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Convergent antibody responses to SARS-CoV-2 in convalescent individuals
Open accessPublished version of a preprint
Abstract
During the coronavirus disease-2019 (COVID-19) pandemic, severe acute respiratory syndrome-related coronavirus-2 (SARS-CoV-2) has led to the infection of millions of people and has claimed hundreds of thousands of lives. The entry of the virus into cells depends on the receptor-binding domain (RBD) of the spike (S) protein of SARS-CoV-2. Although there is currently no vaccine, it is likely that antibodies will be essential for protection. However, little is known about the human antibody response to SARS-CoV-2 1-5. Here we report on 149 COVID-19-convalescent individuals. Plasma samples collected an average of 39 days after the onset of symptoms had variable half-maximal pseudovirus neutralizing titres; titres were less than 50 in 33% of samples, below 1,000 in 79% of samples and only 1% of samples had titres above 5,000. Antibody sequencing revealed the expansion of clones of RBD-specific memory B cells that expressed closely related antibodies in different individuals. Despite low plasma titres, antibodies to three distinct epitopes on the RBD neutralized the virus with half-maximal inhibitory concentrations (IC 50 values) as low as 2 ng ml-1. In conclusion, most convalescent plasma samples obtained from individuals who recover from COVID-19 do not contain high levels of neutralizing activity. Nevertheless, rare but recurring RBD-specific antibodies with potent antiviral activity were found in all individuals tested, suggesting that a vaccine designed to elicit such antibodies could be broadly effective.
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“The magnitude of these NAb responses appear to correlate with viral load, with higher responses reported in patients with more severe disease, and in older adults compared with younger adults26–29.”
From Immunological mechanisms of vaccine-induced protection against COVID-19 in humans (2021) · cites this paper as [26]
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 agreement with previous reports3,6,9, there was a broad range of plasma neutralizing activity 3–14 weeks after the second vaccine dose that was similar to that elicited by natural infection in a convalescent cohort after 1.3 months, and greater than the activity at 6.2 months after infection (Fig. 1a, Extended Data Table 1).”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [6]
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
“Spike is the target of SARS-CoV-2 neutralizing antibodies, and the receptor binding domain (RBD) of Spike is the target of >90% of neutralizing antibodies in COVID-19 cases (Brouwer et al., 2020; Piccoli et al., 2020; Robbiani et al., 2020; Rogers et al., 2020; Suthar et al., 2020), with some neutralizing antibodies instead targeting the N-terminal domain (NTD) (Liu et al., 2020).”
From Adaptive immunity to SARS-CoV-2 and COVID-19 (2021) · cites this paper as Robbiani et al., 2020
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
“Although it is unclear how long protective effects last beyond the first few months after vaccination, some studies suggest that the elicited neutralizing activity is maintained for up to 8 months after the natural infection with SARS-CoV-2 (refs. 41,42).”
From Modeling vaccination rollouts, SARS-CoV-2 variants and the requirement for non-pharmaceutical interventions in Italy (2021) · cites this paper as [41]
Experimental — accuracy not yet measuredIn the citing paper
“8 weeks after the second vaccine injection volunteers showed high levels of IgM, and IgG anti-SARS-CoV-2 spike protein (S) and receptor binding domain (RBD) binding titers3,5,6.”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [6]
In the citing paper
“In line with previous reports3,6,9, IgG and IgM levels were significantly higher in the vaccinated group compared to a cohort of convalescent patients assayed 1.3 and 6.2 months after infection, while IgA levels were similar (Extended Data Fig 1j–l).”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [6]
In the citing paper
“We limited our analysis to RBD because plasma RBD antibodies are strongly correlated with neutralizing activity3,10–12.”
From Naturally enhanced neutralizing breadth against SARS-CoV-2 one year after infection (2021) · cites this paper as [3]
In the citing paper
“Consistent with this observation, there was an overall increase in the apparent avidity of plasma antibodies between 1.3 and 12 months3,4 (P < 0.0001) (Extended Data Fig. 7c).”
From Naturally enhanced neutralizing breadth against SARS-CoV-2 one year after infection (2021) · cites this paper as [3]
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 [3]
In the citing paper
“Most serum nAb responses elicited during natural infection are directed at the RBD (21, 23, 30, 31).”
From mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection (2021) · cites this paper as [23]
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 [23]
In the citing paper
“SARS-CoV-2 infection rapidly elicits nAbs (16, 21–24) that decline, but remain detectable, over several months (25–29).”
From mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection (2021) · cites this paper as [23]
In the citing paper
“Analyses of the B cell responses to the spike generally focus on the RBD and on cells sorted with RBD baits introducing an inherent bias by omitting non-RBD targets”
From SARS-CoV-2 mRNA vaccination induces functionally diverse antibodies to NTD, RBD, and S2 (2021) · cites this paper as Robbiani et al., 2020
In the citing paper
“The neutralizing antibodies are produced by B cells with a wide range of heavy chain and light chain V genes (Robbiani et al., 2020; Rogers et al., 2020). SARS-CoV-2 neutralizing antibodies also exhibit little to no somatic hypermutation (Gaebler et al., 2020; Robbiani et al., 2020; Rogers et al., 2020).”
From Adaptive immunity to SARS-CoV-2 and COVID-19 (2021) · cites this paper as Robbiani et al., 2020
In the citing paper
“Although neutralizing antibody titers have not correlated with reduced COVID-19 severity (Dan et al., 2021; Piccoli et al., 2020; Robbiani et al., 2020), SARS-CoV-2 cTfh cell frequencies have been associated with reduced disease severity (Rydyznski Moderbacher et al., 2020).”
From Adaptive immunity to SARS-CoV-2 and COVID-19 (2021) · cites this paper as Robbiani et al., 2020
In the citing paper
“This appears to hold true in the case of SARS-CoV-2, where neutralizing antibody titers (and total Spike antibody titers) have positively correlated with COVID-19 disease severity in large cohort studies (Piccoli et al., 2020; Robbiani et al., 2020).”
From Adaptive immunity to SARS-CoV-2 and COVID-19 (2021) · cites this paper as Robbiani et al., 2020
In the citing paper
“However, it should also be noted that circulating SARS-CoV-2 neutralizing antibody titers are relatively low in a substantial fraction of recovered COVID-19 cases (Dan et al., 2021; Robbiani et al., 2020; Wajnberg et al., 2020), indicating that either the neutralizing antibody potency or the serum concentration is suboptimal in this subset.”
From Adaptive immunity to SARS-CoV-2 and COVID-19 (2021) · cites this paper as Robbiani et al., 2020
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Citations
Cites
A simple method for displaying the hydropathic character of a protein
Kyte, J., & Doolittle, R. F. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90515-0 · Cited by 22,927
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
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
Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein
Walls, A. C., Park, Y.-J., Tortorici, M. A., Wall, A., McGuire, A. T., & Veesler, D. (2020) · doi:10.1101/2020.02.19.956581 · Cited by 8,586
Automated electron microscope tomography using robust prediction of specimen movements
Mastronarde, D. N. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.07.007 · Cited by 5,136
Grifoni, A., Weiskopf, D., Ramirez, S. I., Mateus, J., Dan, J. M., Moderbacher, C. R., Rawlings, S. A., Sutherland, A., Premkumar, L., Jadi, R. S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.015 · Cited by 3,595
Adachi, A., Gendelman, H. E., Koenig, S., Folks, T. M., Willey, R. L., Rabson, A. B., & Martín, M. Á. (1986) · Journal of Virology · doi:10.1128/jvi.59.2.284-291.1986 · Cited by 2,805
Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2349-y · Cited by 1,885
A serological assay to detect SARS-CoV-2 seroconversion in humans
Amanat, F., Stadlbauer, D., Strohmeier, S., Nguyen, T. H. O., Chromikova, V., McMahon, M., Jiang, K., Arunkumar, G. A., Jurczyszak, D., Polanco, J., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-0913-5 · Cited by 1,769
Correlates of protection induced by vaccination
Plotkin, S. A. (2010) · Clinical and Vaccine Immunology · doi:10.1128/cvi.00131-10 · Cited by 1,745
Cited by
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Everett, H., Lean, F. Z. X., Byrne, A. M. P., van Diemen, P. M., Rhodes, S. G., James, J., Mollett, B. C., Coward, V. J., Skinner, P., Warren, C. J., et al. (2021) · Viruses · doi:10.3390/v13010113 · Cited by 67
Breadth and function of antibody response to acute SARS-CoV-2 infection in humans
Huang, K.-Y. A., Tan, T. K., Chen, T.-H., Huang, C., Harvey, R., Hussain, S., Chen, C., Harding, A. C., Gilbert‐Jaramillo, J., Liu, X., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009352 · Cited by 67
Genetic and structural basis for recognition of SARS-CoV-2 spike protein by a two-antibody cocktail
Dong, J., Zost, S. J., Greaney, A. J., Starr, T. N., Dingens, A. S., Chen, E. C., Chen, R. E., Case, J. B., Sutton, R. E., Gilchuk, P., et al. (2021) · doi:10.1101/2021.01.27.428529 · Cited by 55
The Future of Blood Testing Is the Immunome
Arnaout, R., Prak, E. T. L., Schwab, N., Rubelt, F., & Community, T. A. I. R. R. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.626793 · Cited by 66
Broad and potent neutralizing human antibodies to tick-borne flaviviruses protect mice from disease
Agudelo, M., Palus, M., Keeffe, J. R., Bianchini, F., Svoboda, P., Salát, J., Peace, A., Gazumyan, A., Cipolla, M., Kapoor, T., et al. (2021) · The Journal of Experimental Medicine · doi:10.1084/jem.20210236 · Cited by 66
Self-citationImmune evasion and ACE2 binding affinity contribute to SARS-CoV-2 evolution
Ma, W., Fu, H., Jian, F., Cao, Y., & Li, M. (2023) · Nature Ecology & Evolution · doi:10.1038/s41559-023-02123-8 · Cited by 66
Monoclonal antibodies: From magic bullet to precision weapon
Aboul-Ella, H., Gohar, A., Ali, A. A., Ismail, L. M., Mahmoud, A. E. E.-R., Elkhatib, W. F., & Aboul-Ella, H. (2024) · Molecular Biomedicine · doi:10.1186/s43556-024-00210-1 · Cited by 66
Harrington, W. E., Trakhimets, O., Andrade, D. V., Dambrauskas, N., Raappana, A., Jiang, Y., Houck, J., Selman, W., Yang, A., Vigdorovich, V. I., et al. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100253 · Cited by 65
Naturally Acquired SARS-CoV-2 Immunity Persists for Up to 11 Months Following Infection
Giorgi, V. D., West, K. A., Henning, A. N., Chen, L. N., Holbrook, M. R., Gross, R., Liang, J. Y., Postnikova, E. N., Trenbeath, J. L., Pogue, S., et al. (2021) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiab295 · Cited by 65
Karim, F., Gazy, I., Cele, S., Zungu, Y., Krause, R., Bernstein, M. P., Khan, K., Ganga, Y., Rodel, H. E., Mthabela, N., et al. (2021) · eLife · doi:10.7554/elife.67397 · Cited by 64
Self-citationA public antibody class recognizes an S2 epitope exposed on open conformations of SARS-CoV-2 spike
Claireaux, M. A. F., Caniels, T. G., de Gast, M., Han, J., Guerra, D., Kerster, G., van Schaik, B. D. C., Jongejan, A., Schriek, A. I., Grobben, M., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32232-0 · Cited by 64
SARS-CoV-2 Serologic Assay Needs for the Next Phase of the US COVID-19 Pandemic Response
Gundlapalli, A. V., Salerno, R. M., Brooks, J. T., Averhoff, F. M., Petersen, L. R., McDonald, L. C., Iademarco, M. F., Response, C. C.-1., Carroll, Y. I., Gorwitz, R. J., et al. (2020) · Open Forum Infectious Diseases · doi:10.1093/ofid/ofaa555 · Cited by 63
Yang, T., Yu, P., Chang, Y., Kuo, C., Khoo, K., & Hsu, S. D. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101238 · Cited by 63
Cerutti, G., Guo, Y., Wang, P., Nair, M. S., Wang, M., Huang, Y., Yu, J., Liu, L., Katsamba, P. S., Bahna, F. A., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109928 · Cited by 63
Integrative proteomics identifies thousands of distinct, multi-epitope, and high-affinity nanobodies
Xiang, Y., Sang, Z., Bitton, L., Xu, J., Liu, Y., Schneidman‐Duhovny, D., & Shi, Y. (2021) · Cell Systems · doi:10.1016/j.cels.2021.01.003 · Cited by 63
Bloch, E. M., Goel, R., Wendel, S., Burnouf, T., Al‐Riyami, A. Z., Ang, A. L., Angelis, V. D., Dumont, L. J., Land, K. J., Lee, C. K., et al. (2020) · Vox Sanguinis · doi:10.1111/vox.12970 · Cited by 62
Tzou, P. L., Tao, K., Nouhin, J., Rhee, S., Hu, B. D., Pai, S., Parkin, N. T., & Shafer, R. W. (2020) · Viruses · doi:10.3390/v12091006 · Cited by 62
Wendel, S., Kutner, J. M., Machado, R. R. G., Fontão‐Wendel, R., Bub, C. B., Fachini, R. M., Yokoyama, A. P. H., Candelaria, G. D. T. P., Sakashita, A. M., Achkar, R., et al. (2020) · Transfusion · doi:10.1111/trf.16065 · Cited by 62
Chen, P., Lee, N., Cia, C.-T., Ko, W., & Hsueh, P. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.584956 · Cited by 62
A Structural Landscape of Neutralizing Antibodies Against SARS-CoV-2 Receptor Binding Domain
Niu, L., Wittrock, K. N., Clabaugh, G. C., Srivastava, V., & Cho, M. W. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.647934 · Cited by 62
A vaccine-induced public antibody protects against SARS-CoV-2 and emerging variants
Schmitz, A. J., Turner, J. S., Liu, Z., Zhou, J. Q., Aziati, I. D., Chen, R. E., Joshi, A., Bricker, T. L., Darling, T. L., Adelsberg, D. C., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.08.013 · Cited by 62
Landscape of human antibody recognition of the SARS-CoV-2 receptor binding domain
Wheatley, A. K., Pymm, P., Esterbauer, R., Dietrich, M. H., Lee, W. S., Drew, D. R., Kelly, H. G., Chan, L., Mordant, F. L., Black, K. A., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109822 · Cited by 62
Soh, W. T., Liu, Y., Nakayama, E. E., Ono, C., Torii, S., Nakagami, H., Matsuura, Y., Shioda, T., & Arase, H. (2020) · doi:10.1101/2020.11.05.369264 · Cited by 61
Durability of Immunity to SARS-CoV-2 and Other Respiratory Viruses
Siggins, M. K., Thwaites, R. S., & Openshaw, P. (2021) · Trends in Microbiology · doi:10.1016/j.tim.2021.03.016 · Cited by 61
Onodera, T., Kita, S., Adachi, Y., Moriyama, S., Sato, A., Nomura, T., Sakakibara, S., Inoue, T., Tadokoro, T., Anraku, Y., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.08.025 · Cited by 61
B cell receptor repertoire kinetics after SARS-CoV-2 infection and vaccination
Kotagiri, P., Mescia, F., Rae, W. M., Bergamaschi, L., Tuong, Z. K., Turner, L., Hunter, K., Gerber, P. P., Hosmillo, M. D. T., Hess, C., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110393 · Cited by 61
Wang, Z., Zhou, P., Muecksch, F., Cho, A., Tanfous, T. B., Canis, M., Witte, L., Johnson, B., Raspe, R., Schmidt, F., et al. (2022) · The Journal of Experimental Medicine · doi:10.1084/jem.20221006 · Cited by 61
Self-citationFumagalli, V., Ravà, M., Marotta, D., Lucia, P. D., Bono, E. B., Giustini, L., Leo, F. D., Casalgrandi, M., Monteleone, E., Mouro, V., et al. (2024) · Nature Immunology · doi:10.1038/s41590-024-01787-z · Cited by 61
Serum Antibody Profile of a Patient With Coronavirus Disease 2019 Reinfection
To, K. K., Hung, I. F., Chan, K., Yuan, S., To, W., Tsang, D. N., Cheng, V. C., Chen, Z., Kok, K., & Yuen, K. (2020) · Clinical Infectious Diseases · doi:10.1093/cid/ciaa1368 · Cited by 60
Wells, P. M., Doores, K. J., Couvreur, S., Martínez-Nuñez, R. T., Seow, J., Graham, C., Acors, S., Kouphou, N., Neil, S. J. D., Tedder, R. S., et al. (2020) · Journal of Infection · doi:10.1016/j.jinf.2020.10.011 · Cited by 60
Oyaert, M., Scheerder, M. D., Herrewege, S. V., Laureys, G., Assche, S. V., Cambron, M., Naesens, L., Hoste, L., Claes, K., Haerynck, F., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.858399 · Cited by 60
Feldman, J. E., Bals, J., Altomare, C. G., Denis, K. S., Lam, E. C., Hauser, B. M., Ronsard, L., Sangesland, M., Moreno, T. B., Okonkwo, V., et al. (2021) · Science Immunology · doi:10.1126/sciimmunol.abl5842 · Cited by 60
Therapeutic antibodies and fusion inhibitors targeting the spike protein of SARS-CoV-2
Jiang, S., Zhang, X., & Du, L. (2020) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2020.1820482 · Cited by 60
Tomić, S., Đokić, J., Stevanović, D., Ilić, N., Gruden‐Movsesijan, A., Dinić, M., Radojević, D., Bekić, M., Mitrović, N., Tomašević, R., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.614599 · Cited by 59
Modular basis for potent SARS-CoV-2 neutralization by a prevalent VH1-2-derived antibody class
Rapp, M., Guo, Y., Reddem, E. R., Yu, J., Liu, L., Wang, P., Cerutti, G., Katsamba, P. S., Bimela, J. S., Bahna, F. A., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108950 · Cited by 59
Favà, A., Donadeu, L., Sabé, N., Pernin, V., González‐Costello, J., Lladó, L., Meneghini, M., Charmetant, X., García‐Romero, E., Cachero, A., et al. (2021) · American Journal of Transplantation · doi:10.1111/ajt.16570 · Cited by 59
Cerutti, G., Rapp, M., Guo, Y., Bahna, F. A., Bimela, J. S., Reddem, E. R., Yu, J., Wang, P., Liu, L., Huang, Y., et al. (2021) · Structure · doi:10.1016/j.str.2021.05.014 · Cited by 59
Dussupt, V., Sankhala, R. S., Mendez-Rivera, L., Townsley, S., Schmidt, F., Wieczorek, L., Lal, K. G., Donofrio, G. C., Tran, U., Jackson, N. D., et al. (2021) · Nature Immunology · doi:10.1038/s41590-021-01068-z · Cited by 59
Self-citationDesign of the SARS-CoV-2 RBD vaccine antigen improves neutralizing antibody response
Dickey, T. H., Tang, W. K., Butler, B., Ouahes, T., Orr-Gonzalez, S., Salinas, N. D., Lambert, L., & Tolia, N. H. (2022) · Science Advances · doi:10.1126/sciadv.abq8276 · Cited by 59
Focosi, D., Maggi, F., Mazzetti, P., & Pistello, M. (2020) · Reviews in Medical Virology · doi:10.1002/rmv.2170 · Cited by 59
Single-cell profiling of the antigen-specific response to BNT162b2 SARS-CoV-2 RNA vaccine
Kramer, K. J., Wilfong, E. M., Voss, K., Barone, S. M., Shiakolas, A. R., Raju, N., Roe, C. E., Suryadevara, N., Walker, L. M., Wall, S. C., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31142-5 · Cited by 59
Askenase, P. W. (2020) · Journal of Extracellular Vesicles · doi:10.1002/jev2.12004 · Cited by 58
Advances in Neutralization Assays for SARS‐CoV‐2
Lu, Y., Jin, W., Li, Q., Hu, H., Lu, J., & Chen, Z. (2021) · Scandinavian Journal of Immunology · doi:10.1111/sji.13088 · Cited by 58
Discovery of ultrapotent broadly neutralizing antibodies from SARS-CoV-2 elite neutralizers
Vanshylla, K., Fan, C., Wunsch, M., Poopalasingam, N., Meijers, M., Kreer, C., Kleipass, F., Ruchnewitz, D., Ercanoglu, M. S., Gruell, H., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.12.010 · Cited by 58
A SARS-CoV-2 variant elicits an antibody response with a shifted immunodominance hierarchy
Greaney, A. J., Starr, T. N., Eguia, R. T., Loes, A. N., Khan, K., Karim, F., Cele, S., Bowen, J. E., Logue, J. K., Corti, D., et al. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010248 · Cited by 58
Kaneko, N., Boucau, J., Kuo, H.-H., Perugino, C. A., Mahajan, V. S., Farmer, J. R., Liu, H., Diefenbach, T. J., Trocha, A. K., Lefteri, K., et al. (2022) · Clinical Immunology · doi:10.1016/j.clim.2022.108991 · Cited by 58
He, W., Musharrafieh, R. G., Song, G., Dueker, K., Tse, L. V., Martinez, D. R., Schäfer, A., Callaghan, S., Yong, P., Beutler, N., et al. (2022) · Nature Immunology · doi:10.1038/s41590-022-01222-1 · Cited by 58
Liu, H., Yuan, M., Huang, D., Bangaru, S., Zhao, F., Lee, C.-C. D., Peng, L., Barman, S., Zhu, X., Nemazee, D. A., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.04.005 · Cited by 58
Modeling how antibody responses may determine the efficacy of COVID-19 vaccines
Padmanabhan, P., Desikan, R., & Dixit, N. M. (2022) · Nature Computational Science · doi:10.1038/s43588-022-00198-0 · Cited by 57
Preclinical evaluation of a SARS-CoV-2 mRNA vaccine PTX-COVID19-B
Liu, J., Budylowski, P., Samson, R., Griffin, B. D., Babuadze, G., Rathod, B., Colwill, K., Abioye, J. A., Schwartz, J. A., Law, R., et al. (2022) · Science Advances · doi:10.1126/sciadv.abj9815 · Cited by 56
Comorbid illnesses are associated with altered adaptive immune responses to SARS-CoV-2
Yu, K. K. Q., Fischinger, S., Smith, M. T., Atyeo, C. G., Cizmeci, D., Wolf, C. R., Layton, E. D., Logue, J. K., Aguilar, M. S., Shuey, K. D., et al. (2021) · JCI Insight · doi:10.1172/jci.insight.146242 · Cited by 56
Cellular and Humoral Immune Responses in Covid-19 and Immunotherapeutic Approaches
Hasan, A., Al‐Ozairi, E., Albaqsumi, Z., Ahmad, R., & Al‐Mulla, F. (2021) · ImmunoTargets and Therapy · doi:10.2147/itt.s280706 · Cited by 56
Risk of SARS-CoV-2 reinfection after natural infection
Boyton, R. J., & Altmann, D. M. (2021) · The Lancet · doi:10.1016/s0140-6736(21)00662-0 · Cited by 56
Banach, B. B., Cerutti, G., Fahad, A. S., Shen, C., de Souza, M. O., Katsamba, P. S., Tsybovsky, Y., Wang, P., Nair, M. S., Huang, Y., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2021.109771 · Cited by 56
Dealing with a mucosal viral pandemic: lessons from COVID-19 vaccines
Mouro, V., & Fischer, A. (2022) · Mucosal Immunology · doi:10.1038/s41385-022-00517-8 · Cited by 56
Labarrere, C. A., & Kassab, G. S. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.979719 · Cited by 56
Fan, C., Cohen, A. A., Park, M., Hung, A. F.-H., Keeffe, J. R., Gnanapragasam, P. N. P., Lee, Y. E., Gao, H., Kakutani, L. M., Wu, Z., et al. (2022) · Immunity · doi:10.1016/j.immuni.2022.10.019 · Cited by 56
Lagoumintzis, G., Chasapis, C. T., Alexandris, N., Kouretas, D., Tzartos, S. J., Eliopoulos, E., Farsalinos, K. E., & Poulas, K. A. (2021) · Food and Chemical Toxicology · doi:10.1016/j.fct.2021.112009 · Cited by 55
Bradley, B. T., Bryan, A. B., Fink, S. L., Goecker, E. A., Roychoudhury, P., Huang, M.-L. W., Zhu, H., Chaudhary, A., Madarampalli, B., Lu, J., et al. (2021) · Journal of Clinical Microbiology · doi:10.1128/jcm.00989-21 · Cited by 55
Monoclonal Antibody Therapeutics for Infectious Diseases: Beyond Normal Human Immunoglobulin
Otsubo, R., & Yasui, T. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108233 · Cited by 55
Brown, B., Ojha, V., Fricke, I., Al-Sheboul, S. A., Imarogbe, C., Gravier, T., Green, M., Peterson, L., Koutsaroff, I. P., Demir, A. N., et al. (2023) · Vaccines · doi:10.3390/vaccines11020408 · Cited by 55
Klompus, S., Leviatan, S., Vogl, T. J., Mazor, R. D., Kalka, I. N., Stoler‐Barak, L., Nathan, N., Peres, A., Moss, L., Godneva, A., et al. (2021) · Science Immunology · doi:10.1126/sciimmunol.abe9950 · Cited by 55
COVID19 antibody detection using lateral flow assay tests in a cohort of convalescent plasma donors
Ragnesola, B., Jin, D. K., Lamb, C. C., Shaz, B. H., Hillyer, C. D., & Luchsinger, L. L. (2020) · BMC Research Notes · doi:10.1186/s13104-020-05212-0 · Cited by 54
Brüssow, H. (2020) · Environmental Microbiology · doi:10.1111/1462-2920.15302 · Cited by 54
Jain, S., Batra, H., Yadav, P., & Chand, S. (2020) · Vaccines · doi:10.3390/vaccines8040649 · Cited by 54
Weis, S., Scherag, A., Baier, M., Kiehntopf, M., Kamradt, T., Kolanos, S., Ankert, J., Glöckner, S., Makarewicz, O., Hagel, S., et al. (2020) · Clinical Microbiology and Infection · doi:10.1016/j.cmi.2020.11.009 · Cited by 54
Fédry, J., Hurdiss, D. L., Wang, C., Li, W., Obal, G., Drulyte, I., Du, W., Howes, S. C., van Kuppeveld, F. J. M., Förster, F. G., et al. (2021) · Science Advances · doi:10.1126/sciadv.abf5632 · Cited by 54
Markmann, A. J., Giallourou, N., Bhowmik, D. R., Hou, Y. J., Lerner, A., Martinez, D. R., Premkumar, L., Root, H. B., van Duin, D., Napravnik, S., et al. (2021) · mSphere · doi:10.1128/msphere.00275-21 · Cited by 54
Understanding the Secret of SARS-CoV-2 Variants of Concern/Interest and Immune Escape
Lou, F., Li, M., Pang, Z., Jiang, L., Guan, L., Tian, L., Hu, J., Fan, J., & Fan, H. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.744242 · Cited by 54
Human memory B cells show plasticity and adopt multiple fates upon recall response to SARS-CoV-2
Zurbuchen, Y., Michler, J., Taeschler, P., Adamo, S., Cervia, C., Raeber, M. E., Acar, İ. E., Nilsson, J., Warnatz, K., Soyka, M., et al. (2023) · Nature Immunology · doi:10.1038/s41590-023-01497-y · Cited by 54
Perspectives in Peptide-Based Vaccination Strategies for Syndrome Coronavirus 2 Pandemic
Natale, C. D., Manna, S. L., Benedictis, I. D., Brandi, P., & Marasco, D. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.578382 · Cited by 54
Mahajan, S., Kode, V., Bhojak, K., Coral, K., Lee, K. M., Manoharan, M., Ramesh, A., Sudheendra, H., Srivastava, A., Sathian, R., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-92521-4 · Cited by 54
Noval, M. G., Kaczmarek, M. E., Koide, A., Rodriguez-Rodriguez, B. A., Louie, P., Tada, T., Hattori, T., Panchenko, T., Romero, L. A., Teng, K. W., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-84913-3 · Cited by 53
Valdés-Balbín, Y., Santana-Mederos, D., Paquet, F., Fernández-Castillo, S., Climent, Y., Chiodo, F., Rodríguez, L., Ramírez, B. S., León, K., Hernández, T., et al. (2021) · ACS Central Science · doi:10.1021/acscentsci.1c00216 · Cited by 53
Surveilling and Tracking COVID-19 Patients Using a Portable Quantum Dot Smartphone Device
Zhang, Y., Malekjahani, A., Udugama, B. N., Kadhiresan, P., Chen, H., Osborne, M., Franz, M., Kucera, M., Plenderleith, S. W., Yip, L., et al. (2021) · Nano Letters · doi:10.1021/acs.nanolett.1c01280 · Cited by 53
Luo, S., Zhang, J., Kreutzberger, A. J. B., Eaton, A., Edwards, R. J., Jing, C., Dai, H., Sempowski, G. D., Cronin, K. D., Parks, R., et al. (2022) · Science Immunology · doi:10.1126/sciimmunol.add5446 · Cited by 53
Design of a highly thermotolerant, immunogenic SARS-CoV-2 spike fragment
Malladi, S. K., Singh, R., Pandey, S., Gayathri, S., Kanjo, K., Ahmed, S., Khan, M. S. A. A., Kalita, P., Girish, N., Upadhyaya, A., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.016284 · Cited by 52
Mor, M., Werbner, M., Alter, J., Safra, M., Chomsky, E., Lee, J. C., Hada-Neeman, S., Polonsky, K., Nowell, C. J., Clark, A. E., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009165 · Cited by 52
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) · Microbial Cell Factories · doi:10.1186/s12934-021-01576-5 · Cited by 52
Byazrova, M. G., Yusubalieva, G. M., Spiridonova, A. A., Efimov, G. A., Mazurov, D. V., Baranov, K. O., Baklaushev, V. P., & Filatov, A. V. (2021) · Clinical & Translational Immunology · doi:10.1002/cti2.1245 · Cited by 52
Montague, Z., Lv, H., Otwinowski, J., DeWitt, W. S., Isacchini, G., Yip, G. K., Ng, W. W., Tsang, O. T.-Y., Yuan, M., Liu, H., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109173 · Cited by 52
High-affinity, neutralizing antibodies to SARS-CoV-2 can be made without T follicular helper cells
Chen, J., Chow, R. D.-W., Song, E., Mao, T., Israelow, B., Kamath, K., Bozekowski, J. D., Haynes, W. A., Filler, R. B., Menasché, B. L., et al. (2022) · Science Immunology · doi:10.1126/sciimmunol.abl5652 · Cited by 52
Self-citationShiakolas, A. R., Kramer, K. J., Johnson, N. V., Wall, S. C., Suryadevara, N., Wrapp, D., Periasamy, S., Pilewski, K. A., Raju, N., Nargi, R. S., et al. (2022) · Nature Biotechnology · doi:10.1038/s41587-022-01232-2 · Cited by 52
COVID-19: systemic pathology and its implications for therapy
Shen, Q., Li, J., Zhang, Z., Guo, S., Wang, Q., An, X., & Chang, H. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.65911 · Cited by 51
Pushparaj, P., Nicoletto, A., Sheward, D. J., Das, H., Dopico, X. C., Vidakovics, L. P., Hanke, L., Chernyshev, M., Narang, S., Kim, S., et al. (2022) · Immunity · doi:10.1016/j.immuni.2022.12.005 · Cited by 51
Structural basis for a conserved neutralization epitope on the receptor-binding domain of SARS-CoV-2
Huang, K.-Y. A., Chen, X., Mohapatra, A., Nguyen, H. T. V., Schimanski, L. M., Tan, T. K., Rijal, P., Vester, S. K., Hills, R. A., Howarth, M. R., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-35949-8 · Cited by 51
Mosaic sarbecovirus nanoparticles elicit cross-reactive responses in pre-vaccinated animals
Cohen, A. A., Keeffe, J. R., Schiepers, A., Dross, S., Greaney, A. J., Rorick, A. V., Gao, H., Gnanapragasam, P. N. P., Fan, C., West, A. P., et al. (2024) · Cell · doi:10.1016/j.cell.2024.07.052 · Cited by 51
Self-citationGerhards, C., Thiaucourt, M., Kittel, M., Becker, C., Ast, V., Hetjens, M., Neumaier, M., & Haselmann, V. (2021) · International Journal of Infectious Diseases · doi:10.1016/j.ijid.2021.04.080 · Cited by 51
An antibody class with a common CDRH3 motif broadly neutralizes sarbecoviruses
Liu, L., Iketani, S., Guo, Y., Reddem, E. R., Casner, R. G., Nair, M. S., Yu, J., Chan, J. F., Wang, M., Cerutti, G., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abn6859 · Cited by 51
NeutrobodyPlex—monitoring SARS-CoV-2 neutralizing immune responses using nanobodies
Wagner, T. R., Kaiser, P. D., Gramlich, M., Ostertag, E., Ruétalo, N., Junker, D., Häring, J., Traenkle, B., Becker, M., Dulovic, A., et al. (2021) · EMBO Reports · doi:10.15252/embr.202052325 · Cited by 50
Grégoire, C., Layios, N., Lambermont, B. C., Lechanteur, C., Briquet, A., Bettonville, V., Baudoux, É., Thys, M., Dardenne, N., Misset, B., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.932360 · Cited by 50
Ju, B., Zhang, Q., Wang, Z., Aw, Z. Q., Chen, P., Zhou, B., Wang, R., Ge, X., Lv, Q., Cheng, L., et al. (2023) · Nature Immunology · doi:10.1038/s41590-023-01449-6 · Cited by 50
Self-citationDiagnostics and analysis of SARS-CoV-2: current status, recent advances, challenges and perspectives
Dong, T., Wang, M., Liu, J., Ma, P., Pang, S., Liu, W., & Liu, A. (2023) · Chemical Science · doi:10.1039/d2sc06665c · Cited by 50
COVID-19 in Immunosuppressed Children
Nicastro, E., Verdoni, L., Bettini, L. R., Zuin, G., Balduzzi, A., Montini, G., Biondi, A., & D’Antiga, L. (2021) · Frontiers in Pediatrics · doi:10.3389/fped.2021.629240 · Cited by 50
Bošnjak, B., Odak, I., Barros‐Martins, J., Sandrock, I., Hammerschmidt, S. I., Permanyer, M., Patzer, G. E., Georgiev, H., Jauregui, R. G., Tscherne, A., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.772240 · Cited by 50
Yang, L., Beek, M. V., Wang, Z., Muecksch, F., Canis, M., Hatziioannou, T., Bieniasz, P. D., Nussenzweig, M. C., & Chakraborty, A. K. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112256 · Cited by 50
Self-citationNeutralizing monoclonal antibodies for COVID-19 treatment and prevention
Jaworski, J. P. (2020) · Biomedical Journal · doi:10.1016/j.bj.2020.11.011 · Cited by 49
Immunologic memory to SARS-CoV-2 in convalescent COVID-19 patients at 1 year postinfection
Hou, H., Zhang, Y., Tang, G., Luo, Y., Liu, W., Cheng, C., Jiang, Y., Xiong, Z., Wu, S., Sun, Z., et al. (2021) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2021.09.008 · Cited by 49
Development of a rapid point-of-care test that measures neutralizing antibodies to SARS-CoV-2
Lake, D. F., Roeder, A. J., Kaleta, E. J., Jasbi, P., Pfeffer, K., Koelbela, C., Periasamy, S., Kuzmina, N. A., Bukreyev, A. A., Grys, T. E., et al. (2021) · Journal of Clinical Virology · doi:10.1016/j.jcv.2021.105024 · Cited by 49
Human type I IFN deficiency does not impair B cell response to SARS-CoV-2 mRNA vaccination
Sokal, A., Bastard, P., Chappert, P., Spaeth, G. B., Fourati, S., Vandenberghe, A., Lagouge-Roussey, P., Meyts, I., Gervais, A., Bouvier‐Alias, M., et al. (2022) · The Journal of Experimental Medicine · doi:10.1084/jem.20220258 · Cited by 49
Metadata
- Authors
- Robbiani, D. F., Gaebler, C., Muecksch, F., Lorenzi, J. C. C., Wang, Z., Cho, A., Agudelo, M., Barnes, C. O., Gazumyan, A., Finkin, S., Hägglöf, T., Oliveira, T. Y., Viant, C., Hurley, A., Hoffmann, H.-H., Millard, K. G., Kost, R. G., Cipolla, M., Gordon, K., Bianchini, F., Chen, S. T., Ramos, V., Patel, R., Dizon, J., Shimeliovich, I., Mendoza, P., Hartweger, H., Nogueira, L., Pack, M., Horowitz, J., Schmidt, F., Weisblum, Y., Michailidis, E., Ashbrook, A. W., Waltari, E., Pak, J. E., Huey-Tubman, K. E., Koranda, N., Hoffman, P. R., West, A. P., Rice, C. M., Hatziioannou, T., Bjorkman, P. J., Bieniasz, P. D., Caskey, M., & Nussenzweig, M. C.
- Affiliations
- Institute for Research in Biomedicine (CH)
- Rockefeller University (US)
- California Institute of Technology (US)
- Chan Zuckerberg Biohub San Francisco (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Robbiani, Davide F.
- Bieniasz, Paul D.
- Caskey, Marina
- Nussenzweig, Michel C.
- ORCID
- Robbiani, Davide F.
- Gaebler, Christian
- Muecksch, Frauke
- Lorenzi, Julio C. C.
- Wang, Zijun
- Cho, Alice
- Agudelo, Marianna
- Barnes, Christopher O.
- Gazumyan, Anna
- Finkin, Shlomo
- Hägglöf, Thomas
- Oliveira, Thiago Y.
- Viant, Charlotte
- Hurley, Arlene
- Hoffmann, Hans-Heinrich
- Millard, Katrina G.
- Kost, Rhonda G.
- Cipolla, Melissa
- Bianchini, Filippo
- Chen, Spencer T.
- Dizon, Juan
- Shimeliovich, Irina
- Mendoza, Pilar
- Hartweger, Harald
- Nogueira, Lilian
- Schmidt, Fabian
- Weisblum, Yiska
- Michailidis, Eleftherios
- Ashbrook, Alison W.
- Waltari, Eric
- Pak, John E.
- Koranda, Nicholas
- Hoffman, Pauline R.
- West, Anthony P.
- Rice, Charles M.
- Bjorkman, Pamela J.
- Bieniasz, Paul D.
- Caskey, Marina
- Nussenzweig, Michel C.
- Venue
- Nature
- Published
- 2020-06-18
- Volume
- 584
- Issue
- 7821
- Pages
- 437-442
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC7442695
- OpenAlex
- W3036386821
- Cited by
- 1,853
- References
- 47
- Citations by year
- 2026: 49 · 2025: 79 · 2024: 115 · 2023: 194 · 2022: 403 · 2021: 691 · 2020: 321
- FWCI
- 52.98
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- 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)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Howard Hughes Medical Institute (UL1TR001866)
- George Mason University
- California Institute of Technology
- Fast Grants
- National Institutes of Health (P01-AI138398-S1, AI150464, TR001866, UL1TR001866)
- Beckman Institute, California Institute of Technology
- National Institute of Allergy and Infectious Diseases (R01AI091707, R01AI078788, P50AI150464, U19AI111825, P01AI138938, R37AI064003, T32AI070084)
- National Center for Advancing Translational Sciences (TR001866)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Keywords
- SARS-CoV-2, COVID-19 pandemic, convalescent plasma, neutralizing antibodies, receptor binding domain, spike protein, antibody response, memory B cells, pseudovirus neutralization, vaccine design, antibody epitopes
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