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Structures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies
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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.
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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
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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
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Items 301–400 of 803
Song, G., Yuan, M., Liu, H., Capozzola, T., Lin, R. N., Torres, J. L., He, W., Musharrafieh, R., Dueker, K., Zhou, P.-P., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115948 · Cited by 30
Inhibitory effect on SARS‐CoV‐2 infection of neferine by blocking Ca2+‐dependent membrane fusion
Yang, Y., Yang, P., Huang, C., Wu, Y., Zhou, Z., Wang, X., & Wang, S. (2021) · Journal of Medical Virology · doi:10.1002/jmv.27117 · Cited by 30
Structural basis of Omicron neutralization by affinity-matured public antibodiesPreprint
Sheward, D. J., Pushparaj, P., Das, H., Kim, C., Kim, S., Hanke, L., Dyrdak, R., McInerney, G. M., Albert, J., Murrell, B., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.03.474825 · Cited by 27
Structural understanding of SARS-CoV-2 virus entry to host cells
Le, K. P. U., Kannappan, S., Kim, T., Lee, J. H., Lee, H.-R., & Kim, K. K. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1288686 · Cited by 34
Structural Immunology of SARS ‐ CoV ‐2
Yuan, M., & Wilson, I. A. (2024) · Immunological Reviews · doi:10.1111/imr.13431 · Cited by 29
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) · CaltechAUTHORS (California Institute of Technology) · Cited by 29
Self-citationFreitas, F. C., Ferreira, P. H. B., Favaro, D. C., & de Oliveira, R. J. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c01320 · Cited by 29
Pan-India novel coronavirus SARS-CoV-2 genomics and global diversity analysis in spike protein
Alai, S., Gujar, N., Joshi, M., Gautam, M., & Gairola, S. (2021) · Heliyon · doi:10.1016/j.heliyon.2021.e06564 · Cited by 29
Longitudinal analysis of antibody decay in convalescent COVID-19 patients
Xia, W., Li, M., Wang, Y., Kazis, L. E., Berlo, K., Melikechi, N., & Chiklis, G. R. (2021) · Scientific Reports · doi:10.1038/s41598-021-96171-4 · Cited by 32
Saville, J. W., Berezuk, A., Srivastava, S. S., & Subramaniam, S. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c01062 · Cited by 32
Defining neutralization and allostery by antibodies against COVID-19 variants
Tulsian, N. K., Raghuvamsi, P. V., Qian, X., Gu, Y., Shunmuganathan, B. D. O., Samsudin, F., Wong, Y. H., Lin, J., Purushotorman, K., Kozma, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42408-x · Cited by 27
A Biochemical Perspective of the Nonstructural Proteins (NSPs) and the Spike Protein of SARS CoV-2
Yoshimoto, F. K. (2021) · The Protein Journal · doi:10.1007/s10930-021-09967-8 · Cited by 28
Nayak, K., Gottimukkala, K. P., Kumar, S., Reddy, E. S., Edara, V. V., Kauffman, R. C., Floyd, K. A., Mantus, G. E., Savargaonkar, D., Goel, P. K., et al. (2021) · Virology · doi:10.1016/j.virol.2021.02.002 · Cited by 28
Track-etched membrane microplate and smartphone immunosensing for SARS-CoV-2 neutralizing antibody
Wang, C., Wu, Z., Liu, B., Zhang, P., Lu, J., Li, J., Zou, P., Li, T., Fu, Y., Chen, R., et al. (2021) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2021.113550 · Cited by 28
Mishra, N., Kumar, S., Singh, S., Bansal, T., Jain, N., Saluja, S., Kumar, R., Bhattacharyya, S., Palanichamy, J. K., Mir, R. A., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009958 · Cited by 27
Montgomerie, I., Bird, T. W., Palmer, O. R., Mason, N. C., Pankhurst, T. E., Lawley, B., Hernández, L. C., Harfoot, R., Authier-Hall, A., Anderson, D. E., et al. (2023) · iScience · doi:10.1016/j.isci.2023.106256 · Cited by 27
Genetic determinants of IgG antibody response to COVID-19 vaccination
Bian, S., Guo, X., Yang, X., Wei, Y., Yang, Z., Cheng, S., Yan, J., Chen, Y., Chen, G., Du, X., et al. (2024) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2023.12.005 · Cited by 29
Watanabe, K., Watanabe, C., Honma, T., Tian, Y., Kawashima, Y., Kawashita, N., Takagi, T., & Fukuzawa, K. (2021) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.1c00663 · Cited by 27
SARS-CoV-2: Origin, Evolution, and Targeting Inhibition
Ning, S., Yu, B., Wang, Y., & Wang, F. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.676451 · Cited by 28
Shinnakasu, R., Sakakibara, S., Yamamoto, H. H., Wang, P.-H., Moriyama, S., Sax, N., Ono, C., Yamanaka, A., Adachi, Y., Onodera, T., et al. (2021) · The Journal of Experimental Medicine · doi:10.1084/jem.20211003 · Cited by 28
Marconato, M., Abela, I. A., Hauser, A., Schwarzmüller, M., Katzensteiner, R., Braun, D. L., Epp, S., Audigé, A., Weber, J., Rusert, P., et al. (2022) · PubMed Central · doi:10.5167/uzh-221980 · Cited by 27
Paschold, L., Simnica, D., Willscher, E., Vehreschild, M. J. G. T., Dutzmann, J., Sedding, D., Schultheiß, C., & Binder, M. (2020) · Journal of Clinical Investigation · doi:10.1172/jci142966 · Cited by 26
Barre, A., Damme, E. J. M. V., Simplicien, M., Benoist, H., & Rougé, P. (2020) · Marine Drugs · doi:10.3390/md18110543 · Cited by 27
Dingens, A. S., Pratap, P. P., Malone, K. D., Hilton, S. K., Ketas, T. J., Cottrell, C. A., Overbaugh, J. M., Moore, J. P., Klasse, P. J., Ward, A. B., et al. (2021) · eLife · doi:10.7554/elife.64281 · Cited by 26
Qiao, X., Qu, L., Guo, Y., & Hoshino, T. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c05997 · Cited by 26
Borgoyakova, M. B., Карпенко, Л. И., Рудометов, А. П., Volosnikova, E. A., Merkuleva, I. A., Starostina, E. V., Zadorozhny, A. M., Исаева, А. А., Nesmeyanova, V. S., Васильевич, Ш. Д., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042188 · Cited by 28
Ip, J. D., Kok, K., Chan, W.-M., Chu, A. W., Wu, W., Yip, C. C., To, W., Tsang, O. T., Leung, W.-S., Chik, T. S., et al. (2020) · Clinical Microbiology and Infection · doi:10.1016/j.cmi.2020.10.030 · Cited by 25
Xu, K., An, Y., Li, Q., Huang, W., Han, Y., Zheng, T., Fang, F., Liu, H., Liu, C., Gao, P., et al. (2021) · Emerging Microbes & Infections · doi:10.1080/22221751.2021.1959270 · Cited by 25
Cho, B. G., Gautam, S., Peng, W., Huang, Y., Goli, M., & Mechref, Y. S. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00323 · Cited by 25
Zhao, S., Zhang, H., Yang, X., Zhang, H., Chen, Y., Zhan, Y., Zhang, X., Jiang, R.-D., Liu, M., Liu, L., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25153-x · Cited by 25
Fukuzawa, K., Kato, K., Watanabe, C., Kawashima, Y., Handa, Y., Yamamoto, A., Watanabe, K., Ohyama, T., Kamisaka, K., Takaya, D., et al. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c00694 · Cited by 27
Francino-Urdaniz, I. M., & Whitehead, T. A. (2021) · RSC Chemical Biology · doi:10.1039/d1cb00169h · Cited by 28
Li, R., Mor, M., Ma, B., Clark, A. E., Alter, J., Werbner, M., Lee, J. C., Leibel, S. L., Carlin, A. F., Dessau, M., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03739-5 · Cited by 25
Antibody-mediated immunity to SARS-CoV-2 spike
Errico, J. M., Adams, L. J., & Fremont, D. H. (2022) · Advances in immunology · doi:10.1016/bs.ai.2022.07.001 · Cited by 22
Rabaan, A. A., Al-Ahmed, S. H., Albayat, H., Alwarthan, S. M., Alhajri, M. M., Najim, M. A., Alshehail, B. M., Al-Adsani, W., Alghadeer, A., Abduljabbar, W. A., et al. (2023) · Medicina · doi:10.3390/medicina59030507 · Cited by 26
Moriyama, S., Anraku, Y., Taminishi, S., Adachi, Y., Kuroda, D., Kita, S., Higuchi, Y., Kirita, Y., Kotaki, R., Tonouchi, K., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39890-8 · Cited by 22
Double-Barreled CRISPR Technology as a Novel Treatment Strategy For COVID-19
Nalawansha, D. A., & Samarasinghe, K. T. G. (2020) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.0c00071 · Cited by 24
Zaichuk, T. A., Nechipurenko, Y. D., Adzhubey, A. A., Оникиенко, С. Б., Черешнев, В. А., Zainutdinov, S. S., Kochneva, G. V., Sv, N., & Matveeva, O. V. (2020) · Molecular Biology · doi:10.1134/s0026893320060151 · Cited by 25
Tabll, A. A., Shahein, Y. E., Omran, M. M., Elnakib, M., Ragheb, A., & Amer, K. (2021) · Human Antibodies · doi:10.3233/hab-200441 · Cited by 24
Structural mechanism of SARS-CoV-2 neutralization by two murine antibodies targeting the RBD
Errico, J. M., Zhao, H., Chen, R. E., Liu, Z., Case, J. B., Ma, M., Schmitz, A. J., Rau, M., Fitzpatrick, J. A. J., Shi, P., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109881 · Cited by 23
Uncovering a conserved vulnerability site in SARS‐CoV‐2 by a human antibody
Li, T., Cai, H., Zhao, Y., Li, Y., Lai, Y., Yao, H., Liu, L. D., Sun, Z., van Vlissingen, M. F., Kuiken, T., et al. (2021) · EMBO Molecular Medicine · doi:10.15252/emmm.202114544 · Cited by 23
Rapid identification of neutralizing antibodies against SARS-CoV-2 variants by mRNA display
Tanaka, S., Olson, C. A., Barnes, C. O., Higashide, W., Gonzalez, M. R., Taft, J. D., Richardson, A., Martín-Fernández, M., Bogunovic, D., Gnanapragasam, P. N. P., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110348 · Cited by 20
Self-citationGenomic surveillance, evolution and global transmission of SARS-CoV-2 during 2019–2022
Sharif, N., Alzahrani, K. J., Ahmed, S. N., Khan, A., Banjer, H. J., Alzahrani, F. M., Parvez, A. K., & Dey, S. K. (2022) · PLoS ONE · doi:10.1371/journal.pone.0271074 · Cited by 26
Zhou, J., Liu, Z., Zhang, G., Xu, W., Xing, L., Lu, L., Wang, Q., & Jiang, S. (2022) · Journal of Medical Virology · doi:10.1002/jmv.28172 · Cited by 24
Andreano, E., Paciello, I., Pierleoni, G., Piccini, G., Abbiento, V., Antonelli, G., Pileri, P., Manganaro, N., Pantano, E., Maccari, G., et al. (2023) · Nature Communications · doi:10.1038/s41467-022-35781-6 · Cited by 24
SARS-CoV-2 antibodies recognize 23 distinct epitopic sites on the receptor binding domain
Jiang, J., Boughter, C. T., Ahmad, J., Natarajan, K., Boyd, L. F., Meier-Schellersheim, M., & Margulies, D. H. (2023) · Communications Biology · doi:10.1038/s42003-023-05332-w · Cited by 24
Structure-guided antibody cocktail for prevention and treatment of COVID-19
Su, S.-C., Yang, T., Yu, P., Liang, K.-H., Wy, C., Yang, C.-W., Lin, H.-T., Wang, M.-J. S., Lu, R., Tso, H.-C., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009704 · Cited by 24
Severe COVID-19 patients display a back boost of seasonal coronavirus-specific antibodiesPreprint
Westerhuis, B. M., Aguilar-Bretones, M., Raadsen, M. P., de Bruin, E., Okba, N. M. A., Haagmans, B. L., Langerak, T., Endeman, H., van den Akker, J. P. C., Gommers, D. A. M. P. J., et al. (2020) · medRxiv · doi:10.1101/2020.10.10.20210070 · Cited by 25
Structural review of SARS-CoV-2 antiviral targets
Cui, W., Duan, Y., Gao, Y., Wang, W., & Yang, H. (2024) · Structure · doi:10.1016/j.str.2024.08.005 · Cited by 24
Ong, E., Huang, X., Pearce, R., Zhang, Y., & He, Y. O. (2020) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2020.12.039 · Cited by 24
Community engagement during COVID: A field report from seven CTSAs
Marsh, E. E., Kappelman, M. D., Kost, R. G., Mudd‐Martin, G., Shannon, J., Stark, L. A., & Carrasquillo, O. (2021) · Journal of Clinical and Translational Science · doi:10.1017/cts.2021.785 · Cited by 25
Immune Evasive Effects of SARS-CoV-2 Variants to COVID-19 Emergency Used Vaccines
Zhang, Y., Ndzouboukou, J. B., Gan, M., Lin, X., & Fan, X. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.771242 · Cited by 21
Schmitz, A., Weber, A., Bayin, M., Breuers, S., Fieberg, V., Famulok, M., & Mayer, G. (2021) · Angewandte Chemie · doi:10.1002/ange.202100316 · Cited by 24
Research progress in spike mutations of SARS‐CoV‐2 variants and vaccine development
He, X., He, C., Hong, W., Yang, H. J., & Wei, X. (2023) · Medicinal Research Reviews · doi:10.1002/med.21941 · Cited by 25
COVID-19: The Effect of Host Genetic Variations on Host–Virus Interactions
Chakravarty, S. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00637 · Cited by 23
Zha, L., Zhao, H., Mohsen, M. O., Hong, L., Zhou, Y., Li, Z., Chen, H., Liu, X., Chang, X., Zhang, J., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.06.079830 · Cited by 24
Versatile, Multivalent Nanobody Cocktails Efficiently Neutralize SARS-CoV-2Preprint
Xiang, Y., Nambulli, S., Xiao, Z., Liu, H., Sang, Z., Duprex, W. P., Schneidman‐Duhovny, D., Zhang, C., & Shi, Y. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.24.264333 · Cited by 23
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Joyce, M. G., Chen, W.-H., Sankhala, R. S., Hajduczki, A., Thomas, P. V., Choe, M., Chang, W., Peterson, C. E., Martinez, E., Morrison, E. B., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.09.443331 · Cited by 23
Mannar, D., Saville, J. W., Poloni, C., Zhu, X. Q., Bezeruk, A., Tidey, K., Ahmed, S., Tuttle, K. R., Hassani, F. V., CHOLAK, S., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-46104-2 · Cited by 22
Hangyu, W., Li, P., Shen, J., Wang, H., Linmiao, W., Kangning, H., Yichen, S., Wang, S., & Wang, C. (2024) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.2403.03008 · Cited by 25
Molecular detection of SARS-CoV-2 being challenged by virus variation and asymptomatic infection
Jiang, C., Li, X., Ge, C., Ding, Y., Zhang, T., Cao, S., Meng, L., & Lu, S. (2021) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2021.03.006 · Cited by 21
Antibody evolution to SARS-CoV-2 after single-dose Ad26.COV2.S vaccine in humans
Cho, A., Muecksch, F., Wang, Z., Tanfous, T. B., DaSilva, J., Raspe, R., Johnson, B., Bednarski, E., Ramos, V., Schaefer-Babajew, D. J., et al. (2022) · The Journal of Experimental Medicine · doi:10.1084/jem.20220732 · Cited by 22
Self-citationZhang, Y., Li, Q., Luo, L., Duan, C., Shen, J., & Wang, Z. (2023) · Biotechnology Advances · doi:10.1016/j.biotechadv.2023.108143 · Cited by 23
Huang, R., Jenkins, G. W., Kim, Y., Stanfield, R. L., Singh, A., Martinez‐Yamout, M. A., Kroon, G. J. A., Torres, J. L., Jackson, A. M., Kelley, A., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2303455120 · Cited by 24
Tsai, W.-Y., Ching, L. L., Hsieh, S., Melish, M. E., Nerurkar, V. R., & Wang, W. (2021) · Emerging Microbes & Infections · doi:10.1080/22221751.2021.1925163 · Cited by 22
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Cao, Y., Choi, Y. K., Frank, M., Woo, H., Park, S., Yeom, M. S., Seok, C., & Im, W. (2021) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.1c00552 · Cited by 24
Paschold, L., Klee, B., Gottschick, C., Willscher, E., Diexer, S., Schultheiß, C., Simnica, D., Sedding, D., Girndt, M., Gekle, M., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.876306 · Cited by 21
Cross-reactive sarbecovirus antibodies induced by mosaic RBD nanoparticles
Fan, C., Keeffe, J. R., Malecek, K. E., Cohen, A. A., West, A. P., Baharani, V. A., Rorick, A. V., Gao, H., Gnanapragasam, P. N. P., Rho, S., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2501637122 · Cited by 23
Self-citationGlycosylation and Serological Reactivity of an Expression-enhanced SARS-CoV-2 Viral Spike Mimetic
Chawla, H., Jossi, S. E., Faustini, S. E., Samsudin, F., Allen, J. D., Watanabe, Y., Newby, M. L., Marcial‐Juárez, E., Lamerton, R. E., McLellan, J. S., et al. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167332 · Cited by 19
Design of customized coronavirus receptors
Liu, P., Huang, M., Guo, H., McCallum, M., Si, J.-Y., Chen, Y., Wang, C., Xiao, Y., Shi, L., Xiong, Q., et al. (2024) · Nature · doi:10.1038/s41586-024-08121-5 · Cited by 21
Current and Future Direct-Acting Antivirals Against COVID-19
Chan, S. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.587944 · Cited by 21
Lee, C. Y., Amrun, S. N., Chee, R. S., Goh, Y. S., Mak, T. M., Octavia, S., Yeo, N. K., Chang, Z. W., Tay, M. Z., Torres‐Ruesta, A., et al. (2021) · Clinical & Translational Immunology · doi:10.1002/cti2.1241 · Cited by 20
Bell, B. N., Powell, A. E., Rodríguez, C., Cochran, J. R., & Kim, P. S. (2021) · Protein Science · doi:10.1002/pro.4044 · Cited by 18
Girl, P., Zwirglmaier, K., von Buttlar, H., Wölfel, R., & Müller, K. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.820151 · Cited by 19
A universal DNA aptamer as an efficient inhibitor against spike-protein/hACE2 interactions
Silwal, A. P., Jahan, R., Thennakoon, S. K. S., Arya, S. P., Postema, R. M., Ark, E. C. V., & Tan, X. (2022) · Chemical Communications · doi:10.1039/d2cc02647c · Cited by 19
Choteau, M., Scohy, A., Messe, S., Luyckx, M., Dechamps, M., Montiel, V., Yombi, J. C., Gruson, D., Limaye, N., Michiels, T., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-06038-5 · Cited by 19
Mäkelä, A. R., Uğurlu, H., Hannula, L., Kant, R., Salminen, P., Fagerlund, R., Mäki, S., Haveri, A., Strandin, T. M., Kareinen, L., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37290-6 · Cited by 22
Brockman, M. A., Mwimanzi, F. M., Sang, Y., Ng, K., Agafitei, O., Ennis, S., Lapointe, H. R., Young, L., Umviligihozo, G., Burns, L., et al. (2021) · medRxiv · doi:10.1101/2021.03.17.21253773 · Cited by 19
Structure of a SARS-CoV-2 spike S2 subunit in a pre-fusion, open conformation
Olmedillas, E., Rajamanickam, R. R., Avalos, R. D., Ana-Sosa-Batiz, F., Zyla, D., Zandonatti, M. A., Harkins, S. S., Shresta, S., Hastie, K. M., & Saphire, E. O. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116052 · Cited by 19
Role of the SphK‐S1P‐S1PRs pathway in invasion of the nervous system by SARS‐CoV‐2 infection
Pan, Y., Gao, F., Zhao, S., Han, J., & Chen, F. (2021) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.13483 · Cited by 19
Yang, M., Li, J., Huang, Z., Li, H., Wang, Y., Wang, X., Kang, S., Huang, X., Wu, C., Liu, T., et al. (2021) · Microbiology Spectrum · doi:10.1128/spectrum.01352-21 · Cited by 19
Geographical prevalence of SARS-CoV-2 variants, August 2020 to July 2021
Chan, W. S., Lam, Y. M., Law, J. H. Y., Chan, T. L., Ma, E. S. K., & Tang, B. S. F. (2022) · Scientific Reports · doi:10.1038/s41598-022-08684-1 · Cited by 20
Huffman, A., Ong, E., Hur, J., D’Mello, A., Tettelin, H., & He, Y. O. (2022) · Briefings in Bioinformatics · doi:10.1093/bib/bbac190 · Cited by 20
Adams, L. J., VanBlargan, L. A., Liu, Z., Gilchuk, P., Zhao, H., Chen, R. E., Raju, S., Chong, Z., Whitener, B. M., Shrihari, S., et al. (2023) · Cell Reports Medicine · doi:10.1016/j.xcrm.2023.101305 · Cited by 18
Chang, M., Ke, H., Coherd, C. D., Wang, Y., Mashima, K., Kastrunes, G. M., Huang, C., & Marasco, W. A. (2022) · EBioMedicine · doi:10.1016/j.ebiom.2022.104025 · Cited by 20
Wang, C., van Haperen, R., Gutiérrez-Álvarez, J., Li, W., Okba, N. M. A., Albulescu, I., Widjaja, I., van Dieren, B., Fernandez-Delgado, R., Sola, I., et al. (2020) · doi:10.1101/2020.10.20.346916 · Cited by 15
Barber, K. W., Shrock, E. L., & Elledge, S. J. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.07.027 · Cited by 18
Su, W., Sia, S. F., Schmitz, A. J., Bricker, T. L., Starr, T. N., Greaney, A. J., Turner, J. S., Mohammed, B. M., Liu, Z., Choy, K. T., et al. (2021) · mBio · doi:10.1128/mbio.02395-21 · Cited by 17
Avidity of IgG to SARS-CoV-2 RBD as a Prognostic Factor for the Severity of COVID-19 Reinfection
Manuylov, V. A., Burgasova, O., Borisova, O. V., Васильевна, С. С., Vasina, D. V., Grigoriev, I. V., Kudryashova, A. M., Semashko, M. A., Сергеевич, Ч. Б., Сергеевна, Х. О., et al. (2022) · Viruses · doi:10.3390/v14030617 · Cited by 19
Protein engineering responses to the COVID-19 pandemic
Hsieh, C., & McLellan, J. S. (2022) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102385 · Cited by 17
Oligomerization-driven avidity correlates with SARS-CoV-2 cellular binding and inhibition
Asor, R., Olerinyova, A., Burnap, S. A., Kushwah, M. S., Soltermann, F., Rudden, L. S. P., Hensen, M., Vasiljević, S., Brun, J., Hill, M. L., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2403260121 · Cited by 16
Virion morphology and on-virus spike protein structures of diverse SARS-CoV-2 variants
Ke, Z., Peacock, T. P., Brown, J. C., Sheppard, C., Croll, T. I., Kotecha, A., Goldhill, D. H., Barclay, W., & Briggs, J. A. G. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00303-1 · Cited by 16
Makdasi, E., Zvi, A., Alcalay, R., Noy-Porat, T., Peretz, E., Mechaly, A., Levy, Y., Epstein, E., Chitlaru, T., Tennenhouse, A., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109679 · Cited by 19
de Campos‐Mata, L., Vaquero, S. T., Tachó‐Piñot, R., Piñero, J., Grasset, E. K., Arrieta‐Aldea, I., Melero, N. R., Carolis, C., Horcajada, J. P., Cerutti, A., et al. (2021) · Clinical & Translational Immunology · doi:10.1002/cti2.1339 · Cited by 17
Neutralizing Antibodies to SARS‐CoV‐2 Selected from a Human Antibody Library Constructed Decades Ago
Qiang, M., Ma, P., Li, Y., Liu, H., Harding, A. C., Min, C., Wang, F., Liu, L., Yuan, M., Ji, Q., et al. (2021) · Advanced Science · doi:10.1002/advs.202102181 · Cited by 20
Vanhove, B., Marot, S., So, R. T. Y., Gaborit, B. J., Evanno, G., Malet, I., Lafrogne, G., Mevel, E., Ciron, C., Royer, P., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.761250 · Cited by 20
Braun, B. A., Schein, C. H., & Braun, W. A. (2021) · Bioinformatics and Biology Insights · doi:10.1177/11779322211020316 · Cited by 18
Teruel, N., Crown, M. R., Bashton, M., & Najmanovich, R. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.14.472622 · Cited by 18
Conserved Neutralizing Epitopes on the N-Terminal Domain of Variant SARS-CoV-2 Spike ProteinsPreprint
Wang, Z.-J., Muecksch, F., Cho, A., Gaebler, C., Hoffmann, H., Ramos, V. A., Zong, S., Cipolla, M., Johnson, B., Schmidt, F., et al. (2022) · bioRxiv · doi:10.1101/2022.02.01.478695 · Cited by 20
Self-citationMcConnell, S. A., & Casadevall, A. (2025) · Nature reviews. Immunology · doi:10.1038/s41577-025-01150-9 · Cited by 27
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
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