi:10.1126/science.abh2315 · Cited by 299 · see citing works
Structural biology of SARS-CoV-2: open the door for novel therapies
Yan, W., Zheng, Y., Zeng, X., He, B., & Cheng, W. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00884-5 · Cited by 293 · see citing works
“T478K mutation was previously selected in vitro and shown to exhibit reduced neutralization by monoclonal antibodies and human convalescent sera.(79) The significantly increased immune escape capacity to neutralize antibodies of this variant may be related to the RBD mutations and their combination with NTD mutations.”
BackgroundGenetic and structural basis for SARS-CoV-2 variant neutralization by a two-antibody cocktail
Dong, J., Zost, S. J., Greaney, A. J., Starr, T. N., Dingens, A. S., Chen, E. C., Chen, R. E., Case, J. B., Sutton, R. E., Gilchuk, P., et al. (2021) · Nature Microbiology · doi:10.1038/s41564-021-00972-2 · Cited by 285 · see citing works
Self-citationMuecksch, F., Weisblum, Y., Barnes, C., Schmidt, F., Schaefer-Babajew, D. J., Wang, Z.-J., Lorenzi, J. C. C., Flyak, A., DeLaitsch, A. T., Huey-Tubman, K. E., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.07.008 · Cited by 256 · see citing works
“Affinity matured antibodies exhibit activity against SARS-CoV-2 VOC Selection for rVSV/SARS-CoV-2 resistance to class 1, 2, and 3 antibodies in cell culture has repeatedly identified K417, E484, and N501 substitutions, with E484K giving the most pervasive effects against polyclonal plasma (Baum et al., 2020; Greaney e…”
BackgroundBroad sarbecovirus neutralization by a human monoclonal antibody
Tortorici, M. A., Czudnochowski, N., Starr, T. N., Marzi, R., Walls, A. C., Zatta, F., Bowen, J. E., Jaconi, S., di Iulio, J., Wang, Z., et al. (2021) · Nature · doi:10.1038/s41586-021-03817-4 · Cited by 251 · see citing works
Self-citationThe germinal centre B cell response to SARS-CoV-2
Laidlaw, B. J., & Ellebedy, A. H. (2021) · Nature reviews. Immunology · doi:10.1038/s41577-021-00657-1 · Cited by 250 · see citing works
Self-citationBroadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift
Cameroni, E., Bowen, J. E., Rosen, L. E., Saliba, C., Zepeda, S. K., Culap, K., Pinto, D., VanBlargan, L. A., Marco, A. D., di Iulio, J., et al. (2021) · Nature · doi:10.1038/d41586-021-03825-4 · Cited by 247 · see citing works
Self-citationCopin, R., Baum, A., Wloga, E., Pascal, K. E., Giordano, S., Fulton, B. O., Zhou, A., Negron, N., Lanza, K., Chan, N., et al. (2021) · Cell · doi:10.1016/j.cell.2021.06.002 · Cited by 212 · see citing works
Hoffmann, M., Hofmann-Winkler, H., Krüger, N., Kempf, A., Nehlmeier, I., Graichen, L., Arora, P., Sidarovich, A., Moldenhauer, A.-S., Winkler, M. S., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109415 · Cited by 258 · see citing works
Monoclonal antibodies for COVID-19 therapy and SARS-CoV-2 detection
Hwang, Y., Lu, R., Su, S.-C., Chiang, P.-Y., Ko, S.-H., Ke, F.-Y., Liang, K.-H., Hsieh, T.-Y., & Wu, H. (2022) · Journal of Biomedical Science · doi:10.1186/s12929-021-00784-w · Cited by 236 · see citing works
SARS-COV-2 Variants: Differences and Potential of Immune Evasion
Hirabara, S. M., Serdan, T. D. A., Gorjão, R., Masi, L. N., Pithon‐Curi, T. C., Covas, D. T., Curi, R., & Durigon, E. L. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.781429 · Cited by 216 · see citing works
In vivo monoclonal antibody efficacy against SARS-CoV-2 variant strains
Chen, R. E., Winkler, E. S., Case, J. B., Aziati, I. D., Bricker, T. L., Joshi, A., Darling, T. L., Ying, B., Errico, J. M., Shrihari, S., et al. (2021) · Nature · doi:10.1038/s41586-021-03720-y · Cited by 209 · see citing works
Self-citationMutations and Evolution of the SARS-CoV-2 Spike Protein
Magazine, N., Zhang, T., Wu, Y., McGee, M. C., Veggiani, G., & Huang, W. (2022) · Viruses · doi:10.3390/v14030640 · Cited by 218 · see citing works
Tchesnokova, V. L., Kulasekara, H. D., Larson, L., Bowers, V., Rechkina, E., Kisiela, D., Sledneva, Y., Choudhury, D., Maslova, I., Deng, K., et al. (2021) · Journal of Clinical Microbiology · doi:10.1128/jcm.00921-21 · Cited by 210 · see citing works
Tracking cryptic SARS-CoV-2 lineages detected in NYC wastewater
Smyth, D. S., Trujillo, M., Gregory, D. A., Cheung, K., Gao, A., Graham, M., Guan, Y., Guldenpfennig, C., Hoxie, I., Kannoly, S., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28246-3 · Cited by 211 · 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
Increased immune escape of the new SARS-CoV-2 variant of concern Omicron
Hu, J., Peng, P., Cao, X., Wu, K., Chen, J., Wang, K., Tang, N., & Huang, A.-L. (2022) · Cellular & Molecular Immunology · doi:10.1038/s41423-021-00836-z · Cited by 204 · see citing works
The SARS-CoV-2 mutations versus vaccine effectiveness: New opportunities to new challenges
Malik, J. A., Ahmed, S., Aroosa, M., Shinde, M., Bender, O., Alshammari, F., Ansari, M., & Anwar, S. (2022) · Journal of Infection and Public Health · doi:10.1016/j.jiph.2021.12.014 · Cited by 201 · see citing works
Experimental Evidence for Enhanced Receptor Binding by Rapidly Spreading SARS-CoV-2 Variants
Laffeber, C., de Koning, K., Kanaar, R., & Lebbink, J. H. G. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167058 · Cited by 190 · see citing works
“Mutation of glutamate to lysine at this position abrogates binding to certain antibodies and results in immune evasion, reinfection and reduced efficacy of vaccines [11, 18-22].”
SARS-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
“This mutation weakened antibody neutralization and increased the virus’s ability to infect [75].”
The Global Epidemic of the SARS-CoV-2 Delta Variant, Key Spike Mutations and Immune Escape
Tian, D., Sun, Y., Zhou, J., & Ye, Q. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.751778 · Cited by 192 · see citing works
Immune Evasion of SARS-CoV-2 Emerging Variants: What Have We Learnt So Far?
Lazarević, I., Pravica, V., Miljanovic, D., & Cupic, M. D. (2021) · Viruses · doi:10.3390/v13071192 · Cited by 188 · see citing works
SARS‐CoV‐2 Alpha, Beta, and Delta variants display enhanced Spike‐mediated syncytia formation
Rajah, M. M., Hubert, M., Bishop, E., Saunders, N., Robinot, R., Grzelak, L., Planas, D., Dufloo, J., Gellenoncourt, S., Bongers, A., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2021108944 · Cited by 179 · see citing works
Reduced neutralisation of the Delta (B.1.617.2) SARS-CoV-2 variant of concern following vaccination
Davis, C., Logan, N. A., Tyson, G. B., Orton, R. J., Harvey, W. T., Perkins, J. S., Mollett, G., Blacow, R., Peacock, T. P., Barclay, W., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1010022 · Cited by 188 · see citing works
Walls, A. C., Miranda, M. C., Schäfer, A., Pham, M. N., Greaney, A., Arunachalam, P. S., Navarro, M.-J., Tortorici, M. A., Rogers, K., O’Connor, M. A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.09.015 · Cited by 185 · see citing works
“These findings show that, as is the case for many convalescent individuals (Greaney et al., 2021b; Liu et al., 2021; Piccoli et al., 2020), an important fraction of vaccine-elicited neutralizing Abs in NHPs and humans is focused on the RBM (specifically around position 484), independently of the immunogen (RBD-NP, Hex…”
Truong, T., Ryutov, A., Pandey, U., Yee, R., Goldberg, L., Bhojwani, D., Aguayo-Hiraldo, P. I., Pinsky, B. A., Pekosz, A. S., Shen, L., et al. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103355 · Cited by 183 · see citing works
Kuzmina, A., Khalaila, Y., Voloshin, O., Keren‐Naus, A., Cohen, L. B., Raviv, Y., Shemer‐Avni, Y., Rosenberg, E., & Taube, R. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.03.008 · Cited by 172 · see citing works
Nasal delivery of an IgM offers broad protection from SARS-CoV-2 variants
Ku, Z., Xie, X., Hinton, P. R., Liu, X., Ye, X., Muruato, A. E., Ng, D., Biswas, S., Zou, J., Liu, Y., et al. (2021) · Nature · doi:10.1038/s41586-021-03673-2 · Cited by 170 · see citing works
In vitro selection of Remdesivir resistance suggests evolutionary predictability of SARS-CoV-2
Szemiel, A. M., Merits, A., Orton, R. J., MacLean, O. A., Pinto, R. M., Wickenhagen, A., Lieber, G., Turnbull, M. L., Wang, S., Furnon, W., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009929 · Cited by 175 · see citing works
Zuo, F., Abolhassani, H., Du, L., Piralla, A., Bertoglio, F., de Campos‐Mata, L., Wan, H., Schubert, M., Cassaniti, I., Wang, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30340-5 · Cited by 172 · see citing works
SARS-CoV-2 Omicron boosting induces de novo B cell response in humans
Alsoussi, W. B., Malladi, S. K., Zhou, J. Q., Liu, Z., Ying, B., Kim, W., Schmitz, A. J., Lei, T., Horvath, S. C., Sturtz, A. J., et al. (2023) · Nature · doi:10.1038/s41586-023-06025-4 · Cited by 167 · see citing works
Self-citationNeutralization of BA.4–BA.5, BA.4.6, BA.2.75.2, BQ.1.1, and XBB.1 with Bivalent Vaccine
Zou, J., Kurhade, C., Patel, S., Kitchin, N. R. E., Tompkins, K. R., Cutler, M. W., Cooper, D., Yang, Q., Cai, H., Muik, A., et al. (2023) · New England Journal of Medicine · doi:10.1056/nejmc2214916 · Cited by 166 · see citing works
“Cell Host Microbe 2021; 29(3): 477-488.”
SARS-CoV-2 evolution and vaccines: cause for concern?
Williams, T., & Burgers, W. A. (2021) · The Lancet Respiratory Medicine · doi:10.1016/s2213-2600(21)00075-8 · Cited by 163 · see citing works
Huang, X., Tang, T., Zhang, G., & Liang, T. (2021) · Molecular Cancer · doi:10.1186/s12943-021-01342-6 · 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
Tada, T., Dcosta, B. M., Samanovic, M. I., Herati, R. S., Cornelius, A. R., Zhou, H., Vaill, A., Kazmierski, W., Mulligan, M. J., & Landau, N. R. (2021) · mBio · doi:10.1128/mbio.00696-21 · Cited by 152 · see citing works
Focosi, D., & Maggi, F. (2021) · Reviews in Medical Virology · doi:10.1002/rmv.2231 · Cited by 148 · see citing works
Chakraborty, C., Sharma, A. R., Bhattacharya, M., & Lee, S. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.801522 · Cited by 150 · see citing works
Case, J. B., Mackin, S., Errico, J. M., Chong, Z., Madden, E. A., Whitener, B. M., Guarino, B., Schmid, M., Rosenthal, K., Ren, K., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31615-7 · Cited by 144 · see citing works
Self-citationAntibody-mediated neutralization of SARS-CoV-2
Gruell, H., Vanshylla, K., Weber, T., Barnes, C. O., Kreer, C., & Klein, F. (2022) · Immunity · doi:10.1016/j.immuni.2022.05.005 · Cited by 145 · see citing works
Review of Current COVID-19 Diagnostics and Opportunities for Further Development
Mardian, Y., Kosasih, H., Karyana, M., Neal, A., & Lau, C. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.615099 · Cited by 147 · see citing works
“, Spike-E484K and SpikeS477N) have demonstrated ability to escape neutralization by convalescent sera and monoclonal antibodies (258).”
BackgroundFrom delta to Omicron: S1-RBD/S2 mutation/deletion equilibrium in SARS-CoV-2 defined variants
PAPANIKOLAOU, V. S., Chrysovergis, A., Ragos, V., Tsiambas, E., Katsinis, S., Manoli, A., Papouliakos, S. M., Roukas, D., Mastronikolis, S. N., Peschos, D., et al. (2022) · Gene · doi:10.1016/j.gene.2021.146134 · Cited by 142 · see citing works
Systematic analysis of SARS-CoV-2 infection of an ACE2-negative human airway cell
Puray‐Chavez, M., LaPak, K. M., Schrank, T. P., Elliott, J. L., Bhatt, D. P., Agajanian, M. J., Jasuja, R., Lawson, D. Q., Davis, K., Rothlauf, P. W., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109364 · Cited by 131 · see citing works
“Monoclonal antibody SARS2-55 was generated and as previously described (Liu et al., 2021).”
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: Longevity, breadth, and evasion by emerging viral variants
Tea, F., Stella, A. O., Aggarwal, A., Darley, D. R., Pilli, D., Vitale, D., Merheb, V., Lee, F. X. Z., Cunningham, P., Walker, G. J., et al. (2021) · PLoS Medicine · doi:10.1371/journal.pmed.1003656 · Cited by 134 · 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
Molecular characteristics, immune evasion, and impact of SARS-CoV-2 variants
Sun, C., Xie, C., Bu, G., Zhong, L., & Zeng, M. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01039-2 · Cited by 139 · see citing works
“With multiple critical mutations destabilizing the antibody interaction with spike or RBD, in vitro experiments also revealed the worrying performance of current antibodies against the SARS-CoV-2 variants.(201,202) Considering that in vitro neutralization for the same therapeutic agent might differ under different cir…”
MethodHeilmann, E., Costacurta, F., Moghadasi, S. A., Ye, C., Pavan, M., Bassani, D., Volland, A., Ascher, C., Weiss, A. K. H., Bante, D., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abq7360 · Cited by 144 · see citing works
Fast-spreading SARS-CoV-2 variants: challenges to and new design strategies of COVID-19 vaccines
Zhou, W., & Wang, W. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00644-x · Cited by 132 · see citing works
“All four mutants undergoing substitution at E484 are resistant to neutralization of human immune serum.(25) Bloom et al.”
BackgroundLi, W., Chen, Y., Prévost, J., Ullah, I., Lu, M., Gong, S. Y., Tauzin, A., Gasser, R., Vézina, D., Anand, S. P., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110210 · Cited by 125 · see citing works
“These data demonstrate that in contrast to other antibodies that are attenuated against emerging variants (Greaney et al., 2021a; Liu et al., 2021; Starr et al., 2021; Weisblum et al., 2020), CV3-1 and CV3-25 remain potent against these variants and are therefore prime candidates to elucidate the…”
Characterization of the emerging B.1.621 variant of interest of SARS-CoV-2
Laiton‐Donato, K., Franco-Muñoz, C., Álvarez-Díaz, D. A., Ruiz-Moreno, H. A., Usme-Ciro, J. A., Prada-Cardozo, D., Reales-González, J., Corchuelo, S., Herrera-Sepúlveda, M. T., Naizaque, J., et al. (2021) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2021.105038 · Cited by 123 · see citing works
SARS-CoV-2 immune evasion by variant B.1.427/B.1.429Preprint
McCallum, M., Bassi, J., Marco, A. D., Chen, A., Walls, A. C., di Iulio, J., Tortorici, M. A., Navarro, M.-J., Silacci-Fregni, C., Saliba, C., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.31.437925 · Cited by 128 · see citing works
An intranasal vaccine durably protects against SARS-CoV-2 variants in mice
Hassan, A. O., Shrihari, S., Gorman, M. J., Ying, B., Yuan, D., Raju, S., Chen, R. E., Dmitriev, I. P., Kashentseva, E. A., Adams, L. J., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109452 · Cited by 129 · see citing works
Self-citationSpike and nsp6 are key determinants of SARS-CoV-2 Omicron BA.1 attenuation
Chen, D. W., Chin, C. V., Kenney, D., Tavares, A. H., Khan, N., Conway, H. L., Liu, G., Choudhary, M. C., Gertje, H. P., O’Connell, A. K., et al. (2023) · Nature · doi:10.1038/s41586-023-05697-2 · Cited by 144 · see citing works
Hunt, A. C., Case, J. B., Park, Y., Cao, L., Wu, K., Walls, A. C., Liu, Z., Bowen, J. E., Yeh, A. H.-W., Saini, S., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abn1252 · Cited by 116 · see citing works
Self-citationAggarwal, A., Stella, A. O., Walker, G. J., Akerman, A., Esneau, C., Milogiannakis, V., Burnett, D. L., McAllery, S., Silva, M. R., Lu, Y., et al. (2022) · Nature Microbiology · doi:10.1038/s41564-022-01135-7 · Cited by 121 · see citing works
Emerging 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
“617, L452R, appears to reduce the sensitivity to certain antibodies and human convalescent sera [139,158].”
BackgroundLu, L., Sikkema, R. S., Velkers, F. C., Nieuwenhuijse, D. F., Fischer, E. A. J., Meijer, P. A., Bouwmeester-Vincken, N., Rietveld, A., Wegdam-Blans, M. C. A., Tolsma, P., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27096-9 · Cited by 120 · see citing works
SARS‐CoV‐2 Omicron variant: Immune escape and vaccine development
Ao, D., Lan, T., He, X., Liu, J., Chen, L., Baptista‐Hon, D. T., Zhang, K., & Wei, X. (2022) · MedComm · doi:10.1002/mco2.126 · Cited by 117 · see citing works
Concerns about SARS-CoV-2 evolution should not hold back efforts to expand vaccination
Cobey, S. E., Larremore, D. B., Grad, Y. H., & Lipsitch, M. (2021) · Nature reviews. Immunology · doi:10.1038/s41577-021-00544-9 · Cited by 118 · see citing works
LY-CoV1404 (bebtelovimab) potently neutralizes SARS-CoV-2 variantsPreprint
Westendorf, K., Žentelis, S., Wang, L., Foster, D., Vaillancourt, P., Wiggin, M., Lovett, E., van der Lee, R., Hendle, J., Pustilnik, A., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.30.442182 · Cited by 117 · see citing works
Mutations of SARS-CoV-2 spike protein: Implications on immune evasion and vaccine-induced immunity
Mengist, H. M., Kombe, A. J. K., Mekonnen, D. S., Abebaw, A., Getachew, M., & Jin, T. (2021) · Seminars in Immunology · doi:10.1016/j.smim.2021.101533 · Cited by 112 · see citing works
Chen, X., Chen, Z., Azman, A. S., Sun, R., Lu, W., Zheng, N., Zhou, J., Wu, Q., Deng, X., Zhao, Z., et al. (2022) · Clinical Infectious Diseases · doi:10.1093/cid/ciab646 · Cited by 113 · see citing works
Hodcroft, E. B., Domman, D., Snyder, D. J., Oguntuyo, K. Y., Diest, M. V., Densmore, K. H., Schwalm, K. C., Femling, J., Carroll, J. L., Scott, R. S., et al. (2021) · medRxiv · doi:10.1101/2021.02.12.21251658 · Cited by 109 · see citing works
- Authors
- Liu, Z., VanBlargan, L. A., Bloyet, L.-M., Rothlauf, P. W., Chen, R. E., Stumpf, S., Zhao, H., Errico, J. M., Theel, E. S., Liebeskind, M. J., Alford, B., Buchser, W. J., Ellebedy, A. H., Fremont, D. H., Diamond, M. S., & Whelan, S. P. J.
- Affiliations
- Washington University in St. Louis (US)
- Harvard University (US)
- Mayo Clinic (US)
- Corresponding author
- Diamond, Michael S.
- Whelan, Sean P.J.
- ORCID
- Venue
- Cell Host & Microbe
- Publisher
- Elsevier BV
- Published
- 2021-03
- Volume
- 29
- Issue
- 3
- Pages
- 477-488.e4
- ISSN
- 1931-3128 (ISSN-L)
- PMC
- PMC7839837
- OpenAlex
- W3121995178
- Cited by
- 725
- References
- 38
- Citations by year
- 2026: 11 · 2025: 22 · 2024: 57 · 2023: 77 · 2022: 255 · 2021: 302
- FWCI
- 55.27
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 374 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell Host & Microbe (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Washington University in St. Louis
- University of Washington
- Saint Louis University
- National Institutes of Health (75N93019C00062, R01 AI127828, R01 AI157155, R37 AI059371)
- AbbVie
- Defense Advanced Research Projects Agency (HR001117S0019)
- 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, antibody escape mutants, neutralizing monoclonal antibodies, receptor binding domain, E484K mutation
- MeSH terms
- Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, COVID-19 Vaccines, Animals, Antibodies, Monoclonal, Antibodies, Viral, Chlorocebus aethiops, Female, Humans, Mice, Inbred BALB C, Models, Molecular, Mutation, Neutralization Tests, Protein Binding, Receptors, Virus, Vero Cells, Amino Acid Substitution, Mice, Antibodies, Neutralizing, Spike Glycoprotein, Coronavirus
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
