Impact of the B.1.1.7 variant on neutralizing monoclonal antibodies recognizing diverse epitopes on SARS-CoV-2 Spike
Open accessAbstract
The interaction of the SARS-CoV-2 Spike receptor binding domain (RBD) with the ACE2 receptor on host cells is essential for viral entry. RBD is the dominant target for neutralizing antibodies and several neutralizing epitopes on RBD have been molecularly characterized. Analysis of circulating SARS-CoV-2 variants has revealed mutations arising in the RBD, the N-terminal domain (NTD) and S2 subunits of Spike. To fully understand how these mutations affect the antigenicity of Spike, we have isolated and characterized neutralizing antibodies targeting epitopes beyond the already identified RBD epitopes. Using recombinant Spike as a sorting bait, we isolated >100 Spike-reactive monoclonal antibodies from SARS-CoV-2 infected individuals. ~45% showed neutralizing activity of which ~20% were NTD-specific. None of the S2-specific antibodies showed neutralizing activity. Competition ELISA revealed that NTD-specific mAbs formed two distinct groups: the first group was highly potent against infectious virus, whereas the second was less potent and displayed glycan-dependant neutralization activity. Importantly, mutations present in B.1.1.7 Spike frequently conferred resistance to neutralization by the NTD-specific neutralizing antibodies. This work demonstrates that neutralizing antibodies targeting subdominant epitopes need to be considered when investigating antigenic drift in emerging variants.
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?
Mutations found in emergent S variants decrease sensitivity to neutralization by mAbs, convalescent plasma, and sera from vaccinated individuals.
“Mutations found in emergent S variants decrease sensitivity to neutralization by mAbs, convalescent plasma, and sera from vaccinated individuals (27, 37, 58, 61–70).”
From mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection (2021) · cites this paper as [67]
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
Lu, R., Zhao, X., Li, J., Niu, P., Yang, B., Wu, H., Wang, W., Song, H., Huang, B., Zhu, N., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30251-8 · Cited by 11,907 · see citing works
Complex heatmaps reveal patterns and correlations in multidimensional genomic data
Gu, Z., Eils, R., & Schlesner, M. (2016) · Bioinformatics · doi:10.1093/bioinformatics/btw313 · Cited by 10,122 · 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
Immunological memory to SARS-CoV-2 assessed for up to 8 months after infection.
Dan, J. M., Mateus, J., Kato, Y., Hastie, K. M., Yu, E. D., Faliti, C. E., Grifoni, A., Ramirez, S. I., Haupt, S., Frazier, A., et al. (2021) · Science · doi:10.1126/science.abf4063 · Cited by 2,656 · see citing works
Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7
Wang, P., Nair, M. S., Liu, L., Iketani, S., Luo, Y., Guo, Y., Wang, M., Yu, J., Zhang, B., Kwong, P. D., et al. (2021) · Nature · doi:10.1038/s41586-021-03398-2 · Cited by 2,312 · see citing works
Cross-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
Convergent Antibody Responses to SARS-CoV-2 in Convalescent Individuals
Robbiani, D. F., Gaebler, C., Muecksch, F., Lorenzi, J. C. C., Wang, Z., Cho, A., Agudelo, M., Barnes, C. O., Gazumyan, A., Finkin, S., et al. (2020) · Nature · doi:10.1038/s41586-020-2456-9 · Cited by 1,853 · see citing works
Okba, N. M. A., Müller, M. A., Li, W., Wang, C., GeurtsvanKessel, C. H., Corman, V. M., Lamers, M. M., Sikkema, R. S., de Bruin, E., Chandler, F. D., et al. (2020) · Emerging Infectious Diseases · doi:10.3201/eid2607.200841 · Cited by 1,614 · see citing works
A minimal common outcome measure set for COVID-19 clinical research
Marshall, J. C., Murthy, S., Diaz, J. V., Adhikari, N. K., Angus, D., Arabi, Y. M., Baillie, J. K., Bauer, M. W., Berry, S., Blackwood, B., et al. (2020) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(20)30483-7 · Cited by 1,605 · see citing works
SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies
Barnes, C. O., Jette, C. A., Abernathy, M. E., Dam, K.-M. A., Esswein, S. R., Gristick, H. B., Malyutin, A. G., Sharaf, N. G., Huey-Tubman, K. E., Lee, Y. E., et al. (2020) · Nature · doi:10.1038/s41586-020-2852-1 · Cited by 1,599 · see citing works
Site-specific glycan analysis of the SARS-CoV-2 spike
Watanabe, Y., Allen, J. D., Wrapp, D., McLellan, J. S., & Crispin, M. (2020) · Science · doi:10.1126/science.abb9983 · Cited by 1,507 · 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 · see citing works
Seow, J., Graham, C., Merrick, B., Acors, S., Pickering, S., Steel, K. J. A., Hemmings, O., O’Byrne, A., Kouphou, N., Galao, R. P., et al. (2020) · Nature Microbiology · doi:10.1038/s41564-020-00813-8 · Cited by 1,419 · see citing works
Self-citationA 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
Piccoli, L., Park, Y.-J., Tortorici, M. A., Czudnochowski, N., Walls, A. C., Beltramello, M., Silacci-Fregni, C., Pinto, D., Rosen, L. E., Bowen, J. E., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.037 · Cited by 1,395 · see citing works
A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2
Chi, X., Yan, R., Zhang, J., Zhang, G., Zhang, Y., Hao, M., Zhang, Z., Fan, P., Dong, Y., Yang, Y., et al. (2020) · Science · doi:10.1126/science.abc6952 · Cited by 1,385 · 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
Escape 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
Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein
Walls, A. C., Park, Y., Tortorici, M. A., Wall, A., McGuire, A. T., & Veesler, D. (2020) · Cell · doi:10.1016/j.cell.2020.11.032 · Cited by 1,283 · see citing works
Persistence and Evolution of SARS-CoV-2 in an Immunocompromised Host
Choi, B., Choudhary, M. C., Regan, J., Sparks, J. A., Padera, R. F., Qiu, X., Solomon, I. H., Kuo, H.-H., Boucau, J., Bowman, K., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmc2031364 · Cited by 1,246 · see citing works
Rogers, 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
Brochet, X., Lefranc, M., & Giudicelli, V. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn316 · Cited by 1,220 · 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) · doi:10.1101/2020.12.31.425021 · Cited by 1,178 · 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
SARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma
Wibmer, C. K., Ayres, F., Hermanus, T., Madzivhandila, M., Kgagudi, P., Oosthuysen, B., Lambson, B. E., de Oliveira, T., Vermeulen, M., van der Berg, K., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01285-x · Cited by 1,147 · 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
A human monoclonal antibody blocking SARS-CoV-2 infection
Wang, C., Li, W., Drabek, D., Okba, N. M. A., van Haperen, R., Osterhaus, A. D. M. E., van Kuppeveld, F. J. M., Haagmans, B. L., Grosveld, F. G., & Bosch, B. (2020) · Nature Communications · doi:10.1038/s41467-020-16256-y · Cited by 1,115 · see citing works
SARS-CoV-2 evolution during treatment of chronic infection
Kemp, S. A., Collier, D. A., Datir, R. P., Ferreira, I. A. T. M., Gayed, S., Jahun, A., Hosmillo, M., Rees-Spear, C., Mlcochova, P., Lumb, I. U., et al. (2021) · Nature · doi:10.1038/s41586-021-03291-y · Cited by 1,097 · see citing works
Tiller, T., Meffre, E., Yurasov, S., Tsuiji, M., Nussenzweig, M. C., & Wardemann, H. (2007) · Journal of Immunological Methods · doi:10.1016/j.jim.2007.09.017 · Cited by 1,078 · see citing works
Molecular Architecture of the SARS-CoV-2 Virus
Yao, H., Song, Y., Chen, Y., Wu, N., Xu, J., Sun, C., Zhang, J., Weng, T., Zhang, Z., Wu, Z., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.018 · Cited by 1,060 · cited 2× · see citing works
“The S2 subunit, containing the fusion peptide, two heptad repeats (HR1 and HR2), the cytoplasmic tail and the transmembrane domain, is crucial for viral membrane fusion (Yao et al., 2020).”
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
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
Wu, 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
Self-citationA dynamic COVID-19 immune signature includes associations with poor prognosis
Laing, A. G., Lorenc, A., del Molino del Barrio, I., Das, A., Fish, M., Monin, L., Muñoz-Ruiz, M., McKenzie, D. R., Hayday, T. S., Francos-Quijorna, I., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-1038-6 · Cited by 946 · see citing works
Self-citationN-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2
McCallum, M., Marco, A. D., Lempp, F., Tortorici, M. A., Pinto, D., Walls, A. C., Beltramello, M., Chen, A., Liu, Z., Zatta, F., et al. (2021) · doi:10.1101/2021.01.14.426475 · Cited by 901 · cited 3× · see citing works
“Overall, these results suggest that some antibodies described here neutralize SARS-CoV-2 through mechanisms beyond direct receptor binding inhibition, such as inhibiting membrane fusion (McCallum et al., 2021) or S1 shedding (Piccoli et al., 2020), which need be investigated further.”
InfluentialN-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
Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals
Scheid, J. F., Mouquet, H., Feldhahn, N., Seaman, M. S., Velinzon, K., Pietzsch, J., Ott, R. G., Anthony, R. M., Zebroski, H. A., Hurley, A., et al. (2009) · Nature · doi:10.1038/nature07930 · Cited by 855 · see citing works
Neutralizing Antibodies against SARS-CoV-2 and Other Human Coronaviruses
Jiang, S., Hillyer, C., & Du, L. (2020) · Trends in Immunology · doi:10.1016/j.it.2020.03.007 · Cited by 847 · 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 time- and cost-efficient system for high-level protein production in mammalian cells
Aricescu, A. R., Lu, W., & Jones, E. Y. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906029799 · Cited by 746 · see citing works
Prospective mapping of viral mutations that escape antibodies used to treat COVID-19
Starr, T. N., Greaney, A. J., Addetia, A., Hannon, W. W., Choudhary, M. C., Dingens, A. S., Li, J. Z., & Bloom, J. D. (2021) · Science · doi:10.1126/science.abf9302 · Cited by 743 · see citing works
Avanzato, V. A., Matson, M. J., Seifert, S. N., Pryce, R., Williamson, B. N., Anzick, S. L., Barbian, K., Judson, S. D., Fischer, E. R., Martens, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.049 · Cited by 703 · see citing works
Self-citationProspective mapping of viral mutations that escape antibodies used to treat COVID-19Preprint
Starr, T. N., Greaney, A. J., Addetia, A., Hannon, W. W., Choudhary, M., Dingens, A. S., Li, J. Z., & Bloom, J. (2020) · bioRxiv · doi:10.1101/2020.11.30.405472 · Cited by 633 · see citing works
Structural basis of a shared antibody response to SARS-CoV-2
Yuan, M., Liu, H., Wu, N. C., Lee, C.-C. D., Zhu, X., Zhao, F., Huang, D., Yu, W., Hua, Y., Tien, H., et al. (2020) · Science · doi:10.1126/science.abd2321 · Cited by 589 · see citing works
Commonality despite exceptional diversity in the baseline human antibody repertoire
Briney, B., Inderbitzin, A., Joyce, C., & Burton, D. R. (2019) · Nature · doi:10.1038/s41586-019-0879-y · Cited by 544 · see citing works
Recurrent deletions in the SARS-CoV-2 spike glycoprotein drive antibody escape
McCarthy, K. R., Rennick, L. J., Nambulli, S., Robinson-McCarthy, L. R., Bain, W. G., Haidar, G., & Duprex, W. P. (2021) · Science · doi:10.1126/science.abf6950 · Cited by 535 · see citing works
Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms
Tortorici, M. A., Beltramello, M., Lempp, F. A., Pinto, D., Dang, H. V., Rosen, L. E., McCallum, M., Bowen, J., Minola, A., Jaconi, S., et al. (2020) · Science · doi:10.1126/science.abe3354 · Cited by 510 · see citing works
SARS-CoV-2 escape from a highly neutralizing COVID-19 convalescent plasma
Andreano, E., Piccini, G., Licastro, D., Casalino, L., Johnson, N. V., Paciello, I., Monego, S. D., Pantano, E., Manganaro, N., Manenti, A., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2103154118 · Cited by 421 · see citing works
Carter, M. J., Fish, M., Jennings, A., Doores, K. J., Wellman, P., Seow, J., Acors, S., Graham, C., Timms, E., Kenny, J., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-1054-6 · Cited by 419 · see citing works
Self-citationSeydoux, E., Homad, L. J., MacCamy, A. J., Parks, K. R., Hurlburt, N. K., Jennewein, M. F., Akins, N. R., Stuart, A. B., Wan, Y.-H., Feng, J., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.06.001 · Cited by 364 · see citing works
D614G Spike Mutation Increases SARS CoV-2 Susceptibility to Neutralization
Weissman, D., Alameh, M.-G., de Silva, T., Collini, P., Hornsby, H., Brown, R., LaBranche, C. C., Edwards, R. J., Sutherland, L., Santra, S., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2020.11.012 · Cited by 324 · see citing works
Muecksch, F., Wise, H., Batchelor, B., Squires, M., Semple, E., Richardson, C., McGuire, J., Clearly, S., Furrie, E., Greig, N., et al. (2021) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiaa659 · Cited by 308 · see citing works
Legros, V., Denolly, S., Vogrig, M., Boson, B., Siret, E., Rigaill, J., Pillet, S., Grattard, F., Gonzalo, S., Verhoeven, P. O., et al. (2021) · Cellular and Molecular Immunology · doi:10.1038/s41423-020-00588-2 · Cited by 297 · see citing works
Compromised Humoral Functional Evolution Tracks with SARS-CoV-2 Mortality
Zohar, T., Loos, C., Fischinger, S., Atyeo, C., Wang, C., Slein, M. D., Burke, J., Yu, J., Feldman, J., Hauser, B. M., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.052 · Cited by 297 · see citing works
Crawford, K. H. D., Dingens, A. S., Eguia, R., Wolf, C. R., Wilcox, N., Logue, J. K., Shuey, K., Casto, A. M., Fiala, B., Wrenn, S., et al. (2021) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiaa618 · Cited by 265 · see citing works
Variable Loop Glycan Dependency of the Broad and Potent HIV-1-Neutralizing Antibodies PG9 and PG16
Doores, K. J., & Burton, D. R. (2010) · Journal of Virology · doi:10.1128/jvi.00552-10 · Cited by 235 · see citing works
Self-citationDynamics of neutralizing antibody titers in the months after SARS-CoV-2 infectionPreprint
Crawford, K. H., Dingens, A., Eguia, R. T., et al. (2020) · medRxiv · doi:10.1101/2020.08.06.20169367 · Cited by 229 · see citing works
The effect of spike mutations on SARS-CoV-2 neutralization
Rees-Spear, C., Muir, L., Griffith, S. A., Heaney, J., Aldon, Y., Snitselaar, J. L., Thomas, P., Graham, C., Seow, J., Lee, N., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108890 · Cited by 215 · see citing works
Self-citationSequencing and cloning of antigen-specific antibodies from mouse memory B cells
von Boehmer, L., Liu, C., Ackerman, S. E., Gitlin, A. D., Wang, Q., Gazumyan, A., & Nussenzweig, M. C. (2016) · Nature Protocols · doi:10.1038/nprot.2016.102 · Cited by 203 · see citing works
Neutralizing Antibodies against SARS-CoV-2 and Other Human Coronaviruses
Jiang, S., Hillyer, C. D., & Du, L. (2020) · Trends in Immunology · doi:10.1016/j.it.2020.04.008 · Cited by 199 · see citing works
Extremely potent human monoclonal antibodies from COVID-19 convalescent patients
Andreano, E., Nicastri, E., Paciello, I., Pileri, P., Manganaro, N., Piccini, G., Manenti, A., Pantano, E., Kabanova, A., Troisi, M., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.035 · Cited by 198 · see citing works
Cross-Sectional Evaluation of Humoral Responses against SARS-CoV-2 Spike
Prévost, J., Gasser, R., Beaudoin-Bussières, G., Richard, J., Duerr, R., Laumaea, A., Anand, S. P., Goyette, G., Benlarbi, M., Ding, S., et al. (2020) · Cell Reports Medicine · doi:10.1016/j.xcrm.2020.100126 · Cited by 197 · see citing works
Inhibition of SARS-CoV-2 viral entry upon blocking N- and O-glycan elaboration
Yang, Q., Hughes, T. A., Kelkar, A., Yu, X., Cheng, K., Park, S., Huang, W., Lovell, J. F., & Neelamegham, S. (2020) · eLife · doi:10.7554/elife.61552 · Cited by 195 · see citing works
Decline of Humoral Responses against SARS-CoV-2 Spike in Convalescent Individuals
Beaudoin-Bussières, G., Laumaea, A., Anand, S. P., Prévost, J., Gasser, R., Goyette, G., Medjahed, H., Perreault, J., Tremblay, T., Lewin, A., et al. (2020) · mBio · doi:10.1128/mbio.02590-20 · Cited by 189 · see citing works
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
Neutralising antibodies in Spike mediated SARS-CoV-2 adaptationPreprint
Kemp, S. A., Collier, D. A., Datir, R. P., et al. (2020) · medRxiv · doi:10.1101/2020.12.05.20241927 · Cited by 180 · see citing works
Fc-optimized antibodies elicit CD8 immunity to viral respiratory infection
Bournazos, S., Corti, D., Virgin, H. W., & Ravetch, J. V. (2020) · Nature · doi:10.1038/s41586-020-2838-z · Cited by 139 · see citing works
SARS-CoV-2 can recruit a heme metabolite to evade antibody immunity
Rosa, A., Pye, V. E., Graham, C., Muir, L., Seow, J., Ng, K., Cook, N., Rees-Spear, C., Parker, E., dos Santos, M. S., et al. (2021) · SciAdv · doi:10.1126/sciadv.abg7607 · Cited by 120 · see citing works
Self-citationNatural deletions in the SARS-CoV-2 spike glycoprotein drive antibody escapePreprint
McCarthy, K. R., Rennick, L., Nambulli, S., et al. (2020) · bioRxiv · doi:10.1101/2020.11.19.389916 · Cited by 117 · see citing works
SARS-CoV-2 Infection Severity Is Linked to Superior Humoral Immunity against the Spike
Guthmiller, J. J., Stovicek, O., Wang, J., Changrob, S., Li, L., Halfmann, P., Zheng, N., Utset, H. A., Stamper, C. T., Dugan, H. L., et al. (2021) · mBio · doi:10.1128/mbio.02940-20 · Cited by 113 · see citing works
Pickering, S., Betancor, G., Galão, R. P., Merrick, B., Signell, A. W., Wilson, H., Ik, M. T. K., Seow, J., Graham, C., Acors, S., et al. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008817 · Cited by 107 · see citing works
Self-citationDoores, K. J., Kong, L., Krumm, S. A., Le, K. M., Sok, D., Laserson, U., Garcés, F., Poignard, P., Wilson, I. A., & Burton, D. R. (2014) · Journal of Virology · doi:10.1128/jvi.02905-14 · Cited by 88 · see citing works
Self-citationLi, W., Chen, C., Drelich, A. K., Martinez, D. R., Gralinski, L. E., Sun, Z., Schäfer, A., Kulkarni, S. S., Liu, X., Leist, S. R., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2010197117 · Cited by 81 · see citing works
Muecksch, F., Wise, H. M., Batchelor, B., et al. (2020) · medRxiv · doi:10.1101/2020.08.05.20169128 · Cited by 77 · see citing works
Kim, S. I., Noh, J., Kim, S., Choi, Y., Yoo, D. K., Lee, Y., Lee, H., Jung, J., Kang, C. K., Song, K., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abd6990 · Cited by 74 · see citing works
D614G Spike Mutation Increases SARS CoV-2 Susceptibility to NeutralizationPreprint
Weissman, D., Alameh, M., de Silva, T. I., Collini, P., Hornsby, H. R., Brown, R. L., LaBranche, C. C., Edwards, R. J., Sutherland, L. L., Santra, S., et al. (2020) · medRxiv · doi:10.1101/2020.07.22.20159905 · Cited by 72 · see citing works
An optimised method for the production of MERS-CoV spike expressing viral pseudotypes
Grehan, K., Ferrara, F., & Temperton, N. J. (2015) · MethodsX · doi:10.1016/j.mex.2015.09.003 · Cited by 70 · 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
Self-citationStructural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein VariantPreprint
Yurkovetskiy, L., Wang, X., Pascal, K. E., et al. (2020) · SSRN Electronic Journal · doi:10.2139/ssrn.3657338 · Cited by 31 · see citing works
Extremely potent human monoclonal antibodies from convalescent Covid-19 patientsPreprint
Andreano, E., Nicastri, E., Paciello, I., et al. (2020) · bioRxiv · doi:10.1101/2020.10.07.328302 · Cited by 12 · see citing works
Park, Y., Tortorici, M. A., Walls, A. C., Czudnochowski, N., Snell, G., & Veesler, D. (2020) · Worldwide Protein Data Bank · doi:10.2210/pdb7jxd/pdb · Cited by 6 · see citing works
Schäfer, A., Gralinski, L. E., Conard, A., et al. (2020) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/2e2k-mw25 · Cited by 2 · see citing works
SARS-CoV-2 escape <i>in vitro</i> from a highly neutralizing COVID-19 convalescent plasma
Andreano, E., Piccini, G., Licastro, D., Casalino, L., Johnson, N. V., Paciello, I., Monego, S. D., Pantano, E., Manganaro, N., Manenti, A., et al. (2020) · doi:10.1101/2020.12.28.424451
SARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma
Wibmer, C. K., Ayres, F., Hermanus, T., Madzivhandila, M., Kgagudi, P., Oosthuysen, B., Lambson, B. E., de Oliveira, T., Vermeulen, M., van der Berg, K., et al. (2021) · doi:10.1101/2021.01.18.427166
Flagged first, then by citations
Research works printed but not linked: 4
- Laing A.G., Lorenc A., Del Molino Del Barrio I., Das A., Fish M., Monin L., Munoz-Ruiz M., McKenzie D.R., Hayday T.S., Francos-Quijorna I., (2020b). A dynamic COVID-19 immune signature includes associations with poor prognosis. Nat Med 26, 1623– 1635. 32807934
- Muecksch F., Wise H., Batchelor B., Squires M., Semple E., Richardson C., McGuire J., Clearly S., Furrie E., Greig N., (2020). Longitudinal analysis of serology and neutralizing antibody levels in COVID19 convalescents. J Infect Dis. PMC7665595 33140086
- Rosa A., Pye V.E., Graham C., Muir L., Seow J., Ng K.W., Cook N.J., Rees-Spear C., Parker E., Kassiotis G., (2021). SARS-CoV-2 recruits a haem metabolite to evade antibody immunity. medRxiv. PMC8163077 33888467
- Thompson C.N.G., Paton Robert, Lourenço José, View ORCID Profile Penman Bridget, View ORCID Profile Lee Lian Ni, View ORCID Profile Odon Valerie, View ORCID Profile Mongkolsapaya Juthathip, View ORCID Profile Chinnakannan Senthil, Dejnirattisai Wanwisa, Edmans Matthew, Fyfe Alexander, Imlach Carol, View ORCID Profile Kooblall Kreepa, Lim Nicholas, Liu Chang, Lopez-Camacho Cesar, McInally Carol-Anne, View ORCID Profile Ramamurthy Narayan, View ORCID Profile Ratcliff Jeremy, Supasa Piyada, Wang Beibei, Mentzer Alexander J, Marc Turner, Calum Semple, View ORCID Profile Baillie John Kenneth, ISARIC4C Investigators, Harvala Heli, View ORCID Profile Gavin Screaton, View ORCID Profile Temperton Nigel, View ORCID Profile Klenerman Paul, Jarvis Lisa, View ORCID Profile Gupta Sunetra, View ORCID Profile Simmonds Peter (2020). Neutralising antibodies to SARS coronavirus 2 in Scottish blood donors - a pilot study of the value of serology to determine population exposure. medRxiv.
Cited by
Sorted by citations
Monin, L., Laing, A. G., Muñoz‐Ruiz, M., McKenzie, D. R., del Barrio, I. D. M., Alaguthurai, T., Domingo‐Vila, C., Hayday, T. S., Graham, C., Seow, J., et al. (2021) · The Lancet Oncology · doi:10.1016/s1470-2045(21)00213-8 · Cited by 601 · see citing works
Self-citationmRNA 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
Focosi, D., & Maggi, F. (2021) · Reviews in Medical Virology · doi:10.1002/rmv.2231 · Cited by 148 · see citing works
Memory B cell repertoire for recognition of evolving SARS-CoV-2 spike
Tong, P., Gautam, A. K., Windsor, I. W., Travers, M. E., Chen, Y., Garcia, N., Whiteman, N. B., McKay, L. G. A., Storm, N., Malsick, L. E., et al. (2021) · Cell · doi:10.1016/j.cell.2021.07.025 · Cited by 113 · see citing works
The success of SARS-CoV-2 vaccines and challenges ahead
Subbarao, K. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.06.016 · Cited by 90 · see citing works
Fielding, C. A., Sabberwal, P., Williamson, J. C., Greenwood, E. J. D., Crozier, T. W. M., Zelek, W. M., Seow, J., Graham, C., Huettner, I., Edgeworth, J. D., et al. (2022) · eLife · doi:10.7554/elife.74489 · Cited by 85 · see citing works
Self-citationLumley, S., Rodger, G., Constantinides, B., Sanderson, N. D., Chau, K., Street, T. L., O’Donnell, D., Howarth, A., Hatch, S. B., Marsden, B. D., et al. (2021) · Clinical Infectious Diseases · doi:10.1093/cid/ciab608 · Cited by 70 · see citing works
Lumley, S., Rodger, G., Constantinides, B., Sanderson, N., Chau, K. K., Street, T. L., O’Donnell, D., Howarth, A., Hatch, S. B., Marsden, B. D., et al. (2021) · medRxiv · doi:10.1101/2021.03.09.21253218 · Cited by 48 · see citing works
Polyiam, K., Phoolcharoen, W., Butkhot, N., Srisaowakarn, C., Thitithanyanont, A., Auewarakul, P., Hoonsuwan, T., Ruengjitchatchawalya, M., Mekvichitsaeng, P., & Roshorm, Y. M. (2021) · Scientific Reports · doi:10.1038/s41598-021-99642-w · Cited by 35 · see citing works
SARS-CoV-2 501Y.V2 (B.1.351) elicits cross-reactive neutralizing antibodiesPreprint
Moyo-Gwete, T., Madzivhandila, M., Makhado, Z., Ayres, F., Mhlanga, D., Oosthuysen, B., Lambson, B., Kgagudi, P., Tegally, H., Iranzadeh, A., et al. (2021) · bioRxiv · doi:10.1101/2021.03.06.434193 · Cited by 134 · see citing works
Dicken, S. J., Murray, M. J., Thorne, L., Reuschl, A., Forrest, C., Ganeshalingham, M., Muir, L., Kalemera, M. D., Palor, M., McCoy, L. E., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.22.436468 · Cited by 30 · see citing works
Self-citationKaku, Y., Kuwata, T., Zahid, H. M., Hashiguchi, T., Noda, T., Kuramoto, N., Biswas, S., Matsumoto, K., Shimizu, M., Kawanami, Y., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109385 · Cited by 26 · see citing works
Rotavirus as an Expression Platform of Domains of the SARS-CoV-2 Spike Protein
Philip, A. A., & Patton, J. (2021) · Vaccines · doi:10.3390/vaccines9050449 · Cited by 27 · see citing works
Altomare, C. G., Adelsberg, D. C., Carreño, J. M., Sapse, I. A., Amanat, F., Ellebedy, A. H., Simon, V. R., Krammer, F., & Bajic, G. (2022) · mBio · doi:10.1128/mbio.03580-21 · Cited by 24 · see citing works
Identification and Development of Therapeutics for COVID-19
Rando, H. M., Wellhausen, N., Ghosh, S., Lee, A. J., Dattoli, A. A., Hu, F., Byrd, J. B., Rafizadeh, D. N., Qi, Y., Sun, Y., et al. (2021) · Lund University Publications (Lund University) · Cited by 26 · see citing works
Fatihi, S., Rathore, S., Pathak, A. K., Gahlot, D., Mukerji, M., Jatana, N., & Thukral, L. (2021) · Current Research in Structural Biology · doi:10.1016/j.crstbi.2021.11.002 · Cited by 20 · see citing works
Identification and Development of Therapeutics for COVID-19
Rando, H. M., Wellhausen, N., Ghosh, S., Lee, A. J., Dattoli, A. A., Hu, F., Byrd, J. B., Rafizadeh, D. N., Lordan, R., Qi, Y., et al. (2021) · mSystems · doi:10.1128/msystems.00233-21 · Cited by 25 · see citing works
Ghotloo, S., Maghsood, F., Golsaz‐Shirazi, F., Amiri, M. M., Moog, C., & Shokri, F. (2022) · Reviews in Medical Virology · doi:10.1002/rmv.2347 · Cited by 12 · see citing works
Song, Y., Ge, Z., Cui, S., Tian, D., Wan, G., Zhu, S., Wang, X., Wang, Y., Zhao, X., Xiang, P., et al. (2021) · Microbiology Spectrum · doi:10.1128/spectrum.00273-21 · Cited by 12 · see citing works
Smyth, D. S., Trujillo, M., Cheung, K., Gao, A., Hoxie, I., Kannoly, S., Kubota, N., Markman, M., San, K. M., Sompanya, G., et al. (2021) · medRxiv · doi:10.1101/2021.03.21.21253978 · Cited by 10 · see citing works
TONG, J. J., Zhu, C., Lai, H., Feng, C., & Zhou, D. (2021) · Vaccines · doi:10.3390/vaccines9030296 · Cited by 8 · see citing works
Yang, Y., Liu, S., Luo, Y., Wang, B., Wang, J., Li, J., Li, J., Ye, B., Wang, Y., & Xi, J. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011119 · Cited by 7 · see citing works
Passive Immunity Should and Will Work for COVID-19 for Some Patients
Cimolai, N. (2021) · Clinical Hematology International · doi:10.2991/chi.k.210328.001 · Cited by 6 · see citing works
Influenza A H1N1–mediated pre-existing immunity to SARS-CoV-2 predicts COVID-19 outbreak dynamicsPreprint
Almazán, N. M., Rahbar, A., Carlsson, M., Hoffman, T., Kolstad, L., Rönnberg, B. J., Pantalone, M. R., Lewensohn‐Fuchs, I., Nauclér, A., Ohlin, M., et al. (2021) · medRxiv · doi:10.1101/2021.12.23.21268321 · Cited by 6 · see citing works
Cheng, M. H., Krieger, J., Xiang, Y., Kaynak, B., Shi, Y., Arditi, M., & Bahar, İ. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3907841 · Cited by 4 · see citing works
Altomare, C. G., Adelsberg, D. C., Carreño, J. M., Sapse, I. A., Amanat, F., Ellebedy, A. H., Simon, V. R., Krammer, F., & Bajic, G. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.08.451649 · Cited by 1 · see citing works
A importância da resposta imune celular na Covid-19
Napimoga, M. H., & Pinho, A. J., Jr. (2021) · InterAmerican Journal of Medicine and Health · doi:10.31005/iajmh.v4i.185
- Authors
- Graham, C., Seow, J., Huettner, I., Khan, H., Kouphou, N., Acors, S., Winstone, H., Pickering, S., Galao, R. P., Lista, M. J., Jimenez-Guardeno, J. M., Laing, A. G., Wu, Y., Joseph, M., Muir, L., Ng, W. M., Duyvesteyn, H. M. E., Zhao, Y., Bowden, T. A., Shankar-Hari, M., Rosa, A., Cherepanov, P., McCoy, L. E., Hayday, A. C., Neil, S. J. D., Malim, M. H., & Doores, K. J.
- Affiliations
- King's College London (GB)
- University College London (GB)
- Centre for Human Genetics (GB)
- The Francis Crick Institute (GB)
- Corresponding author
- Doores, Katie J.
- ORCID
- Seow, Jeffrey
- Khan, Hataf
- Kouphou, Neophytos
- Acors, Sam
- Winstone, Helena
- Pickering, Suzanne
- Laing, Adam G.
- Wu, Yin
- Joseph, Magdalene
- Muir, Luke
- Ng, Weng M.
- Duyvesteyn, Helen M. E.
- Zhao, Yuguang
- Bowden, Thomas A.
- Rosa, Annachiara
- Cherepanov, Peter
- McCoy, Laura E.
- Hayday, Adrian C.
- Neil, Stuart J.D.
- Malim, Michael H.
- Doores, Katie J.
- Venue
- bioRxiv (Cold Spring Harbor Laboratory)
- Publisher
- openRxiv
- Published
- 2021-02-03
- PMC
- PMC7872354
- OpenAlex
- W3127921995
- Cited by
- 27
- References
- 73
- Citations by year
- 2023: 1 · 2022: 3 · 2021: 23
- Type
- posted content
- Language
- en
- Open access
- green
- doi.org
- Licence
- Locations
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- Funders
- Wellcome Trust (203141/Z/16/Z, 208354/Z/17/Z, MR/S023747/1, 208354, 106223, Z/17/Z, 106223/Z/14/Z, FC001061, 203141, MR/R015643/1)
- Francis Crick Institute (FC001061)
- King's College Hospital NHS Foundation Trust
- Cancer Research UK (FC001061, MR/N013700/1, MR/R015643/1, 203141/Z/16/Z)
- National Institute for Health and Care Research (203141/Z/16/Z., 2016-16-011, MR/S007555/1, COVID-19, CS-2016-16-011)
- Department of Health and Social Care (COVID-19)
- King's College London (MR/N013700/1)
- Rosetrees Trust
- UK Coronavirus Immunology Consortium
- Medical Research Council (MR/S023747/1, MR/R015643/1, FC001061, 203141/Z/16/Z, MR/N013700/1, MR/S007555/1, MR/R008698/1, MC_PC_15068, COVID-19)
- National Institute of Allergy and Infectious Diseases (COVID-19, AI150472, U54AI150472)
- 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, B.1.1.7 variant, neutralizing monoclonal antibodies, spike protein, N-terminal domain, receptor binding domain, S2 subunit, neutralization resistance, antigenic drift, antibody epitopes, ACE2 receptor
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