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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
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Items 801–900 of 1,017
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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-citationElzein, F. E., Ibrahim, A. G. A., Alshahrani, F. S., Mahrous, M., Murshid, E., Aldhehyan, T., Almutiri, G., Altowairqi, M., Ahmed, M., Alsaeed, M., et al. (2021) · Journal of Infection and Public Health · doi:10.1016/j.jiph.2021.01.002 · Cited by 23
Santiago, L., Uranga-Murillo, I., Arias, M. A., González‐Ramírez, A. M., Macías‐León, J., Moreo, E., Redrado, S., García‐García, A., Taleb, V., Lira‐Navarrete, E., et al. (2021) · Biology · doi:10.3390/biology10030208 · Cited by 23
Yang, L., Tian, D., Han, J.-B., Fan, W., Zhang, Y., Li, Y., Sun, W., Wei, Y., Tian, X., Yu, D.-D., et al. (2021) · The Innovation · doi:10.1016/j.xinn.2021.100140 · Cited by 23
Uncovering a conserved vulnerability site in SARS‐CoV‐2 by a human antibody
Li, T., Cai, H., Zhao, Y., Li, Y., Lai, Y., Yao, H., Liu, L. D., Sun, Z., van Vlissingen, M. F., Kuiken, T., et al. (2021) · EMBO Molecular Medicine · doi:10.15252/emmm.202114544 · Cited by 23
Ishaq, S. E., Abdulqadir, S. Z., Khudhur, Z. O., Omar, S. A., Qadir, M. K., Awla, H. K., Rasul, M. F., Bapir, A. A., Zanichelli, A., Mansoor, M. K., et al. (2021) · Gene Reports · doi:10.1016/j.genrep.2021.101409 · Cited by 23
Morinaga, Y., Tani, H., Terasaki, Y., Nomura, S., Kawasuji, H., Shimada, T., Igarashi, E., Saga, Y., Yoshida, Y., Yasukochi, R., et al. (2021) · Microbiology Spectrum · doi:10.1128/spectrum.00560-21 · 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
Dick, D. W., Childs, L. M., Feng, Z., Li, J., Röst, G., Buckeridge, D. L., Ogden, N. H., & Heffernan, J. M. (2021) · Vaccines · doi:10.3390/vaccines10010017 · Cited by 23
Clark, N. M., Janaka, S. K., Hartman, W. R., Stramer, S. L., Goodhue, E., Weiss, J., Evans, D. T., & Connor, J. P. (2022) · PLoS ONE · doi:10.1371/journal.pone.0257930 · Cited by 23
Impact of SARS-CoV-2 vaccination on systemic immune responses in people living with HIV
Bessen, C., Plaza‐Sirvent, C., Simsek, A., Bhat, J., Marheinecke, C. S., Urlaub, D., Bonowitz, P., Buße, S., Schumann, S., Blanco, E. V., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1049070 · Cited by 23
Al-Sheboul, S. A., Brown, B., Shboul, Y., Fricke, I., Imarogbe, C., & Alzoubi, K. H. (2022) · Vaccines · doi:10.3390/vaccines11010051 · Cited by 23
Lee, D. B., Kim, H., Jeong, J. H., Jang, U. S., Jang, Y., Roh, S., Jeon, H., Kim, E. J., Han, S. Y., Maeng, J. Y., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2208425120 · Cited by 23
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Wu, D., Efimov, G. A., Васильевна, Б. А., Pierce, B. G., & Mariuzza, R. A. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.103035 · Cited by 23
Zhang, Y., Li, Q., Luo, L., Duan, C., Shen, J., & Wang, Z. (2023) · Biotechnology Advances · doi:10.1016/j.biotechadv.2023.108143 · Cited by 23
Self-citationJu, 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
Chen, Y., Mason, G. H., Scourfield, D. O., Greenshields‐Watson, A., Haigh, T. A., Sewell, A. K., Long, H. M., Gallimore, A., Rizkallah, P. J., MacLachlan, B. J., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112827 · Cited by 23
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
Prolonged viral replication in patients with hematologic malignancies hospitalized with COVID-19
García‐Vidal, C., Puerta‐Alcalde, P., Mateu, A., Cuesta, G., Meira, F. S., Lopera, C., Monzó, P., Bravo, M. S., Dueñas, G., Chumbita, M., et al. (2022) · Haematologica · doi:10.3324/haematol.2021.280407 · Cited by 23
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
Versatile, Multivalent Nanobody Cocktails Efficiently Neutralize SARS-CoV-2Preprint
Xiang, Y., Nambulli, S., Xiao, Z., Liu, H., Sang, Z., Duprex, W. P., Schneidman‐Duhovny, D., Zhang, C., & Shi, Y. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.24.264333 · Cited by 23
Olmedillas, E., Mann, C. J., Peng, W., Wang, Y.-T., Díaz-Avalos, R., Bedinger, D., Valentine, K. M., Shafee, N., Schendel, S. L., Yuan, M., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.06.441046 · Cited by 23
Комісаренко, С. В. (2020) · Visnik Nacional noi academii nauk Ukrai ni · doi:10.15407/visn2020.08.029 · Cited by 22
Development of SARS-CoV-2 vaccines: challenges, risks, and the way forward
Vashishtha, V. M., & Kumar, P. (2020) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2020.1845524 · Cited by 22
Feng, X., Yin, J., Zhang, J., Hu, Y., Ouyang, Y., Qiao, S., Zhao, H., Zhang, T., Li, X., Zhang, L., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.614436 · Cited by 22
Liang, Z., Peng, T., Jiao, X., Zhao, Y. C., Xie, J., Jiang, Y., Meng, B., Fang, X. Z., Yu, X., & Dai, X. (2022) · Biosensors · doi:10.3390/bios12020103 · Cited by 22
Long, Y., Sun, J., Song, T., Liu, T., Tang, F., Zhang, X., Ding, L., Miao, Y., Zhu, W., Pan, X., et al. (2022) · Cell Discovery · doi:10.1038/s41421-021-00370-2 · Cited by 22
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-citationKhatamzas, E., Antwerpen, M. H., Rehn, A., Graf, A., Hellmuth, J. C., Hollaus, A., Mohr, A., Gaitzsch, E., Weiglein, T., Georgi, E., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32772-5 · Cited by 22
Mechanistic basis for potent neutralization of Sin Nombre hantavirus by a human monoclonal antibody
Stass, R., Engdahl, T. B., Chapman, N. S., Wolters, R. M., Handal, L. S., Diaz, S. M., Crowe, J. E., & Bowden, T. A. (2023) · Nature Microbiology · doi:10.1038/s41564-023-01413-y · Cited by 22
Yuen, R. R., Steiner, D., Pihl, R. M. F., Chavez, E. C., Olson, A., Smith-Mahoney, E. L., Baird, L. A., Korkmaz, F. T., Urick, P., Sagar, M., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.614676 · Cited by 22
Mallano, A., Ascione, A., & Flego, M. (2021) · International Reviews of Immunology · doi:10.1080/08830185.2021.1929205 · Cited by 22
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
SARS-CoV-2 hijacks neutralizing dimeric IgA for nasal infection and injury in Syrian hamsters 1
Zhou, B., Zhou, R., Chan, J. F., Zeng, J., Zhang, Q., Yuan, S., Liu, L., Robinot, R., Shan, S., Liu, N., et al. (2023) · Emerging Microbes & Infections · doi:10.1080/22221751.2023.2245921 · Cited by 22
Self-citationA 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
Drug discovery and development targeting the life cycle of SARS-CoV-2
Su, H., Xu, Y., & Jiang, H. (2021) · Fundamental Research · doi:10.1016/j.fmre.2021.01.013 · Cited by 21
Wendel, S., Fontão‐Wendel, R., Fachini, R. M., Candelaria, G. D. T. P., Scuracchio, P., Achkar, R., Brito, M., Reis, L. F. L., Camargo, A. A., Amano, M. T., et al. (2021) · Transfusion · doi:10.1111/trf.16323 · Cited by 21
Animal Models of COVID-19 II. Comparative Immunology
Veenhuis, R. T., & Zeiss, C. J. (2021) · ILAR Journal · doi:10.1093/ilar/ilab010 · Cited by 21
Kyei-Barffour, I., Akwetey, S. A., Aninagyei, E., Ghartey‐Kwansah, G., & Acheampong, D. O. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.112282 · Cited by 21
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
Immune features of COVID-19 convalescent individuals revealed by a single-cell RNA sequencing
Zhao, P., Zou, J., Zhou, F., Zhu, Y., Song, Q., Yu, D., & Li, X. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.108767 · Cited by 21
Humoral Immunogenicity of the mRNA-1273 Vaccine in the Phase 3 Coronavirus Efficacy (COVE) Trial
Sahly, H. M. E., Baden, L. R., Essink, B. J., Montefiori, D. C., McDermont, A., Rupp, R. E., Lewis, M., Swaminathan, S., Griffin, C., Fragoso, V. G., et al. (2022) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiac188 · Cited by 21
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SARS-CoV-2 infection and immune responses
Harne, R., Williams, B., Abdelaal, H. F. M., Baldwin, S. L., & Coler, R. N. (2023) · AIMS Microbiology · doi:10.3934/microbiol.2023015 · Cited by 21
Pan-sarbecovirus prophylaxis with human anti-ACE2 monoclonal antibodies
Zhang, F., Jenkins, J., de Carvalho, R. A., Nakandakari-Higa, S., Chen, T., Abernathy, M. E., Baharani, V. A., Nyakatura, E. K., Andrew, D. P., Lebedeva, I. V., et al. (2023) · Nature Microbiology · doi:10.1038/s41564-023-01389-9 · Cited by 21
Self-citationKim, J. S., Sun, Y., Balte, P., Cushman, M., Boyle, R., Tracy, R. P., Styer, L. M., Bell, T. D., Anderson, M. R., Allen, N. B., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45468-9 · Cited by 21
Rubio, A. A., Baharani, V. A., Dadonaite, B., Parada, M., Abernathy, M. E., Wang, Z., Lee, Y. E., Eso, M. R., Phung, J. L., Ramos, I., et al. (2025) · Science Translational Medicine · doi:10.1126/scitranslmed.adq5720 · Cited by 21
Self-citationRapid and accurate agglutination-based testing for SARS-CoV-2 antibodies
Esmail, S., Knauer, M. J., Abdoh, H., Voss, C., Chin-Yee, B. H., Stogios, P. J., Seitova, A., Hutchinson, A., Yusifov, F., Skarina, T., et al. (2021) · Cell Reports Methods · doi:10.1016/j.crmeth.2021.100011 · Cited by 21
Paschold, L., Klee, B., Gottschick, C., Willscher, E., Diexer, S., Schultheiß, C., Simnica, D., Sedding, D., Girndt, M., Gekle, M., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.876306 · Cited by 21
Of Cross-immunity, Herd Immunity and Country-specific Plans: Experiences from COVID-19 in India
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Li, X., Pan, Y., Yin, Q., Wang, Z., Shan, S., Zhang, L., Yu, J., Qu, Y., Sun, L., Gui, F., et al. (2022) · Cell Discovery · doi:10.1038/s41421-022-00449-4 · Cited by 20
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Freeman, E. E., McMahon, D. E., Hruza, G. J., Lipoff, J. B., French, L. E., Fox, L. P., & Fassett, M. S. (2020) · Journal of the American Academy of Dermatology · doi:10.1016/j.jaad.2020.09.007 · Cited by 20
Anand, S. P., Prévost, J., Richard, J., Perreault, J., Tremblay, T., Drouin, M., Fournier, M., Lewin, A., Bazin, R., & Finzi, A. (2021) · Transfusion · doi:10.1111/trf.16318 · Cited by 20
Chen, Y., Zhu, L., Huang, W., Tong, X., Wu, H., Tao, Y., Tong, B., Huang, H., Chen, J., Zhao, X., et al. (2021) · Emerging Microbes & Infections · doi:10.1080/22221751.2021.1942227 · Cited by 20
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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-citationA self-pressure-driven blood plasma-separation device for point-of-care diagnostics
Kim, H., Park, H., Chung, D. R., Kim, T.-K., Park, E., & Kang, M. (2022) · Talanta · doi:10.1016/j.talanta.2022.123562 · Cited by 20
Shrivastava, S., Palkar, S. H., Shah, J. N., Rane, P. S., Lalwani, S. K., Mishra, A. C., & Arankalle, V. A. (2021) · American Journal of Tropical Medicine and Hygiene · doi:10.4269/ajtmh.21-0014 · Cited by 20
Scaglione, A., Opp, S., Hurtado, A. M., Lin, Z., Pampeno, C., Noval, M. G., Thannickal, S. A., Stapleford, K. A., & Meruelo, D. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.719077 · Cited by 20
Ishida, E., Corrigan, D. T., Malonis, R. J., Hofmann, D., Chen, T., Amin, A. G., Chatterjee, D., Joe, M., Lowary, T. L., Lai, J. R., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02714-w · Cited by 20
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Qiang, M., Ma, P., Li, Y., Liu, H., Harding, A. C., Min, C., Wang, F., Liu, L., Yuan, M., Ji, Q., et al. (2021) · Advanced Science · doi:10.1002/advs.202102181 · Cited by 20
Guo, C. M., Peng, Y., Lin, L., Pan, X., Fang, M., Zhao, Y., Bao, K., Li, R., Han, J.-B., Chen, J., et al. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100448 · Cited by 20
Vanhove, B., Marot, S., So, R. T. Y., Gaborit, B. J., Evanno, G., Malet, I., Lafrogne, G., Mevel, E., Ciron, C., Royer, P., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.761250 · Cited by 20
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Immune response induced by novel coronavirus infection
Sun, Y., Zou, Y., Wang, H., Cui, G., Yu, Z., & Ren, Z. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.988604 · Cited by 20
Jeong, W.-J., Bu, J., Mickel, P., Han, Y., Rawding, P. A., Wang, J., Kang, H., Hong, H., Král, P., & Hong, S. (2022) · Biomacromolecules · doi:10.1021/acs.biomac.2c01018 · Cited by 20
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Hattori, T., Koide, A., Noval, M. G., Panchenko, T., Romero, L. A., Teng, K. W., Tada, T., Landau, N. R., Stapleford, K. A., & Koide, S. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.166748 · Cited by 20
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Abe, K. T., Li, Z., Samson, R., Samavarchi-Tehrani, P., Valcourt, E. J., Wood, H., Budylowski, P., Dupuis, A. P., Girardin, R. C., Rathod, B., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.10.197913 · Cited by 20
Vaisman‐Mentesh, A., Dror, Y., Tur‐Kaspa, R., Markovitch, D., Kournos, T., Dicker, D., & Wine, Y. (2020) · medRxiv · doi:10.1101/2020.08.23.20179796 · Cited by 20
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Wilson, P. C., Stamper, C. T., Dugan, H. L., Li, L., Asby, N. W., Halfmann, P., Guthmiller, J. J., Zheng, N., Huang, M., Stovicek, O., et al. (2020) · Research Square · doi:10.21203/rs.3.rs-80476/v1 · Cited by 20
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Mishra, P. K., Bruiners, N., Ukey, R., Datta, P., Onyuka, A., Handler, D., Hussain, S., Honnen, W. J., Singh, S., Guerrini, V., et al. (2021) · medRxiv · doi:10.1101/2021.04.11.21255153 · Cited by 20
Luan, B., & Huynh, T. (2020) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.0c02706 · Cited by 19
Kombe, A. J. K., Zahid, A., Mohammed, A., Shi, R., & Jin, T. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.670815 · Cited by 19
Ma, T., Ryu, H., McGregor, M. M., Babcock, B. R., Neidleman, J. A., Xie, G., George, A. F., Frouard, J., Murray, V., Gill, G., et al. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2100465 · Cited by 19
Murugavelu, P., Perween, R., Shrivastava, T., Singh, V., Parray, H. A., Singh, S., Chiranjivi, A. K., Thiruvengadam, R., Singh, S., Yadav, N., et al. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.108020 · Cited by 19
Efrati, S., Catalogna, M., Hamad, R. A., Hadanny, A., Bar‐Chaim, A., Benveniste‐Levkovitz, P., & Levtzion‐Korach, O. (2021) · Scientific Reports · doi:10.1038/s41598-021-96129-6 · Cited by 19
Sjöwall, J., Azharuddin, M., Frodlund, M., Zhang, Y., Sandner, L., Dahle, C., Hinkula, J., & Sjöwall, C. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.724047 · Cited by 19
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Zuiani, A., & Wesemann, D. R. (2021) · Clinics in Laboratory Medicine · doi:10.1016/j.cll.2021.10.004 · Cited by 19
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Zou, J., Li, L., Zheng, P., Liang, W., Hu, S., Zhou, S., Wang, Y., Zhao, J., Yuan, D., Liu, L., et al. (2022) · Journal of Clinical Investigation · doi:10.1172/jci154987 · Cited by 19
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Wang, Z., Muecksch, F., Raspe, R., Johannsen, F., Turroja, M., Canis, M., ElTanbouly, M. A., Santos, G. S. S., Johnson, B., Baharani, V. A., et al. (2023) · The Journal of Experimental Medicine · doi:10.1084/jem.20230668 · Cited by 19
Self-citationHederman, A. P., Natarajan, H., Heyndríckx, L., Ariën, K. K., Wiener, J. A., Wright, P. F., Bloch, E. M., Tobian, A. A. R., Redd, A. D., Blankson, J. N., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40960-0 · Cited by 19
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Prabhakaran, M. S., Matassoli, F. L., Leggat, D. J., Hoover, A., Srikanth, A., Wu, W., Henry, A. R., Wang, J. P., Lin, B. C., Teng, I., et al. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.add5960 · Cited by 19
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Romero, J. A. A., Chingaté-López, S. M., Camacho, B., Alméciga-Díaz, C. J., & Ramirez-Segura, C. A. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e26423 · Cited by 19
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Siraj, A. S., Worku, A., Berhane, K. T., Aregawi, M. W., Eshetu, M. K., Mirkuzie, A. H., Berhane, Y., & Siraj, D. S. (2020) · BMJ Global Health · doi:10.1136/bmjgh-2020-003055 · Cited by 19
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Jiang, J.-C., & Zhang, Y. (2020) · Biochemical Society Transactions · doi:10.1042/bst20200744 · Cited by 19
Rompay, K. K. A. V., Olstad, K. J., Sammak, R. L., Dutra, J., Watanabe, J., Usachenko, J. L., Immareddy, R., Verma, A., Lakshmanappa, Y. S., Schmidt, B., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009688 · Cited by 19
Self-citationMakdasi, E., Zvi, A., Alcalay, R., Noy-Porat, T., Peretz, E., Mechaly, A., Levy, Y., Epstein, E., Chitlaru, T., Tennenhouse, A., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109679 · Cited by 19
Vo, H. T. M., Maestri, A., Auerswald, H., Sorn, S., Lay, S., Seng, H., Sann, S., Ya, N., Pean, P., Dussart, P., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.817905 · Cited by 19
Choteau, M., Scohy, A., Messe, S., Luyckx, M., Dechamps, M., Montiel, V., Yombi, J. C., Gruson, D., Limaye, N., Michiels, T., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-06038-5 · Cited by 19
SARS-CoV-2 and Coronavirus Disease Mitigation: Treatment Options, Vaccinations and Variants
Khamees, A., Bani-Issa, J., Zoubi, M. S. A., Qasem, T., Alarjah, M. I. A., Alawadin, S. A., Al‐Shami, K., Hussein, F. H., Hussein, E. I., Bashayreh, I. H., et al. (2022) · Pathogens · doi:10.3390/pathogens11020275 · Cited by 19
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Shi, Z., Li, X., Wang, L., Sun, Z., Zhang, H., Chen, X., Cui, Q., Qiao, H., Lan, Z., Zhang, X., et al. (2022) · Structure · doi:10.1016/j.str.2022.02.011 · Cited by 19
Mosaic nanoparticles elicit cross-reactive immune responses to zoonotic coronaviruses in micePreprint
Cohen, A. A., Gnanapragasam, P. N. P., Lee, Y. E., Hoffman, P. R., Ou, S., Kakutani, L. M., Keeffe, J. R., Wu, H.-J., Howarth, M. R., West, A. P., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.17.387092 · Cited by 19
Self-citationDownes, K. J., Danziger‐Isakov, L. A., Cousino, M. K., Green, M., Michaels, M. G., Muller, W. J., Orscheln, R. C., Sharma, T. S., Statler, V. A., Wattier, R. L., et al. (2020) · Journal of the Pediatric Infectious Diseases Society · doi:10.1093/jpids/piaa095 · Cited by 18
Uraki, R., Imai, M., Ito, M., Shime, H., Odanaka, M., Okuda, M., Kawaoka, Y., & Yamazaki, S. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1010085 · Cited by 18
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Ding, S., Adam, D., Beaudoin-Bussières, G., Tauzin, A., Gong, S. Y., Gasser, R., Laumaea, A., Anand, S. P., Privé, A., Bourassa, C., et al. (2021) · Viruses · doi:10.3390/v14010005 · Cited by 18
Pérez‐Olmeda, M., Saugar, J. M., Fernández-García, A., Pérez‐Gómez, B., Pollán, M., Avellón, A., Pastor‐Barriuso, R., de Larrea, N. F., Martín, M., Cruz, I., et al. (2022) · Journal of Clinical Virology · doi:10.1016/j.jcv.2022.105130 · Cited by 18
Ozawa, T., Tani, H., Anraku, Y., Kita, S., Igarashi, E., Saga, Y., Inasaki, N., Kawasuji, H., Yamada, H., Sasaki, S., et al. (2022) · mAbs · doi:10.1080/19420862.2022.2072455 · Cited by 18
Breakthrough COVID-19 Infections in the US: Implications for Prolonging the Pandemic
Alcendor, D. J., Matthews-Juarez, P., Smoot, D. T., Hildreth, J. E. K., Lamar, K. D., Tabatabai, M., Wilus, D. M., & Juárez, P. D. (2022) · Vaccines · doi:10.3390/vaccines10050755 · Cited by 18
Depression, aging, and immunity: implications for COVID-19 vaccine immunogenicity
Ford, B. N., & Savitz, J. B. (2022) · Immunity & Ageing · doi:10.1186/s12979-022-00288-7 · Cited by 18
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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