The DOI matches its Crossref record; 76 of the 77 references it cites were found in a registry or an index, and 1 are not checked yet.
SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies
Open accessPublished version of a preprint
Abstract
The coronavirus disease 2019 (COVID-19) pandemic presents an urgent health crisis. Human neutralizing antibodies that target the host ACE2 receptor-binding domain (RBD) of the severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) spike protein 1-5 show promise therapeutically and are being evaluated clinically 6-8. Here, to identify the structural correlates of SARS-CoV-2 neutralization, we solved eight new structures of distinct COVID-19 human neutralizing antibodies 5 in complex with the SARS-CoV-2 spike trimer or RBD. Structural comparisons allowed us to classify the antibodies into categories: (1) neutralizing antibodies encoded by the VH3-53 gene segment with short CDRH3 loops that block ACE2 and bind only to 'up' RBDs; (2) ACE2-blocking neutralizing antibodies that bind both up and 'down' RBDs and can contact adjacent RBDs; (3) neutralizing antibodies that bind outside the ACE2 site and recognize both up and down RBDs; and (4) previously described antibodies that do not block ACE2 and bind only to up RBDs 9. Class 2 contained four neutralizing antibodies with epitopes that bridged RBDs, including a VH3-53 antibody that used a long CDRH3 with a hydrophobic tip to bridge between adjacent down RBDs, thereby locking the spike into a closed conformation. Epitope and paratope mapping revealed few interactions with host-derived N-glycans and minor contributions of antibody somatic hypermutations to epitope contacts. Affinity measurements and mapping of naturally occurring and in vitro-selected spike mutants in 3D provided insight into the potential for SARS-CoV-2 to escape from antibodies elicited during infection or delivered therapeutically. These classifications and structural analyses provide rules for assigning current and future human RBD-targeting antibodies into classes, evaluating avidity effects and suggesting combinations for clinical use, and provide insight into immune responses against SARS-CoV-2.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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 [7]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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 [7]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“The T478K mutation in the RBD is unique to the Delta variant and falls within the epitope region of potent neutralizing monoclonal antibodies categorized as 'Class1' 17”
From Reduced sensitivity of SARS-CoV-2 variant Delta to antibody neutralization (2021) · cites this paper as [17]
Experimental — accuracy not yet measuredIn 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 [7]
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 [7]
In the citing paper
“Although circulating antibodies derived from plasma cells wane over time, long-lived immune memory can persist in expanded clones of memory B cells7,20.”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [7]
In the citing paper
“As seen in natural infection, a majority of the antibodies tested (9/17) were at least ten-fold less effective against pseudotyped viruses carrying the E484K mutation7,12,29.”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [7]
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 [7]
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 [7]
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 [7]
In the citing paper
“In contrast to the earlier time point, 13 of 15 neutralizing antibodies obtained after 12 months interfered only with C121, a class 2 antibody3,23 (Fig. 4c, Extended Data Fig. 9).”
From Naturally enhanced neutralizing breadth against SARS-CoV-2 one year after infection (2021) · cites this paper as [23]
In the citing paper
“Residue S477 is close to the receptor binding site (Fig ED2) and part of the epitope recognized by the S2E12 and C102 neutralizing antibodies 17,18 .”
From Spread of a SARS-CoV-2 variant through Europe in the summer of 2020 (2021) · cites this paper as [17]
In the citing paper
“a potent Ab that can recognize both “up” and “down” SARS-CoV-2 RBD conformations [41].”
From Deep geometric representations for modeling effects of mutations on protein-protein binding affinity (2021) · cites this paper as [41]
In the citing paper
“Importantly, our spike did not contain R346K, which has been observed at relatively low frequency (<10%) within the Omicron lineage, but which is known to mediate escape from class 3 neutralizing monoclonal antibodies such as AZD1061/cilgavimab (Barnes et al., 2020; Dong et al., 2021; Greaney et al., 2021b).”
From mRNA-based COVID-19 vaccine boosters induce neutralizing immunity against SARS-CoV-2 Omicron variant (2022) · 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
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
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
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463
MolProbity : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115
Overview of the CCP 4 suite and current developments
Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G. W., McCoy, A., et al. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910045749 · Cited by 12,353
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
Punjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017) · Nature Methods · doi:10.1038/nmeth.4169 · Cited by 11,626
Inference of Macromolecular Assemblies from Crystalline State
Krissinel, E., & Henrick, K. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.05.022 · Cited by 10,007
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
Cited by
Sorted by citations
Items 501–600 of 1,004
Ng, K. T., Mohd-Ismail, N. K., & Tan, Y. (2021) · Vaccines · doi:10.3390/vaccines9020178 · Cited by 28
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
Exploring the immune evasion of SARS-CoV-2 variant harboring E484K by molecular dynamics simulations
Wu, L., Peng, C., Yang, Y., Shi, Y., Zhou, L., Xu, Z., & Zhu, W. (2021) · Briefings in Bioinformatics · doi:10.1093/bib/bbab383 · Cited by 26
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
Yuan, M., Chen, X., Zhu, Y., Dong, X., Liu, Y., Qian, Z., Ye, L., & Liu, P. (2022) · Journal of Virology · doi:10.1128/jvi.00775-22 · Cited by 27
S glycoprotein diversity of the Omicron variantPreprint
Sarkar, R., Lo, M., Saha, R., Dutta, S., & Chawla‐Sarkar, M. (2021) · medRxiv · doi:10.1101/2021.12.04.21267284 · Cited by 26
Lubin, J. H., Markosian, C., Balamurugan, D., Ma, M. T., Chen, C.-H., Liu, D., Pasqualini, R., Arap, W., Burley, S. K., & Khare, S. D. (2023) · JCI Insight · doi:10.1172/jci.insight.168296 · Cited by 26
COVID-19 influenced gut dysbiosis, post-acute sequelae, immune regulation, and therapeutic regimens
Raj, S., Bruce, A. W., Anbalagan, M., Srinivasan, H., Chinnappan, S., Rajagopal, M. S., Khanna, K., Chandramoorthy, H. C. K., & Mani, R. R. (2024) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2024.1384939 · Cited by 26
Structural basis for receptor-binding domain mobility of the spike in SARS-CoV-2 BA.2.86 and JN.1
Yajima, H., Anraku, Y., Kaku, Y., Kimura, K., Plianchaisuk, A., Okumura, K., Nakada-Nakura, Y., Atarashi, Y., Hemmi, T., Kuroda, D., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52808-2 · Cited by 32
Chen, Y., Wu, X., Xu, C., Huang, J., Zhang, L., Qiu, P., Zheng, D., Chen, W., & Zhang, S. (2025) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2025.5614 · Cited by 31
Nitahara, Y., Nakagama, Y., Kaku, N., Candray, K., Michimuko, Y., Tshibangu-Kabamba, E., Kaneko, A., Yamamoto, H., Mizobata, Y., Kakeya, H., et al. (2021) · Microbiology Spectrum · doi:10.1128/spectrum.00965-21 · Cited by 25
Qiao, X., Qu, L., Guo, Y., & Hoshino, T. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c05997 · Cited by 26
Structural Biology of Nanobodies against the Spike Protein of SARS-CoV-2
Tang, Q., Owens, R. J., & Naismith, J. H. (2021) · Viruses · doi:10.3390/v13112214 · Cited by 24
Konrath, K. M., Liaw, K., Wu, Y., Zhu, X., Walker, S. N., Xu, Z., Schultheis, K., Chokkalingam, N., Chawla, H., Du, J., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110318 · Cited by 26
Wang, X., Chen, X., Tan, J., Yue, S., Zhou, R., Xu, Y., Lin, Y., Yang, Y., Zhou, Y. W., Deng, K., et al. (2022) · Cell Host & Microbe · doi:10.1016/j.chom.2022.03.035 · Cited by 25
Skrzat‐Klapaczyńska, A., Bieńkowski, C., Kowalska, J. D., Paciorek, M., Puła, J., Krogulec, D., Stengiel, J., Pawełczyk, A., Perlejewski, K., Osuch, S., et al. (2022) · Vaccines · doi:10.3390/vaccines10040552 · Cited by 27
Sullivan, E., Sung, P.-Y., Wu, W., Berry, N. J., Kempster, S. L., Ferguson, D., Almond, N. M., Jones, I. M., & Roy, P. (2022) · Viruses · doi:10.3390/v14050914 · Cited by 27
Greaney, A. J., Eguia, R. T., Starr, T. N., Khan, K., Franko, N., Logue, J. K., Lord, S. M., Speake, C., Chu, H. Y., Sigal, A., et al. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010592 · Cited by 29
Structural evolution of Delta lineage of SARS-CoV-2
Gomari, M. M., Tarighi, P., Choupani, E., Abkhiz, S., Mohamadzadeh, M., Rostami, N., Sadroddiny, E., Baammi, S., Uversky, V. N., & Dokholyan, N. V. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.11.227 · Cited by 28
Zhou, R., Liu, N., Li, X., Peng, Q., Yiu, C.-K., Huang, H., Yang, D., Du, Z., Kwok, H.-Y., Au, K.-K., et al. (2023) · The Lancet Regional Health - Western Pacific · doi:10.1016/j.lanwpc.2022.100660 · Cited by 26
From Immunogen to COVID-19 vaccines: Prospects for the post-pandemic era
Miao, G., Chen, Z., Cao, H., Wu, W., Chu, X., Liu, H., Zhang, L., Zhu, H., Cai, H., Lu, X., et al. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.114208 · Cited by 27
Future trajectory of SARS-CoV-2: Constant spillover back and forth between humans and animals
Cui, X., Wang, Y., Zhai, J., Xue, M., Zheng, C., & Yu, L. (2023) · Virus Research · doi:10.1016/j.virusres.2023.199075 · Cited by 26
Lenart, K., Cerveira, R. A., Hellgren, F., Ols, S., Sheward, D. J., Kim, C., Cagigi, A., Gagné, M., Davis, B. J., Germosen, D., et al. (2024) · npj Vaccines · doi:10.1038/s41541-024-00806-2 · Cited by 26
Azad, T., Singaravelu, R., Taha, Z., Jamieson, T. R., Boulton, S., Crupi, M. J. F., Martin, N. T., Fekete, E. E. F., Poutou, J., Ghahremani, M., et al. (2021) · Molecular Therapy · doi:10.1016/j.ymthe.2021.02.007 · Cited by 24
Immunodominant antibody germlines in COVID-19
Andreano, E., & Rappuoli, R. (2021) · The Journal of Experimental Medicine · doi:10.1084/jem.20210281 · Cited by 24
Kramer, K. J., Johnson, N. V., Shiakolas, A. R., Suryadevara, N., Periasamy, S., Raju, N., Williams, J. K., Wrapp, D., Zost, S. J., Walker, L. M., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109784 · Cited by 25
Francino-Urdaniz, I. M., & Whitehead, T. A. (2021) · RSC Chemical Biology · doi:10.1039/d1cb00169h · Cited by 28
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
Human inhalable antibody fragments neutralizing SARS-CoV-2 variants for COVID-19 therapy
Minenkova, O., Santapaola, D., Milazzo, F. M., Anastasi, A. M., Battistuzzi, G., Chiapparino, C., Rosi, A., Gritti, G., Borleri, G., Rambaldi, A., et al. (2022) · Molecular Therapy · doi:10.1016/j.ymthe.2022.02.013 · Cited by 24
Role of angiotensin-converting enzyme 2 in fine particulate matter-induced acute lung injury
Zhu, P., Zhang, W., Feng, F., Qin, L., Ji, W., Li, D., Liang, R., Zhang, Y., Wang, Y., Li, M., et al. (2022) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2022.153964 · Cited by 25
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
Molecular aspects of Omicron, vaccine development, and recombinant strain XE: A review
Akash, K., Sharma, A. K., Kumar, D., Singh, S. K., Gupta, G., Chellappan, D. K., Dua, K., & Nagraik, R. (2022) · Journal of Medical Virology · doi:10.1002/jmv.27936 · Cited by 26
A Structure-Based B-cell Epitope Prediction Model Through Combing Local and Global Features
Lu, S., Li, Y., Ma, Q., Nan, X., & Zhang, S. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.890943 · Cited by 23
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
Xiong, H., Sun, H., Wang, S., Yuan, L., Liu, L., Zhu, Y., Zhang, J., Huang, Y., Qi, R., Jiang, Y., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2204256119 · Cited by 21
Ju, B., Fan, Q., Liu, C., Shen, S., Wang, M., Guo, H., Zhou, B., Ge, X., & Zhang, Z. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112532 · Cited by 23
Point-of-Care Devices for Viral Detection: COVID-19 Pandemic and Beyond
Yadav, S. K., Verma, D., Yadav, U., Kalkal, A., Priyadarshini, N., Kumar, A., & Mahato, K. (2023) · Micromachines · doi:10.3390/mi14091744 · Cited by 25
Antibody and B Cell Responses to SARS-CoV-2 Infection and Vaccination: The End of the Beginning
Röltgen, K., & Boyd, S. D. (2023) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-031521-042754 · Cited by 25
Addetia, A., Piccoli, L., Case, J. B., Park, Y., Beltramello, M., Guarino, B., Dang, H. V., Pinto, D., Scheaffer, S. M., Sprouse, K. R., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.17.523798 · Cited by 25
Quarleri, J. F., Delpino, M. V., & Galván, V. (2024) · GeroScience · doi:10.1007/s11357-024-01066-7 · Cited by 27
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
Bridging animal and clinical research during SARS-CoV-2 pandemic: A new-old challenge
Winkler, M. S., Skirecki, T., Brunkhorst, F. M., Cajander, S., Cavaillon, J., Ferrer, R., Flohé, S. B., García‐Salido, A., Giamarellos‐Bourboulis, E. J., Girardis, M., et al. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103291 · Cited by 26
Ferraz, M. V. F., Moreira, E. G., Coêlho, D. F., Wallau, G. L., & Lins, R. D. (2021) · Chemical Communications · doi:10.1039/d1cc01747k · Cited by 24
Interaction of serum proteins with SARS-CoV-2 RBD
Yin, Y., Sheng, Y.-J., Wang, M., Ma, Y., & Ding, H. (2021) · Nanoscale · doi:10.1039/d1nr02687a · Cited by 22
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
Cheng, L., Song, S., Fan, Q., Shen, S., Wang, H., Zhou, B., Ge, X., Ju, B., & Zhang, Z. (2021) · Cell Discovery · doi:10.1038/s41421-021-00347-1 · Cited by 23
Lu, J., Yin, Q., Pei, R., Zhang, Q., Qu, Y., Pan, Y., Sun, L., Gao, D., Liang, C., Yang, J., et al. (2022) · Virologica Sinica · doi:10.1016/j.virs.2022.02.005 · Cited by 24
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-citationTargeted escape of SARS-CoV-2 in vitro from monoclonal antibody S309, the precursor of sotrovimab
Magnus, C. L., Hiergeist, A., Schuster, P., Rohrhofer, A., Medenbach, J., Gessner, A., Peterhoff, D., & Schmidt, B. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.966236 · Cited by 23
Converting non-neutralizing SARS-CoV-2 antibodies into broad-spectrum inhibitors
Weidenbacher, P. A. B., Waltari, E., Kobara, I. D. L. R., Bell, B. N., Morris, M. K., Cheng, Y.-C., Hanson, C. V., Pak, J. E., & Kim, P. S. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01140-1 · Cited by 23
Potent monoclonal antibodies neutralize Omicron sublineages and other SARS-CoV-2 variants
Chen, Z., Zhang, P., Matsuoka, Y., Tsybovsky, Y., West, K. A., Santos, C. P., Boyd, L. F., Nguyen, H., Pomerenke, A., Stephens, T., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111528 · Cited by 23
Durie, I. A., Tehrani, Z. R., Karaaslan, E., Sorvillo, T. E., McGuire, J. R., Golden, J. W., Welch, S. R., Kainulainen, M. H., Harmon, J. R., Mousa, J. J., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34923-0 · Cited by 24
Yu, H., Liu, B., Zhang, Y., Gao, X., Wang, Q., Xiang, H., Peng, X., Xie, C., Wang, Y., Hu, P., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36761-0 · 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
de Campos‐Mata, L., Trinité, B., Modrego, A., Vaquero, S. T., Pradenas, E., Pons-Grífols, A., Melero, N. R., Carlero, D., Marfil, S., Santiago, C. A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45171-9 · Cited by 24
Karim, F., Riou, C., Bernstein, M. P., Jule, Z., Lustig, G., van Graan, S., Keeton, R., Upton, J., Ganga, Y., Khan, K., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-46673-2 · Cited by 26
Starr, T. N., Czudnochowski, N., Zatta, F., Park, Y., Liu, Z., Addetia, A., Pinto, D., Beltramello, M., Hernandez, P., Greaney, A. J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.06.438709 · Cited by 24
Hendricks, G. G., Grigoryan, L., Navarro, M. J., Catanzaro, N., Hubbard, M. L., Powers, J. M., Mattocks, M. D., Treichel, C., Walls, A. C., Lee, J., et al. (2025) · Science Translational Medicine · doi:10.1126/scitranslmed.adu2085 · Cited by 24
Colson, P., Devaux, C. A., Lagier, J., Gautret, P., & Raoult, D. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10153276 · Cited by 22
Essential tremor amplitude modulation by median nerve stimulation
Reis, C., Arruda, B. S., Pogosyan, A. H., Brown, P., & Cagnan, H. (2021) · Scientific Reports · doi:10.1038/s41598-021-96660-6 · Cited by 25
Verkhivker, G. M., Agajanian, S., Öztaş, D. Y., & Gupta, G. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c00766 · Cited by 22
Schardt, J. S., Pornnoppadol, G., Desai, A. A., Park, K. S., Zupancic, J. M., Makowski, E. K., Smith, M. D., Chen, H., Barbosa, M. G. D. M., Cascalho, M., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-99401-x · Cited by 23
Boulton, S., Poutou, J., Martin, N. T., Azad, T., Singaravelu, R., Crupi, M. J. F., Jamieson, T. R., He, X., Marius, R. M., Petryk, J., et al. (2021) · Molecular Therapy · doi:10.1016/j.ymthe.2021.10.008 · Cited by 24
Modeling coronavirus spike protein dynamics: implications for immunogenicity and immune escape
Kunkel, G., Madani, M., White, S. J., Verardi, P. H., & Tarakanova, A. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.11.009 · Cited by 23
Wang, X., Hu, A., Chen, X., Zhang, Y., Yu, F., Yue, S., Li, A., Zhang, J., Pan, Z., Yang, Y., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00954-8 · Cited by 23
Phenotypic determinism and stochasticity in antibody repertoires of clonally expanded plasma cells
Neumeier, D., Yermanos, A., Agrafiotis, A., Csepregi, L., Chowdhury, T., Ehling, R. A., Kuhn, R., Cotet, T., Roberto, R. B. D., Tacchio, M. D., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2113766119 · Cited by 24
Molecular Mechanisms of the Medicines for COVID-19
Komiyama, M. (2022) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.20220179 · Cited by 23
Humoral immunity to SARS-CoV-2 elicited by combination COVID-19 vaccination regimens
Wang, Z., Muecksch, F., Münn, F., Cho, A., Zong, S., Raspe, R., Ramos, V., Johnson, B., Tanfous, T. B., DaSilva, J., et al. (2022) · The Journal of Experimental Medicine · doi:10.1084/jem.20220826 · Cited by 24
Self-citationZhou, 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
Jaago, M., Rähni, A., Pupina, N., Pihlak, A., Sadam, H., Tuvikene, J., Avarlaid, A., Planken, A., Planken, M., Haring, L., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-20849-6 · Cited by 23
Coordinated evolution at amino acid sites of SARS-CoV-2 spike
Neverov, A. D., Fedonin, G. G., Popova, A. V., Bykova, D., & Bazykin, G. A. (2023) · eLife · doi:10.7554/elife.82516 · Cited by 23
Wang, W. B., Yi, B., Lei, Z. H., Zhang, X., Li, J., Li, S. S., Dong, Z. Y., Liang, Y., Li, Q. M., & Su, J. G. (2023) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2023.108540 · Cited by 23
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
Evolution of antibody immunity following Omicron BA.1 breakthrough infectionPreprint
Kaku, C. I., Starr, T. N., Zhou, P.-P., Dugan, H. L., Khalifé, P., Song, G., Champney, E. R., Mielcarz, D. W., Geoghegan, J. C., Burton, D. R., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.21.508922 · 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
Karuna, S., Li, S. S., Grant, S., Walsh, S. R., Frank, I., Casapía, M., Trahey, M., Hyrien, O., Fisher, L. H., Miner, M. D., et al. (2021) · PLoS Medicine · doi:10.1371/journal.pmed.1003868 · Cited by 21
Esparza, T. J., Chen, Y., Martin, N. P., Bielefeldt‐Ohmann, H., Bowen, R. A., Tolbert, W. D., Pazgier, M., & Brody, D. L. (2022) · mAbs · doi:10.1080/19420862.2022.2047144 · Cited by 24
Beeraka, N. M., Sukocheva, O. A., Lukina, E., Liu, J., & Fan, R. (2022) · Reviews in Medical Virology · doi:10.1002/rmv.2346 · Cited by 23
Seow, J., Graham, C., Hallett, S. R., Lechmere, T., Maguire, T. J. A., Huettner, I., Cox, D., Khan, H., Pickering, S., Roberts, R., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110757 · Cited by 18
Feng, B., Chen, Z., Sun, J., Xu, T., Wang, Q., Yi, H., Niu, X., Zhu, J., Fan, M., Hou, R., et al. (2022) · Small Methods · doi:10.1002/smtd.202200387 · Cited by 22
Matsui, Y., Li, L., Prahl, M. K., Cassidy, A. G., Özarslan, N., Golan, Y., Gonzalez, V. J., Lin, C. Y., Jigmeddagva, U., Chidboy, M. A., et al. (2022) · JCI Insight · doi:10.1172/jci.insight.157354 · Cited by 23
Xiong, D., Zhao, X., Luo, S., Cong, Y., Zhang, J. Z. H., & Duan, L. (2022) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.2c00912 · Cited by 23
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-citationNeamțu, A., Mocci, F., Laaksonen, A., & da Silva, F. L. B. (2022) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2022.112986 · Cited by 23
Carnell, G., Billmeier, M., Vishwanath, S., Sans, M. S., Wein, H., George, C. L., Neckermann, P., Rosario, J. M. M. D., Sampson, A., Einhauser, S., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1118523 · Cited by 21
Broadly neutralizing antibodies against COVID-19
Zhou, D., Ren, J., Fry, E. E., & Stuart, D. I. (2023) · Current Opinion in Virology · doi:10.1016/j.coviro.2023.101332 · Cited by 21
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
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
Zhang, Y., Sun, J., Zheng, J. H., Li, S., Rao, H., Dai, J., Zhang, Z., Wang, Y., Liu, D., Chen, Z., et al. (2023) · Advanced Science · doi:10.1002/advs.202303366 · Cited by 24
Addetia, A., Stewart, C., Seo, A. J., Sprouse, K. R., Asiri, A. Y., Al-Mozaini, M., Memish, Z. A., Alshukairi, A. N., & Veesler, D. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114530 · Cited by 19
Dynamic Interactions of Fully Glycosylated SARS-CoV-2 Spike Protein with Various Antibodies
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
Structural basis for broad sarbecovirus neutralization by a human monoclonal antibodyPreprint
Tortorici, M. A., Czudnochowski, N., Starr, T. N., Marzi, R., Walls, A. C., Zatta, F., Bowen, J. E., Jaconi, S., di Iulio, J., Wang, Z., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.07.438818 · Cited by 22
Venkatakrishnan, A., Anand, P., Lenehan, P. J., Ghosh, P., Suratekar, R., Siroha, A., Chowdhury, D. R., O’Horo, J. C., Yao, J. D. C., Pritt, B. S., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-555451/v1 · Cited by 22
A Potent and Protective Human Neutralizing Antibody Against SARS-CoV-2 Variants
Shan, S., Mok, C. K., Zhang, S., Lan, J., Li, J., Yang, Z., Wang, R., Cheng, L., Fang, M., Aw, Z. Q., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.766821 · 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-citationACE2 from Pipistrellus abramus bats is a receptor for HKU5 coronaviruses
Catanzaro, N., Wu, Z., Fan, C., Jefferson, V. A., Abdelgadir, A., Schäfer, A., Yount, B. L., Björkman, P. J., Baric, R. S., & Letko, M. C. (2025) · Nature Communications · doi:10.1038/s41467-025-60286-3 · Cited by 38
Mallano, A., Ascione, A., & Flego, M. (2021) · International Reviews of Immunology · doi:10.1080/08830185.2021.1929205 · Cited by 22
Wolfe, M., Webb, S., Chushak, Y. G., Krabacher, R., Liu, Y., Swami, N. S., Harbaugh, S. V., & Chávez, J. L. (2021) · Scientific Reports · doi:10.1038/s41598-021-01225-2 · Cited by 21
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
Metadata
- Authors
- 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., Robbiani, D. F., Nussenzweig, M. C., West, A. P., & Bjorkman, P. J.
- Affiliations
- California Institute of Technology (US)
- Institute for Research in Biomedicine (CH)
- Howard Hughes Medical Institute (US)
- ORCID
- Venue
- Nature
- Published
- 2020-10-12
- Volume
- 588
- Issue
- 7839
- Pages
- 682-687
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC8092461
- OpenAlex
- W3092403777
- Cited by
- 1,599
- References
- 70
- Citations by year
- 2026: 94 · 2025: 121 · 2024: 181 · 2023: 267 · 2022: 448 · 2021: 440 · 2020: 35
- FWCI
- 39.08
- Type
- journal article
- Language
- en
- Update notices
- correction (2024-04-02)
- Open access
- bronze
- doi.org
- Licence
- Locations
- Nature (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion, cc-by-nc-nd)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- U.S. Department of Energy (P41GM103393, DE-AC02-)
- Burroughs Wellcome Fund
- George Mason University
- California Institute of Technology
- Wellcome Trust
- National Institutes of Health (AI138938, P01 AI138938-S1, AI150464)
- Office of Science (P41GM103393, DE-AC02)
- Beckman Institute, California Institute of Technology
- National Institute of General Medical Sciences (AI150464, P41GM103393)
- National Institute of Allergy and Infectious Diseases (P50AI150464, F30AI147579, P01AI138938)
- Basic Energy Sciences (DE-AC02, P41GM103393)
- Biological and Environmental Research (P41 GM103393)
- SLAC National Accelerator Laboratory (P41GM103393)
- 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, COVID-19 pandemic, neutralizing antibodies, spike protein receptor-binding domain, antibody-antigen complex structure, ACE2 receptor, epitope mapping, N-glycans, somatic hypermutation, antibody escape, avidity, antibody combination therapy, spike trimer
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
