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
Items 701–800 of 803
The diversity of the glycan shield of sarbecoviruses closely related to SARS-CoV-2Preprint
Allen, J., Ivory, D., Song, S. G., He, W.-T., Capozzola, T., Yong, P., Burton, D., Andrabi, R., & Crispin, M. (2022) · bioRxiv · doi:10.1101/2022.08.24.505118 · Cited by 2
Nanobody engineering for SARS-CoV-2 neutralization and detectionPreprint
Hannula, L., Kuivanen, S. H., Lasham, J., Kant, R., Kareinen, L., Bogacheva, M. S., Strandin, T. M., Sironen, T. A., Sharma, V., Saviranta, P., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.14.507920 · Cited by 1
Defining neutralization and allostery by antibodies against COVID-19 variantsPreprint
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) · Research Square · doi:10.21203/rs.3.rs-2465199/v1 · Cited by 1
Alshahrani, M. (2023) · Chapman University Digital Commons (Chapman University) · doi:10.36837/chapman.000491 · Cited by 1
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. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.14.557399 · Cited by 1
Differential Adaptive Immune Responses Following SARS-CoV-2 Infection in Children Compared to AdultsPreprint
Nantel, S., Arnold, C. R., Bhatt, M., Galipeau, Y., Bourdin, B., Bowes, J., Zemek, R. L., Langlois, M., Quach, C., Decaluwe, H., et al. (2024) · medRxiv · doi:10.1101/2024.04.05.24305283 · Cited by 1
SARS-CoV-2 B cell receptor signatures in at-risk populations
Flyak, A. I. (2020) · Journal of Clinical Investigation · doi:10.1172/jci144685
WITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v32
Neutralizing antibodies against coronaviruses
Björkman, P. J. (2021) · Microscopy and Microanalysis · doi:10.1017/s1431927621004177
D’Souza, M. P., Palin, A., Calder, T., Golding, H., Kleinstein, S. H., Milliken, E. L., O’Connor, D. H., Tomaras, G. D., Warren, J., & Boggiano, C. (2021) · Vaccine · doi:10.1016/j.vaccine.2021.07.071 · Cited by 1
Rational Vaccine Design by Reverse & Structural Vaccinology and Ontology
Ong, E. (2021) · Deep Blue (University of Michigan) · doi:10.7302/1424
A bacteria-based assay to study SARS-CoV-2 protein-protein interactionsPreprint
Springstein, B. L., Deighan, P., Grabe, G., & Hochschild, A. (2021) · bioRxiv · doi:10.1101/2021.10.07.463611
Datta, S. (2021) · doi:10.33774/chemrxiv-2021-l393t-v35
Insights into Molecular Mechanisms Underlying COVID-19 Pathogenesis and Potential Therapeutics
Ravula, S., Mullaguri, S. C., Akula, S., Silveri, R., & Kancha, R. K. (2021) · Indian Journal of Pharmaceutical Sciences · doi:10.36468/pharmaceutical-sciences.839
Protective characteristics of COVID-19 convalescent and post-vaccination IgG antibodiesPreprint
Klegerman, M. E., Peng, T., Seferovich, I., Rahbar, M. H., Hessabi, M., Tahanan, A., Wanger, A. R., Grimes, C. Z., Ostrosky‐Zeichner, L., Koster, K. J., et al. (2021) · medRxiv · doi:10.1101/2021.11.19.21266547
Verkhivker, G. M., Agajanian, S., Kassab, R., & Krishnan, K. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.09.471953
Watanabe, K., Watanabe, C., Honma, T., Tian, Y., Kawashima, Y., Kawashita, N., Takagi, T., & Fukuzawa, K. (2021) · ChemRxiv · doi:10.26434/chemrxiv.14135138
WITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v31
Structure and function analysis of a potent human neutralizing antibody CA521LALA against SARS-CoV-2Preprint
Dou, C., Qin, C., Wang, L., Song, D., Deng, Y., Wang, W., Dong, C., Ning, Z., Liu, X., Liu, C., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-141793/v1
Datta, S. (2021) · doi:10.33774/chemrxiv-2021-l393t-v33
Mapping the allosteric effects that define functional activity of SARS-CoV-2 specific antibodiesPreprint
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. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.27.474251
Verkhivker, G. M., Agajanian, S., Kassab, R., & Krishnan, K. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.11.487920
Computational Electrostatics Predict Variations in SARS-CoV-2 Spike and Human ACE2 Interactions
Morton, S. P., & Phillips, J. L. (2021) · IEEE International Conference on Bioinformatics and Biomedicine (BIBM) · doi:10.1109/bibm52615.2021.9669765
Kaytaz, M., Akkaya, E., Gümüş, Ş. N., Genç, S., İşsever, H., & Ömer, B. (2022) · Laboratory Medicine · doi:10.1093/labmed/lmac047
Whitehead, T. A., & Francino-Urdaniz, I. M. (2022) · doi:10.1162/2e3983f5.58085a9c
WITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v19
WITHDRAWNPreprint
Datta, S. (2020) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v10
Datta, S. (2021) · doi:10.33774/chemrxiv-2021-l393t-v36
WITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v20
Would It Be Possible to Stabilize Prefusion SARS-COV-2 Spikes with Ligands?Preprint
Lorenzo, M. M., Blasco, R., & Coll, J. M. (2020) · ChemRxiv · doi:10.26434/chemrxiv.13453919
WITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v25
WITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v26
WITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v28
WITHDRAWNPreprint
Datta, S. (2020) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v14
WITHDRAWNPreprint
Datta, S. (2020) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v13
WITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v24
WITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v18
WITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v17
WITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v29
WITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv-2021-l393t-v34
WITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v22
WITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v27
WITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v23
Datta, S. (2021) · doi:10.33774/chemrxiv-2021-l393t-v34
WITHDRAWNPreprint
Datta, S. (2020) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v12
Louten, J. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90565-7.00014-9
SARS-CoV-2 Variant Surveillance in Genomic Medicine Era
Diaconu, C. C., Pitica, I. M., Chivu‐Economescu, M., Necula, L. G., Botezatu, A., Iancu, I. V., Neagu, A. I., Radu, E. L., Matei, L., Ruță, S. M., et al. (2022) · Infectious diseases · doi:10.5772/intechopen.107137
Poumbourios, P., Langer, C., Boo, I., Zakir, T., Akerman, A., Milogiannakis, V., Aggarwal, A., Turville, S. G., & Drummer, H. E. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.08.515567
"SARS-CoV-2 Antibodies and Immunity: Still to Explore for COVID-19"
Chakraborty, A. K. (2022) · Biomedical Journal of Scientific & Technical Research · doi:10.26717/bjstr.2022.45.007229
Suryanto, S., & Gugun, A. M. (2023) · Cerdika Jurnal Ilmiah Indonesia · doi:10.59141/cerdika.v3i7.637
Jirarojwattana, P., & Phoolcharoen, W. (2022) · Chula Digiverse · doi:10.58837/chula.the.2022.293
Development of plant-produced subunit vaccine and therapeutic protein for COVID-19
Siriwattananon, K. (2021) · Chula Digiverse · doi:10.58837/chula.the.2021.306
Monoclonal antibodies lock down SARS-CoV-2 spike
Huang, H., & Angeletti, D. (2023) · Trends in Immunology · doi:10.1016/j.it.2023.09.006
Yasa, S., Guirales-Medrano, S., Machado, D. J., Ford, C. T., & Janies, D. A. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.22.568364
Broadly neutralizing antibodies against emerging delta-coronavirusesPreprint
Rexhepaj, M., Park, Y., Perruzza, L., Asarnow, D. E., McCallum, M., Culap, K., Saliba, C., Leoni, G., Balmelli, A., Yoshiyama, C. N., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.27.586411
Yi, C., Sun, X., Lin, Y., Gu, C., Ding, L., Lu, X., Yang, Z. R., Zhang, Y., Ma, L., Gu, W., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16815705
Yi, C., Sun, X., Lin, Y., Gu, C., Ding, L., Lu, X., Yang, Z. R., Zhang, Y., Ma, L., Gu, W., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16815708
Yi, C., Sun, X., Lin, Y., Gu, C., Ding, L., Lu, X., Yang, Z. R., Zhang, Y., Ma, L., Gu, W., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16815702
van Eerden, F. J., Li, S., Lusiany, T., Ismanto, H. S., Terada, T., Gerle, C., Akamatsu, K., Hirose, M., Sugihara, F., Chen, D. V., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.21.608921
On the Nature of the Interactions That Govern COV-2 Mutants Escape from Neutralizing Antibodies
Sussman, F., & Villaverde, D. S. (2024) · Molecules · doi:10.3390/molecules29215206
Nan, X., Li, Y., Zhang, R., Wang, R., Lv, N., Li, J., Chen, Y., Zhou, B., Wang, Y., Wang, Z., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.07.622402
Sistemas nanoparticulados como estratégia vacinal para SARS-CoV-2
Pagni, R. L. (2024) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.5.2024.tde-03122024-172543
Simpson, J., & Kasson, P. M. (2025) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1012812 · Cited by 2
Yang, Z.-Q., Wen, J., Zheng, M.-Z., Xue, Y., Zheng, L.-T., Yang, Y.-H., Jiang, H., Long, C., & Lin, J. J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.05.641771
Novel progression on clinical therapy of COVID-19: Western and Traditional Chinese Medicines
Xiong, Y., Li, Y., & Xing, F. (2025) · Exploration of Drug Science · doi:10.37349/eds.2025.1008102
Carter, J. J., Hurlburt, N. K., Scherer, E. M., Singh, S., Rodarte, J. V., Smith, R. A. J., Lewis, P., Kinzelman, R., Kieltyka, J., Cabán, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.31.646278
Dissecting serum polyclonal antibody escape to SARS-CoV-2 variants by deep mutational learning
Shlesinger, D., Sadílek, V., Minot, M., Stamkopoulos, E. T., Bikias, T., Kuhn, R., Agrafiotis, A., Taft, J. M., Yermanos, A., & Reddy, S. T. (2025) · bioRxiv · doi:10.1016/j.crmeth.2026.101417 · Cited by 1
B Cell Epitope Mapping by High-Density Competition ELISAs
Vance, D. J., & Mantis, N. J. (2025) · Methods in molecular biology · doi:10.1007/978-1-0716-4591-8_21 · Cited by 1
Two cross-neutralizing antibodies isolated from a COVID-19 convalescent via single B cell sorting
Hu, Y.-Y., Hu, C.-Q., Su, J.-W., Zhu, B., Liang, H., & Shao, Y.-M. (2025) · Archives of Virology · doi:10.1007/s00705-025-06372-9
Epitope-driven polyfunctional divergence of SARS-CoV-2 RBD antibodies
Rosenbaum, P., Planchais, C., Bruel, T., Beretta, M., Staropoli, I., Bolland, W., Guivel‐Benhassine, F., Planas, D., French COVID Cohort Study Group, CORSER Study Group, et al. (2026) · iScience · doi:10.1016/j.isci.2026.117345
Woodward, S. E., McMillan, B., Gaultier, G. N., Márquez, A. C., Valadbeigy, T., Simmons, K., Nikiforuk, A. M., Bartlett, S., Sekirov, I., Morshed, M. G., et al. (2025) · medRxiv · doi:10.1101/2025.08.26.25334476
Persistent Spike antigenemia is not associated with Post-COVID conditionPreprint
Coppens, L., Górska, A., Hotterbeekx, A., Canziani, L. M., Mateescu, V. O., Gentilotti, E., Pirici, D. N., Berkell, M., Orchestra Biomarker Study Group, Malhotra, S., et al. (2025) · medRxiv · doi:10.1101/2025.10.24.25338528
Additional file 1 of Landscape and selection of vaccine epitopes in SARS-CoV-2
Smith, C. C., Olsen, K. S., Gentry, K. M., Sambade, M., Beck, W. A., Garness, J. A., Entwistle, S., Willis, C., Vensko, S. P., II, Woods, A., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14782768
Valdez‐Cruz, N. A., García-Hernández, E., Espitia, C., Cobos-Marín, L., Altamirano, C., Bando-Campos, C. G., Cofas‐Vargas, L. F., Coronado-Aceves, E. W., González-Hernández, R. A., Hernández‐Peralta, P., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14471586
Nepali, K., Sharma, R., Sharma, S., Thakur, A., & Liou, J.-P. (2022) · Figshare · doi:10.6084/m9.figshare.20962344
Additional file 1 of Broadly neutralizing human antibodies against Omicron subvariants of SARS-CoV-2
Chiang, H.-L., Liang, K.-H., Lu, R.-M., Kuo, T.-W., Lin, Y., & Wu, H.-C. (2023) · Figshare · doi:10.6084/m9.figshare.23812506
Schröder, S., Richter, A., Veith, T., Emanuel, J., Gudermann, L., Friedmann, K., Jeworowski, L. M., Mühlemann, B., Jones, T. C., Müller, M. A., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26637489
Yi, C., Sun, X., Lin, Y., Gu, C., Ding, L., Lu, X., Yang, Z., Zhang, Y., Ma, L., Gu, W., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16815699
Additional file 2 of Broadly neutralizing human antibodies against Omicron subvariants of SARS-CoV-2
Chiang, H.-L., Liang, K.-H., Lu, R.-M., Kuo, T.-W., Lin, Y., & Wu, H.-C. (2023) · Figshare · doi:10.6084/m9.figshare.23812509
Li, L., Gao, M., Jiao, P., Zu, S., Deng, Y.-Q., Wan, D., Cao, Y., Duan, J., Aliyari, S. R., Li, J., et al. (2022) · Figshare · doi:10.6084/m9.figshare.19783635
Ayres, F., Lambson, B. E., Mkhize, N. N., Makhado, Z., Mhlanga, D., Serage, R., Moore, P. L., Wibmer, C. K., & Moyo-Gwete, T. (2026) · Structure · doi:10.1016/j.str.2026.01.006
ST-Analyzer: A Packaged Web and Command-Line Interface for Simulation Trajectory AnalysisPreprint
Kern, N. R., Park, S., Cao, Y., & Im, W. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.06.704471
Evaluating southern pigtail macaques as an immunological model for human antibody responses
Zoest, V. P., Lee, W. S., Esterbauer, R., Tan, H., Juno, J. A., & Wheatley, A. K. (2026) · Scientific Reports · doi:10.1038/s41598-026-42695-6
Caractérisation des activités antivirales des anticorps anti-VIH-1 et anti-SARS-CoV-2
Dufloo, J. (2021) · theses.fr (ABES) · doi:10.70675/215798eaz7f82z4e57za8eazf4453d37b8c8
Seroepidemiology of emerging viruses in Bolivia
Jordan, L. I. (2023) · theses.fr (ABES) · doi:10.70675/1070f335z49aaz4d85zb796z713dd35bc6fc
Computational design of an ultrapotent deltacoronavirus miniprotein inhibitor
Avery, N. G., Yoshiyama, C. N., Taylor, A. L., Park, Y., Asarnow, D. E., Perruzza, L., Brown, J. T., Corti, D., Benigni, F., Starr, T. N., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2533456123
Yang, Z., Ding, N., Zheng, M., Wen, J., Xue, Y., Li-ting, Z., Yang, Y., Shi, C.-H., Jiang, H., Lin, J., et al. (2026) · Frontiers in Medicine · doi:10.3389/fmed.2026.1817137
Systems-Scale Structural Modeling Reveals the Germline Architecture of ImmunodominancePreprint
Shrock, E. L., Sun, E., Dhindsa, A., Witwer, M. H., Yu, Z., Ivanochko, D., Lee, I., Coventry, B., Gonzalez, M. B., Julien, J., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.02.729678
Affinity Enhancement in Discrete Multivalent MegaMolecules
Gu, Z., Kimmel, B. R., Modica, J. A., Huang, C., Salaria, R. K., Sridhar, S., Kelleher, N. L., & Mrksich, M. (2026) · ChemBioChem · doi:10.1002/cbic.70411
Skelly, A. N., Fan, C., Keeffe, J. R., Ökten, A. B., Gavor, E., Newby, M. L., Allen, J. D., Kreider, E. F., Ding, W., Osbaldeston, R. A., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2536870123
Self-citationZhou, L., 余志立, Lin, S., Jiang, Y., Gao, J., Ma, Y., Jiang, W., Liang, S., Chen, Y., Zhang, Y., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117582
James‐Pemberton, P. H., Kohli, S., Westlake, A. C., Antill, A., Olkhov, R. V., & Shaw, A. M. (2026) · Frontiers in Virology · doi:10.3389/fviro.2026.1837217
Chi, Y., Yin, H., Huang, C., Ge, Y., Liu, J., Ding, Y., Shi, F., Cui, Z., Ning, S., 焦永军, et al. (2026) · Infectious Medicine · doi:10.1016/j.imj.2026.100277
Chowdary, P. S. (2026) · Research Square · doi:10.21203/rs.3.rs-10529241/v1
Suryadevara, N., Zost, S. J., Powers, J. M., Dadonaite, B., Gilchuk, P., Binshtein, E., Scheaffer, S. M., Leist, S. R., Myers, L., Ravera, S., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.08.15.745004
Sacco, F., Baroni, F., Capolupo, A., Petrocchi, S., Zöller, J., Cerofolini, L., Russomanno, P., Calamandrei, R., Susini, B., Lin, S., et al. (2026) · Angewandte Chemie · doi:10.1002/ange.1540355
Sacco, F., Baroni, F., Capolupo, A., Petrocchi, S., Zöller, J., Cerofolini, L., Russomanno, P., Calamandrei, R., Susini, B., Lin, S., et al. (2026) · Angewandte Chemie International Edition · doi:10.1002/anie.1540355
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