The DOI matches its Crossref record; 106 of the 109 references it cites were found in a registry or an index.
Structures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies
Open accessPublished version of a preprint
Abstract
and RBD epitopes on SARS-CoV-2 spike. Moreover, a 3.4 Å cryo-electron microscopy (cryo-EM) structure of a neutralizing monoclonal Fab-spike complex revealed an epitope that blocks ACE2 receptor binding. Modeling based on these structures suggested different potentials for inter-spike crosslinking by IgGs on viruses, and characterized IgGs would not be affected by identified SARS-CoV-2 spike mutations. Overall, our studies structurally define a recurrent anti-SARS-CoV-2 antibody class derived from VH3-53/VH3-66 and similarity to a SARS-CoV VH3-30 antibody, providing criteria for evaluating vaccine-elicited antibodies.
Overview
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
Verification
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?
In the citing paper
“Moreover, the plasma neutralizing activity, and the relative numbers of RBD-specific memory B cells were equivalent to individuals who recovered from natural infection7,8.”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [8]
In the citing paper
“As expected, plasma neutralizing activity was directly correlated to anti-S and -RBD binding titers in ELISAs7,8 (Fig. 1c, d, and Extended Data Fig. 2a–d).”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [8]
In the citing paper
“A475V is resistant to class 1 antibodies (structurally defined as described29); E484K and Q493R are resistant to class 2 antibodies7,8,12,13,29,30,32,33; while R346S, N439K, and N440K are resistant to class 3 antibodies7,8,12,13,29,33.”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [8]
In the citing paper
“In addition, antibodies that share the same combination of IGHV and IGLV genes in vaccinees comprised 39% of all the clonal sequences (Extended Data Fig. 4b) and 59% when combined with naturally infected individuals7,8 (Fig. 2f), and some of these antibodies were nearly identical (Extended Data Table 3 and 4).”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [8]
In the citing paper
“Class 1 and 2 antibodies are among the most potent and also the most abundant antibodies7,8,21,22,25,39.”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [8]
In the citing paper
“Consistent with the plasma neutralization results, the geometric mean neutralization half-maximal inhibitory concentration of the Pfizer-BioNTech and Moderna vaccinee antibodies were not significantly different from each other or to antibody collections obtained from naturally infected individuals 1.3 or 6.2 months after infection (Fig. 3a and 7,8).”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [8]
In the citing paper
“In anti-RBD ELISAs the mean half-maximal effective concentration (EC50) was higher than that observed in infected individuals after 6.2 months but not significantly different from antibodies obtained 1.3 months after infection (Extended Data Fig. 6a, and Table 5 and 7,8).”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [8]
In the citing paper
“Numerous neutralizing anti-RBD monoclonal antibodies (mAbs) have been characterized, the most potent of which block the RBD-ACE2 interaction (16, 17, 22–24, 32–37).”
From mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection (2021) · cites this paper as [32]
In the citing paper
“Antibodies binding to the RBD can potently block attachment of the virus to ACE2 and thereby neutralize the virus”
From SARS-CoV-2 mRNA vaccination induces functionally diverse antibodies to NTD, RBD, and S2 (2021) · cites this paper as Barnes et al., 2020
In the citing paper
“Their engagement with the RBD is dictated by CDR-H1 and CDR-H2, while the CDR-H3 is characteristically short and makes rather few interactions”
From Antibody evasion by the P.1 strain of SARS-CoV-2 (2021) · cites this paper as Barnes et al., 2020
In the citing paper
“A number of public antibody responses have been reported for SARS-CoV-2, principal among these being VH3–53/VH3–66 and VH1–58 (VH3–30 is also found, but the antibodies are not potent neutralizers) (Yuan et al., 2020; Barnes et al., 2020; Dejnirattisai et al., 2021).”
From Antibody evasion by the P.1 strain of SARS-CoV-2 (2021) · cites this paper as Barnes et al., 2020
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
MAFFT Multiple Sequence Alignment Software Version 7: Improvements in Performance and Usability
Katoh, K., & Standley, D. M. (2013) · Molecular Biology and Evolution · doi:10.1093/molbev/mst010 · Cited by 46,209
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 45,882
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
A pneumonia outbreak associated with a new coronavirus of probable bat origin
Zhou, P., Yang, X.-L., Wang, X.-G., Hu, B., Zhang, L., Zhang, W., Si, H.-R., Zhu, Y., Li, B., Huang, C.-L., et al. (2020) · Nature · doi:10.1038/s41586-020-2012-7 · Cited by 21,969
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
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
Self-citationGuindon, S., Dufayard, J.-F., Lefort, V., Anisimova, M., Hordijk, W., & Gascuel, O. (2010) · Systematic Biology · doi:10.1093/sysbio/syq010 · Cited by 18,376
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463
Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
Sievers, F., Wilm, A., Dineen, D., Gibson, T., Karplus, K., Li, W.-Z., Lopez, R., McWilliam, H., Remmert, M., Söding, J., et al. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.75 · Cited by 15,576
Flagged first, then by citations
3 of the 109 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies
Cao, Y., Wang, J., Jian, F., Xiao, T., Song, W., Yisimayi, A., Huang, W., Li, Q., Wang, P., An, R., et al. (2022) · Nature · doi:10.1038/s41586-021-04385-3 · Cited by 2,006
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
Self-citationEvolution of antibody immunity to SARS-CoV-2
Gaebler, C., Wang, Z., Lorenzi, J. C. C., Muecksch, F., Finkin, S., Tokuyama, M., Cho, A., Jankovic, M., Schaefer-Babajew, D., Oliveira, T. Y., et al. (2021) · Nature · doi:10.1038/s41586-021-03207-w · Cited by 1,674
Self-citationSARS-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
Self-citationEscape 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
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 1,429
mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants
Wang, Z., Schmidt, F., Weisblum, Y., Muecksch, F., Barnes, C. O., Finkin, S., Schaefer-Babajew, D., Cipolla, M., Gaebler, C., Lieberman, J. A., et al. (2021) · Nature · doi:10.1038/s41586-021-03324-6 · Cited by 1,343
Self-citationGreaney, 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
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
“In addition, anti-RBD antibodies often dominate the neutralizing activity of the polyclonal antibody response elicited by natural infection (Barnes et al., 2020a; Steffen et al., 2020; Weisblum et al., 2020).”
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
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
Viral targets for vaccines against COVID-19
Dai, L., & Gao, G. F. (2020) · Nature reviews. Immunology · doi:10.1038/s41577-020-00480-0 · Cited by 1,056
N-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
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
Naturally enhanced neutralizing breadth against SARS-CoV-2 one year after infection
Wang, Z., Muecksch, F., Schaefer-Babajew, D., Finkin, S., Viant, C., Gaebler, C., Hoffmann, H. H., Barnes, C. O., Cipolla, M., Ramos, V., et al. (2021) · Nature · doi:10.1038/s41586-021-03696-9 · Cited by 721
Self-citationReceptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion
Benton, D. J., Wrobel, A. G., Xu, P., Roustan, C., Martin, S. R., Rosenthal, P. B., Skehel, J. J., & Gamblin, S. J. (2020) · Nature · doi:10.1038/s41586-020-2772-0 · Cited by 781
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
Antibody evasion by the P.1 strain of SARS-CoV-2
Dejnirattisai, W., Zhou, D., Supasa, P., Liu, C., Mentzer, A. J., Ginn, H. M., Zhao, Y., Duyvesteyn, H. M. E., Tuekprakhon, A., Nutalai, R., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.055 · Cited by 583
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
Self-citationUltrapotent 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
Walls, A. C., Fiala, B., Schäfer, A., Wrenn, S., Pham, M. N., Murphy, M., Tse, L. V., Shehata, L., O’Connor, M. A., Chen, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.043 · Cited by 532
Cerutti, G., Guo, Y., Zhou, T., Gorman, J., Lee, M., Rapp, M., Reddem, E. R., Yu, J., Bahna, F., Bimela, J., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.03.005 · Cited by 519
Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement
McCallum, M., Czudnochowski, N., Rosen, L. E., Zepeda, S. K., Bowen, J. E., Walls, A. C., Hauser, K., Joshi, A., Stewart, C., Dillen, J. R., et al. (2022) · Science · doi:10.1126/science.abn8652 · Cited by 535
Structural biology of SARS-CoV-2 and implications for therapeutic development
Yang, H., & Rao, Z. (2021) · Nature Reviews Microbiology · doi:10.1038/s41579-021-00630-8 · Cited by 588
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
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
Shrestha, L. B., Foster, C. S. P., Rawlinson, W. D., Tedla, N. T., & Bull, R. A. (2022) · Reviews in Medical Virology · doi:10.1002/rmv.2381 · Cited by 483
Enhanced SARS-CoV-2 neutralization by dimeric IgA
Wang, Z., Lorenzi, J. C. C., Muecksch, F., Finkin, S., Viant, C., Gaebler, C., Cipolla, M., Hoffmann, H.-H., Oliveira, T. Y., Oren, D. A., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abf1555 · Cited by 475
Self-citationReduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera
Supasa, P., Zhou, D., Dejnirattisai, W., Liu, C., Mentzer, A. J., Ginn, H. M., Zhao, Y., Duyvesteyn, H. M. E., Nutalai, R., Tuekprakhon, A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.033 · Cited by 460
The antigenic anatomy of SARS-CoV-2 receptor binding domain
Dejnirattisai, W., Zhou, D., Ginn, H. M., Duyvesteyn, H. M. E., Supasa, P., Case, J. B., Zhao, Y., Walter, T. S., Mentzer, A. J., Liu, C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.032 · Cited by 371
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
Self-citationControlling 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 416
Versatile and multivalent nanobodies efficiently neutralize SARS-CoV-2
Xiang, Y., Nambulli, S., Xiao, Z., Liu, H., Sang, Z., Duprex, W. P., Schneidman‐Duhovny, D., Zhang, C., & Shi, Y. (2020) · Science · doi:10.1126/science.abe4747 · Cited by 396
Mosaic nanoparticles elicit cross-reactive immune responses to zoonotic coronaviruses in mice
Cohen, A. A., Gnanapragasam, P. N. P., Lee, Y. E., Hoffman, P. R., Ou, S. K.-H., Kakutani, L. M., Keeffe, J. R., Wu, H., Howarth, M. R., West, A. P., et al. (2021) · Science · doi:10.1126/science.abf6840 · Cited by 396
Self-citationTali, S. H. S., LeBlanc, J. J., Sadiq, Z., Oyewunmi, O. D., Camargo, C., Nikpour, B., Armanfard, N., Sagan, S. M., & Jahanshahi‐Anbuhi, S. (2021) · Clinical Microbiology Reviews · doi:10.1128/cmr.00228-20 · Cited by 430
Structure-guided multivalent nanobodies block SARS-CoV-2 infection and suppress mutational escape
Koenig, P.-A., Das, H., Liu, H., Kümmerer, B. M., Gohr, F. N., Jenster, L., Schiffelers, L. D. J., Tesfamariam, Y. M., Uchima, M., Wuerth, J. D., et al. (2021) · Science · doi:10.1126/science.abe6230 · Cited by 380
Self-citationEffect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity
Gobeil, S., Janowska, K., McDowell, S., Mansouri, K., Parks, R., Stalls, V., Kopp, M., Manne, K., Li, D., Wiehe, K. J., et al. (2021) · Science · doi:10.1126/science.abi6226 · Cited by 385
Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants
Yuan, M., Huang, D., Lee, C.-C. D., Wu, N. C., Jackson, A. M., Zhu, X., Liu, H., Peng, L., van Gils, M. J., Sanders, R. W., et al. (2021) · doi:10.1101/2021.02.16.430500 · Cited by 364
Heinz, F. X., & Stiasny, K. (2021) · npj Vaccines · doi:10.1038/s41541-021-00369-6 · Cited by 378
Suryadevara, N., Shrihari, S., Gilchuk, P., VanBlargan, L. A., Binshtein, E., Zost, S. J., Nargi, R. S., Sutton, R. E., Winkler, E. S., Chen, E. C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.029 · Cited by 345
Schäfer, A., Muecksch, F., Lorenzi, J. C. C., Leist, S. R., Cipolla, M., Bournazos, S., Schmidt, F., Maison, R. M., Gazumyan, A., Martinez, D. R., et al. (2021) · Journal of Experimental Medicine · doi:10.1084/jem.20201993 · Cited by 305
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 346
Kreye, J., Reincke, S. M., Kornau, H.-C., Sánchez-Sendin, E., Corman, V. M., Liu, H., Yuan, M., Wu, N. C., Zhu, X., Lee, C.-C. D., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.049 · Cited by 347
An alpaca nanobody neutralizes SARS-CoV-2 by blocking receptor interaction
Hanke, L., Vidakovics, L. P., Sheward, D. J., Das, H., Schulte, T., Moliner-Morro, A., Corcoran, M., Achour, A., Hedestam, G. B. K., Hällberg, B. M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18174-5 · Cited by 334
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
Membrane fusion and immune evasion by the spike protein of SARS-CoV-2 Delta variant
Zhang, J., Xiao, T., Cai, Y., Lavine, C. L., Peng, H., Zhu, H., Anand, K., Tong, P., Gautam, A. K., Mayer, M. L., et al. (2021) · Science · doi:10.1126/science.abl9463 · Cited by 288
Increased memory B cell potency and breadth after a SARS-CoV-2 mRNA boost
Muecksch, F., Wang, Z., Cho, A., Gaebler, C., Ben Tanfous, T., DaSilva, J., Bednarski, E., Ramos, V., Zong, S., Johnson, B., et al. (2022) · Nature · doi:10.1038/s41586-022-04778-y · Cited by 297
Self-citationMuecksch, 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
Self-citationMolecular basis of immune evasion by the Delta and Kappa SARS-CoV-2 variants
McCallum, M., Walls, A. C., Sprouse, K. R., Bowen, J. E., Rosen, L. E., Dang, H. V., Marco, A. D., Franko, N., Tilles, S. W., Logue, J. K., et al. (2021) · Science · doi:10.1126/science.abl8506 · Cited by 280
Song, G., He, W., Callaghan, S., Anzanello, F., Huang, D., Ricketts, J., Torres, J. L., Beutler, N., Peng, L., Vargas, S., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23074-3 · Cited by 277
A therapeutic neutralizing antibody targeting receptor binding domain of SARS-CoV-2 spike protein
Kim, C.-M., Ryu, D.-K., Lee, J., Kim, Y., Seo, J. M., Kim, Y., Jeong, J.-H., Kim, M., Kim, J.-I., Kim, P., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20602-5 · Cited by 283
Muecksch, F., Weisblum, Y., Barnes, C. O., Schmidt, F., Schaefer-Babajew, D. J., Wang, Z., Lorenzi, J. C. C., Flyak, A. I., DeLaitsch, A. T., Huey‐Tubman, K. E., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.07.008 · Cited by 279
Self-citationAnti-SARS-CoV-2 receptor-binding domain antibody evolution after mRNA vaccination
Cho, A., Muecksch, F., Schaefer-Babajew, D. J., Wang, Z., Finkin, S., Gaebler, C., Ramos, V., Cipolla, M., Mendoza, P., Agudelo, M., et al. (2021) · Nature · doi:10.1038/s41586-021-04060-7 · Cited by 263
Self-citationSARS-CoV-2 mRNA vaccination induces functionally diverse antibodies to NTD, RBD, and S2
Amanat, F., Thapa, M., Lei, T., Ahmed, S. M. S., Adelsberg, D. C., Carreño, J. M., Strohmeier, S., Schmitz, A. J., Zafar, S., Zhou, J. Q., et al. (2021) · Cell · doi:10.1016/j.cell.2021.06.005 · Cited by 273
Engineered ACE2 receptor traps potently neutralize SARS-CoV-2
Glasgow, A., Glasgow, J., Limonta, D., Solomon, P., Lui, I., Zhang, Y., Nix, M. A., Rettko, N. J., Zha, S., Yamin, R., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2016093117 · Cited by 251
Prevalent, protective, and convergent IgG recognition of SARS-CoV-2 non-RBD spike epitopes
Voss, W. N., Hou, Y. J., Johnson, N. V., Delidakis, G., Kim, J. E., Javanmardi, K., Horton, A. P., Bartzoka, F., Paresi, C., Tanno, Y., et al. (2021) · Science · doi:10.1126/science.abg5268 · Cited by 255
Mosaic RBD nanoparticles protect against challenge by diverse sarbecoviruses in animal models
Cohen, A. A., van Doremalen, N., Greaney, A. J., Andersen, H., Sharma, A., Starr, T. N., Keeffe, J. R., Fan, C., Schulz, J. E., Gnanapragasam, P. N. P., et al. (2022) · Science · doi:10.1126/science.abq0839 · Cited by 264
Self-citationA human coronavirus evolves antigenically to escape antibody immunity
Eguia, R., Crawford, K. H. D., Stevens-Ayers, T., Kelnhofer-Millevolte, L., Greninger, A. L., Englund, J. A., Boeckh, M. J., & Bloom, J. D. (2020) · doi:10.1101/2020.12.17.423313 · Cited by 258
Du, 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
Evolutionary analysis of the Delta and Delta Plus variants of the SARS-CoV-2 viruses
Kannan, S. R., Spratt, A. N., Cohen, A. R., Naqvi, S. H., Chand, H. S., Quinn, T. P., Lorson, C. L., Byrareddy, S. N., & Singh, K. D. (2021) · Journal of Autoimmunity · doi:10.1016/j.jaut.2021.102715 · Cited by 247
Delayed production of neutralizing antibodies correlates with fatal COVID-19
Lucas, C. G. D. O., Klein, J., Sundaram, M. E., Liu, F., Wong, P., Silva, J. D. S., Mao, T., Oh, J. E., Mohanty, S., Huang, J., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01355-0 · Cited by 289
Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies
Cao, Y., Wang, J., Jian, F., Xiao, T., Song, W., Yisimayi, A., Huang, W., Li, Q., Wang, P., An, R., et al. (2021) · Nature · doi:10.1038/d41586-021-03796-6 · Cited by 227
Skelly, D. T., Harding, A. C., Gilbert-Jaramillo, J., Knight, M. L., Longet, S., Brown, A., Adele, S., Adland, E., Brown, H., Team, M. L., et al. (2021) · doi:10.21203/rs.3.rs-226857/v2 · Cited by 216
Liu, H., Wu, N. C., Yuan, M., Bangaru, S., Torres, J. L., Caniels, T. G., van Schooten, J., Zhu, X., Lee, C.-C. D., Brouwer, P. J. M., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.10.023 · Cited by 201
High genetic barrier to SARS-CoV-2 polyclonal neutralizing antibody escape
Schmidt, F., Weisblum, Y., Rutkowska, M., Poston, D., DaSilva, J., Zhang, F., Bednarski, E., Cho, A., Schaefer-Babajew, D. J., Gaebler, C., et al. (2021) · Nature · doi:10.1038/s41586-021-04005-0 · Cited by 216
Self-citationDe novo design of potent and resilient hACE2 decoys to neutralize SARS-CoV-2
Linsky, T. W., Vergara, R., Codina, N., Nelson, J. W., Walker, M. J., Su, W., Barnes, C. O., Hsiang, T.-Y., Esser-Nobis, K., Yu, K., et al. (2020) · Science · doi:10.1126/science.abe0075 · Cited by 216
Self-citationGreaney, 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
“For instance, mutations in the S309 epitope footprint (Pinto et al., 2020) and at sites of escape from antibody C135 (e.g., R346 and N440) (Barnes et al., 2020a; Weisblum et al., 2020) had minimal effects on serum antibody binding ( Figures 3, S3 ).”
InfluentialThe 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
Real-Time Conformational Dynamics of SARS-CoV-2 Spikes on Virus Particles
Lu, M., Uchil, P. D., Li, W., Zheng, D., Terry, D. S., Gorman, J., Shi, W., Zhang, B., Zhou, T., Ding, S., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.11.001 · Cited by 198
Ultrapotent antibodies against diverse and highly transmissible SARS-CoV-2 variants
Wang, L., Zhou, T., Zhang, Y., Yang, E. S., Schramm, C. A., Shi, W., Pegu, A., Oloniniyi, O. K., Henry, A. R., Darko, S. W., et al. (2021) · Science · doi:10.1126/science.abh1766 · Cited by 193
Zhou, P.-P., Yuan, M., Song, G., Beutler, N., Shaabani, N., Huang, D., He, W., Zhu, X., Callaghan, S., Yong, P., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abi9215 · Cited by 196
Structural Characterization of SARS-CoV-2: Where We Are, and Where We Need to Be
Mariano, G., Farthing, R. J., Lale-Farjat, S. L. M., & Bergeron, J. R. C. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.605236 · Cited by 219
COVID-19 and SARS-CoV-2. Modeling the present, looking at the future
Estrada, E. (2020) · Physics Reports · doi:10.1016/j.physrep.2020.07.005 · Cited by 196
SARS-CoV-2 evolution in an immunocompromised host reveals shared neutralization escape mechanisms
Clark, S. A., Clark, L. E., Pan, J., Coscia, A., McKay, L. G. A., Shankar, S., Johnson, R. I., Brusic, V., Choudhary, M. C., Regan, J., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.027 · Cited by 193
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 184
Viral Respiratory Pathogens and Lung Injury
Clementi, N., Ghosh, S., Santis, M. D., Castelli, M., Criscuolo, E., Zanoni, I., Clementi, M., & Mancini, N. (2021) · Clinical Microbiology Reviews · doi:10.1128/cmr.00103-20 · Cited by 202
The humoral response and antibodies against SARS-CoV-2 infection
Qi, H., Liu, B., Wang, X., & Zhang, L. (2022) · Nature Immunology · doi:10.1038/s41590-022-01248-5 · Cited by 195
Structural basis for broad coronavirus neutralization
Sauer, M. M., Tortorici, M. A., Park, Y., Walls, A. C., Homad, L. J., Acton, O. J., Bowen, J. E., Wang, C., Xiong, X., de van der Schueren, W., et al. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00596-4 · Cited by 175
SARS-CoV-2 ferritin nanoparticle vaccines elicit broad SARS coronavirus immunogenicity
Joyce, M. G., Chen, W., Sankhala, R. S., Hajduczki, A., Thomas, P. V., Choe, M., Martinez, E. J., Chang, W. C., Peterson, C. E., Morrison, E. B., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110143 · Cited by 180
SARS-CoV-2 B.1.617 Mutations L452R and E484Q Are Not Synergistic for Antibody Evasion
Ferreira, I. A. T. M., Kemp, S. A., Datir, R., Saito, A., Meng, B., Rakshit, P., Takaori-Kondo, A., Kosugi, Y., Uriu, K., Kimura, I., et al. (2021) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiab368 · Cited by 151
Wang, C., van Haperen, R., Gutierrez-Alvarez, F. J., Li, W., Okba, N. M. A., Albulescu, I. C., Widjaja, I., van Dieren, B., Fernández‐Delgado, R., Sola, I., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21968-w · Cited by 178
A single-dose live-attenuated YF17D-vectored SARS-CoV-2 vaccine candidate
Sánchez-Felipe, L., Vercruysse, T., Sharma, S., Ma, J., Lemmens, V., Looveren, D. V., Javarappa, M. P. A., Boudewijns, R., Malengier‐Devlies, B., Liesenborghs, L., et al. (2020) · Nature · doi:10.1038/s41586-020-3035-9 · Cited by 176
Antivirals with common targets against highly pathogenic viruses
Lu, L., Su, S., Yang, H., & Jiang, S. (2021) · Cell · doi:10.1016/j.cell.2021.02.013 · Cited by 176
Prolonged evolution of the human B cell response to SARS-CoV-2 infection
Sakharkar, M., Rappazzo, C. G., Wieland-Alter, W. F., Hsieh, C.-L., Wrapp, D., Esterman, E. S., Kaku, C. I., Wec, A. Z., Geoghegan, J. C., McLellan, J. S., et al. (2021) · Science Immunology · doi:10.1126/sciimmunol.abg6916 · Cited by 174
Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation
Hurlburt, N. K., Seydoux, E., Wan, Y.-H., Edara, V. V., Stuart, A. B., Feng, J., Suthar, M. S., McGuire, A. T., Stamatatos, L., & Pancera, M. (2020) · Nature Communications · doi:10.1038/s41467-020-19231-9 · Cited by 162
Lévy, Y., Wiedemann, A., Hejblum, B. P., Durand, M., Lefebvre, C., Surénaud, M., Lacabaratz, C., Perreau, M., Foucat, E., Déchenaud, M., et al. (2021) · iScience · doi:10.1016/j.isci.2021.102711 · Cited by 168
Antibody feedback regulates immune memory after SARS-CoV-2 mRNA vaccination
Schaefer-Babajew, D. J., Wang, Z., Muecksch, F., Cho, A., Loewe, M., Cipolla, M., Raspe, R., Johnson, B., Canis, M., DaSilva, J., et al. (2022) · Nature · doi:10.1038/s41586-022-05609-w · Cited by 172
Self-citationAn Alternative Binding Mode of IGHV3-53 Antibodies to the SARS-CoV-2 Receptor Binding Domain
Wu, N. C., Yuan, M., Liu, H., Lee, C.-C. D., Zhu, X., Bangaru, S., Torres, J. L., Caniels, T. G., Brouwer, P. J. M., van Gils, M. J., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108274 · Cited by 158
Zhou, P.-P., Song, G., Liu, H., Yuan, M., He, W., Beutler, N., Zhu, X., Tse, L. V., Martinez, D. R., Schäfer, A., et al. (2023) · Immunity · doi:10.1016/j.immuni.2023.02.005 · Cited by 154
Mini-Review Discussing the Reliability and Efficiency of COVID-19 Vaccines
Doroftei, B., Ciobica, A. S., Ilie, O., Maftei, R., & Ilea, C. G. (2021) · Diagnostics · doi:10.3390/diagnostics11040579 · Cited by 151
Schmitz, A., Weber, A., Bayin, M., Breuers, S., Fieberg, V., Famulok, M., & Mayer, G. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202100316 · Cited by 152
The SARS-CoV-2 spike reversibly samples an open-trimer conformation exposing novel epitopes
Costello, S. M., Shoemaker, S. R., Hobbs, H. T., Nguyen, A. W., Hsieh, C., Maynard, J. A., McLellan, J. S., Pak, J. E., & Marqusee, S. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00735-5 · Cited by 147
Cao, Y., Yisimayi, A., Bai, Y., Huang, W., Li, X., Zhang, Z., Yuan, T., An, R., Wang, J., Xiao, T., et al. (2021) · Cell Research · doi:10.1038/s41422-021-00514-9 · Cited by 140
Antibody-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 150
Self-citationCustódio, T. F., Das, H., Sheward, D. J., Hanke, L., Pažický, S., Pieprzyk, J., Sorgenfrei, M., Schroer, M. A., Gruzinov, A. Y., Jeffries, C. M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19204-y · Cited by 154
Long, S. W., Olsen, R. J., Christensen, P. A., Bernard, D. W., Davis, J. J., Shukla, M. P., Nguyen, M., Saavedra, M. O., Yerramilli, P., Pruitt, L., et al. (2020) · mBio · doi:10.1128/mbio.02707-20 · Cited by 145
Engineering luminescent biosensors for point-of-care SARS-CoV-2 antibody detection
Elledge, S. K., Zhou, X. X., Byrnes, J. R., Martinko, A. J., Lui, I., Pance, K., Lim, S. A., Glasgow, J. E., Glasgow, A. A., Turcios, K., et al. (2021) · Nature Biotechnology · doi:10.1038/s41587-021-00878-8 · Cited by 146
Wang, Z., Muecksch, F., Cho, A., Gaebler, C., Hoffmann, H.-H., Ramos, V., Zong, S., Cipolla, M., Johnson, B., Schmidt, F., et al. (2022) · Immunity · doi:10.1016/j.immuni.2022.04.003 · Cited by 145
Self-citation
Metadata
- Authors
- Barnes, C. O., West, A. P., Huey-Tubman, K. E., Hoffmann, M. A. G., Sharaf, N. G., Hoffman, P. R., Koranda, N., Gristick, H. B., Gaebler, C., Muecksch, F., Lorenzi, J. C. C., Finkin, S., Hägglöf, T., Hurley, A., Millard, K. G., Weisblum, Y., Schmidt, F., Hatziioannou, T., Bieniasz, P. D., Caskey, M., Robbiani, D. F., Nussenzweig, M. C., & Bjorkman, P. J.
- Affiliations
- California Institute of Technology (US)
- Rockefeller University (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Nussenzweig, Michel C.
- ORCID
- Barnes, Christopher O.
- West, Anthony P.
- Hoffmann, Magnus A.G.
- Sharaf, Naima G.
- Hoffman, Pauline R.
- Koranda, Nicholas
- Gristick, Harry B.
- Gaebler, Christian
- Muecksch, Frauke
- Lorenzi, Julio C. Cetrulo
- Finkin, Shlomo
- Hägglöf, Thomas
- Hurley, Arlene
- Millard, Katrina G.
- Weisblum, Yiska
- Schmidt, Fabian
- Bieniasz, Paul D.
- Caskey, Marina
- Robbiani, Davide F.
- Nussenzweig, Michel C.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2020-08
- Volume
- 182
- Issue
- 4
- Pages
- 828-842.e16
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC7311918
- OpenAlex
- W3036607916
- Cited by
- 795
- References
- 109
- Citations by year
- 2026: 34 · 2025: 49 · 2024: 50 · 2023: 84 · 2022: 151 · 2021: 319 · 2020: 107
- FWCI
- 21.66
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion, cc-by-nc-nd)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion, cc-by)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- Funders
- National Center for Advancing Translational Sciences (UL1 TR001866)
- Burroughs Wellcome Fund
- Howard Hughes Medical Institute
- Basic Energy Sciences (DE-AC02-76SF00515)
- National Institute of General Medical Sciences (P41GM103393, 2U19AI111825, P50 8 P50 AI150464-13, P01-AI138938-S1)
- Bill and Melinda Gates Foundation (INV-002143)
- Office of Science
- Biological and Environmental Research
- U.S. Department of Energy
- Beckman Institute, California Institute of Technology
- George Mason University
- California Institute of Technology
- National Institutes of Health
- Rockefeller University
- Icahn School of Medicine at Mount Sinai
- 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 › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Keywords
- SARS-CoV-2 spike protein, human antibodies, neutralizing antibodies, ACE2 binding, IgG, spike protein mutations, vaccine-elicited antibodies, antibody structure
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
