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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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Items 301–400 of 1,017
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da Silva, S. J. R., da Silva, C. T. A., Guarines, K. M., Mendes, R. P. G., Pardee, K., Kohl, A., & Pena, L. (2020) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00274 · Cited by 95
Guo, Y., Huang, L., Zhang, G., Yao, Y., Zhou, H., Shěn, S., Shen, B., Li, B., Li, X., Zhang, Q., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22926-2 · Cited by 95
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West, R., Kobokovich, A. L., Connell, N. D., & Grönvall, G. K. (2020) · Trends in Microbiology · doi:10.1016/j.tim.2020.11.002 · Cited by 94
Bertoglio, F., Meier, D., Langreder, N., Steinke, S., Rand, U., Simonelli, L., Heine, P. A., Ballmann, R., Schneider, K.-T., Roth, K. D. R., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21609-2 · Cited by 94
Baral, P., Bhattarai, N., Hossen, M. L., Stebliankin, V., Gerstman, B. S., Narasimhan, G., & Chapagain, P. P. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.08.036 · Cited by 94
Amodio, D., Ruggiero, A., Sgrulletti, M., Pighi, C., Cotugno, N., Medri, C., Rocchi, F., Colagrossi, L., Russo, C., Zaffina, S., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.727850 · Cited by 94
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Hardenbrook, N. J., & Zhang, P. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.11.011 · Cited by 93
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Lakshmanappa, Y. S., Elizaldi, S. R., Roh, J. W., Schmidt, B., Carroll, T. D., Weaver, K. D., Smith, J. C., Verma, A., Deere, J. D., Dutra, J., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20642-x · Cited by 92
Durable SARS-CoV-2 B cell immunity after mild or severe disease
Ogega, C. O., Skinner, N., Blair, P. W., Park, H.-S., Littlefield, K. E., Ganesan, A., Dhakal, S., Ladiwala, P., Antar, A. A. R., Ray, S. C., et al. (2021) · Journal of Clinical Investigation · doi:10.1172/jci145516 · Cited by 91
Spike Glycoprotein and Host Cell Determinants of SARS-CoV-2 Entry and Cytopathic Effects
Nguyen, H. T., Zhang, S., Wang, Q., Anang, S., Wang, J., Ding, H., Kappes, J. C., & Sodroski, J. (2020) · Journal of Virology · doi:10.1128/jvi.02304-20 · Cited by 90
Challenges and opportunities for antiviral monoclonal antibodies as COVID-19 therapy
Cruz-Teran, C. A., Tiruthani, K., McSweeney, M. D., Ma, A. L., Pickles, R. J., & Lai, S. K. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.12.004 · Cited by 90
Immunology, immunopathogenesis and immunotherapeutics of COVID-19; an overview
Khosroshahi, L. M., Rokni, M., Mokhtari, T., & Noorbakhsh, F. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2020.107364 · Cited by 90
SARS-CoV-2 vaccines in advanced clinical trials: Where do we stand?
Chakraborty, S., Mallajosyula, V. V. A., Tato, C. M., Tan, G. S., & Wang, T. T. (2021) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2021.01.014 · Cited by 90
Grzelak, L., Velay, A., Madec, Y., Gallais, F., Staropoli, I., Schmidt‐Mutter, C., Wendling, M.-J., Meyer, N., Planchais, C., Rey, D., et al. (2021) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiab127 · Cited by 90
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Scheid, J. F., Barnes, C. O., Eraslan, B., Hudak, A., Keeffe, J. R., Cosimi, L. A., Brown, E., Muecksch, F., Weisblum, Y., Zhang, S., et al. (2021) · Cell · doi:10.1016/j.cell.2021.04.032 · Cited by 90
Self-citationAsymptomatic and symptomatic SARS-CoV-2 infections elicit polyfunctional antibodies
Dufloo, J., Grzelak, L., Staropoli, I., Madec, Y., Tondeur, L., Anna, F., Pelleau, S., Wiedemann, A., Planchais, C., Buchrieser, J., et al. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100275 · Cited by 89
Bianchini, F., Crivelli, V., Abernathy, M. E., Guerra, C., Palus, M., Muri, J., Marcotte, H., Piralla, A., Pedotti, M., Gasparo, R. D., et al. (2023) · Science Immunology · doi:10.1126/sciimmunol.ade0958 · Cited by 88
Self-citationGermline-encoded amino acid–binding motifs drive immunodominant public antibody responses
Shrock, E. L., Timms, R. T., Kula, T., Mena, E. L., West, A. P., Guo, R., Lee, I., Cohen, A. A., McKay, L. G. A., Bi, C., et al. (2023) · Science · doi:10.1126/science.adc9498 · Cited by 88
Self-citationCOVID-19 Vaccines: “Warp Speed” Needs Mind Melds, Not Warped Minds
Moore, J. P., & Klasse, P. J. (2020) · Journal of Virology · doi:10.1128/jvi.01083-20 · Cited by 87
Zeng, C., Evans, J. P., Pearson, R., Qu, P., Zheng, Y.-M., Robinson, R., Hall‐Stoodley, L., Yount, J. S., Pannu, S. R., Mallampalli, R. K., et al. (2020) · JCI Insight · doi:10.1172/jci.insight.143213 · Cited by 87
Folgueira, M. D., Luczkowiak, J., Lasala, F., Pérez‐Rivilla, A., & Delgado, R. B. (2021) · Clinical Microbiology and Infection · doi:10.1016/j.cmi.2021.02.014 · Cited by 87
VanBlargan, L. A., Adams, L. J., Liu, Z., Chen, R. E., Gilchuk, P., Raju, S., Smith, B. K., Zhao, H., Case, J. B., Winkler, E. S., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.08.016 · Cited by 87
An Effective COVID-19 Vaccine Needs to Engage T Cells
Sauer, K., & Harris, T. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.581807 · Cited by 85
An Update on Antiviral Therapy Against SARS-CoV-2: How Far Have We Come?
Indari, O., Jakhmola, S., Manivannan, E., & Jha, H. C. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.632677 · Cited by 85
von Rhein, C., Scholz, T., Henß, L., Kronstein‐Wiedemann, R., Schwarz, T., Rodionov, R. N., Corman, V. M., Tonn, T., & Schnierle, B. S. (2020) · Journal of Virological Methods · doi:10.1016/j.jviromet.2020.114031 · Cited by 84
Advances in the design and development of SARS-CoV-2 vaccines
Peng, X., Cheng, J., Gong, H., Yuan, M.-D., Zhao, X., Li, Z., & Wei, D. (2021) · Military Medical Research · doi:10.1186/s40779-021-00360-1 · Cited by 84
Halawa, S., Pullamsetti, S. S., Bangham, C. R. M., Stenmark, K. R., Dorfmüller, P., Frid, M. G., BUTROUS, G. S., Morrell, N. W., Pérez, V. D. J., Stuart, D. I., et al. (2021) · Nature Reviews Cardiology · doi:10.1038/s41569-021-00640-2 · Cited by 84
Varghese, P. M., Tsolaki, A. G., Yasmin, H., Shastri, A., Ferluga, J., Vatish, M., Madan, T., & Kishore, U. (2020) · Immunobiology · doi:10.1016/j.imbio.2020.152008 · Cited by 83
Structural Basis of SARS-CoV-2 and SARS-CoV Antibody Interactions
Gavor, E., Choong, Y. K., Er, S. Y., Sivaraman, H., & Sivaraman, J. (2020) · Trends in Immunology · doi:10.1016/j.it.2020.09.004 · Cited by 83
ReScan, a Multiplex Diagnostic Pipeline, Pans Human Sera for SARS-CoV-2 Antigens
Zamecnik, C. R., Rajan, J. V., Yamauchi, K. A., Mann, S. A., Loudermilk, R. P., Sowa, G. M., Zorn, K. C., Alvarenga, B. D., Gaebler, C., Caskey, M. F., et al. (2020) · Cell Reports Medicine · doi:10.1016/j.xcrm.2020.100123 · Cited by 83
Self-citationBecker, M., Strengert, M., Junker, D., Kaiser, P. D., Kerrinnes, T., Traenkle, B., Dinter, H., Häring, J., Ghozzi, S., Zeck, A., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-20973-3 · Cited by 83
Augusto, G. S., Mohsen, M. O., Zinkhan, S., Liu, X., Vogel, M., & Bachmann, M. F. (2021) · Allergy · doi:10.1111/all.15065 · Cited by 83
Discrete SARS-CoV-2 antibody titers track with functional humoral stability
Bartsch, Y. C., Fischinger, S., Siddiqui, S. M., Chen, Z., Yu, J., Gebre, M., Atyeo, C., Gorman, M. J., Zhu, A. L., Kang, J., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21336-8 · Cited by 82
Kim, S. I., Noh, J., Kim, S., Choi, Y. G., Yoo, D. K., Lee, Y., Lee, H., Jung, J., Kang, C. K., Song, K., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abd6990 · Cited by 82
Proactive vaccination using multiviral Quartet Nanocages to elicit broad anti-coronavirus responses
Hills, R. A., Tan, T. K., Cohen, A. A., Keeffe, J. R., Keeble, A. H., Gnanapragasam, P. N. P., Storm, K. N., Rorick, A. V., West, A. P., Hill, M. L., et al. (2024) · Nature Nanotechnology · doi:10.1038/s41565-024-01655-9 · Cited by 82
Self-citationLoretelli, C., Abdelsalam, A., D’Addio, F., Nasr, M. B., Assi, E., Usuelli, V., Maestroni, A., Seelam, A. J., Ippolito, E., Maggio, S. D., et al. (2021) · JCI Insight · doi:10.1172/jci.insight.146701 · Cited by 81
Robust and durable serological response following pediatric SARS-CoV-2 infection
Renk, H., Dulovic, A., Seidel, A., Becker, M., Fabricius, D., Zernickel, M., Junker, D., Groß, R. M., Müller, J. A., Hilger, A., et al. (2022) · Nature Communications · doi:10.1038/s41467-021-27595-9 · Cited by 81
Replication and single-cycle delivery of SARS-CoV-2 replicons
Ricardo-Lax, I., Luna, J. M., Thao, T. T. N., Pen, J. L., Yu, Y., Hoffmann, H.-H., Schneider, W. M., Razooky, B. S., Fernández-Martínez, J., Schmidt, F., et al. (2021) · Science · doi:10.1126/science.abj8430 · Cited by 80
Self-citationCOVID-19 vaccines: neutralizing antibodies and the alum advantage
Hotez, P. J., Corry, D. B., Strych, U., & Bottazzi, M. E. (2020) · Nature reviews. Immunology · doi:10.1038/s41577-020-0358-6 · Cited by 79
Jones, J., Faruqi, A. J., Sullivan, J., Calabrese, C. M., & Calabrese, L. H. (2021) · Pathogens and Immunity · doi:10.20411/pai.v6i1.435 · Cited by 79
Tan, H., Juno, J. A., Lee, W. S., Barber-Axthelm, I. M., Kelly, H. G., Wragg, K. M., Esterbauer, R., Amarasena, T. H., Mordant, F. L., Subbarao, K., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21665-8 · Cited by 79
Primary, Recall, and Decay Kinetics of SARS-CoV-2 Vaccine Antibody Responses
Ibarrondo, F. J., Hofmann, C., Fulcher, J. A., Goodman‐Meza, D., Mu, W., Hausner, M. A., Ali, A., Balamurugan, A., Taus, E., Elliott, J. E., et al. (2021) · ACS Nano · doi:10.1021/acsnano.1c03972 · Cited by 79
Tackling COVID-19 with neutralizing monoclonal antibodies
Corti, D., Purcell, L. A., Snell, G., & Veesler, D. (2021) · Cell · doi:10.1016/j.cell.2021.07.027 · Cited by 78
“S2M11 was not further developed, while C144 mAb is in early clinical development by Bristol Myers Squibb (phase 1, NCT04700163) in combination with another RBM mAb named C135 (both developed with LS mutations in Fc for half-life extension) (Robbiani et al., 2020; Weisblum et al., 2020).”
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Fang, F. C., Benson, C. A., del Río, C., Edwards, K. M., Fowler, V. G., Fredricks, D. N., Limaye, A. P., Murray, B. E., Naggie, S., Pappas, P. G., et al. (2020) · Clinical Infectious Diseases · doi:10.1093/cid/ciaa1654 · Cited by 78
Self-citationVogelzang, E. H., Loeff, F. C., Derksen, N. I. L., Kruithof, S., Heer, P. O., van Mierlo, G. J., Linty, F., Mok, J. Y., van Esch, W. J. E., de Bruin, S., et al. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.2000767 · Cited by 78
Poston, D., Weisblum, Y., Wise, H. M., Templeton, K. E., Jenks, S. J., Hatziioannou, T., & Bieniasz, P. D. (2020) · Clinical Infectious Diseases · doi:10.1093/cid/ciaa1803 · Cited by 78
Self-citationSelhorst, P., van Ierssel, S. H., Michiels, J., Mariën, J., Bartholomeeusen, K., Dirinck, E. L., Vandamme, S., Jansens, H., & Ariën, K. K. (2020) · Clinical Infectious Diseases · doi:10.1093/cid/ciaa1850 · Cited by 78
Zhu, J., Ananthaswamy, N., Jain, S., Batra, H., Tang, W.-C., Lewry, D. A., Richards, M. L., David, S. A., Kilgore, P. B., Sha, J., et al. (2021) · Science Advances · doi:10.1126/sciadv.abh1547 · Cited by 78
Broadly-Neutralizing Antibodies Against Emerging SARS-CoV-2 Variants
Shrestha, L. B., Tedla, N. T., & Bull, R. A. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.752003 · Cited by 78
SARS-CoV-2 uses CD4 to infect T helper lymphocytes
Brunetti, N. S., Davanzo, G. G., de Moraes, D., Ferrari, A., de Souza, G. F., Muraro, S. P., Knittel, T. L., Boldrini, V. D. O., Monteiro, L. D. B., Virgílio-da-Silva, J. V., et al. (2023) · eLife · doi:10.7554/elife.84790 · Cited by 78
Byrnes, J. R., Zhou, X. X., Lui, I., Elledge, S. K., Glasgow, J. E., Lim, S. A., Loudermilk, R. P., Chiu, C. Y., Wang, T. T., Wilson, M. R., et al. (2020) · mSphere · doi:10.1128/msphere.00802-20 · Cited by 77
Mazzini, L., Martinuzzi, D., Hyseni, I., Benincasa, L., Molesti, E., Casa, E., Lapini, G., Piu, P., Trombetta, C. M., Marchi, S., et al. (2020) · Journal of Immunological Methods · doi:10.1016/j.jim.2020.112937 · Cited by 77
Jiang, X.-L., Wang, G.-L., Zhao, X.-N., Yan, F.-H., Lin, Y., Kou, Z.-Q., Ji, S.-X., Zhang, X.-L., Li, C.-B., Duan, L., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21155-x · Cited by 77
Early cross-coronavirus reactive signatures of humoral immunity against COVID-19
Kapłonek, P., Wang, C., Bartsch, Y. C., Fischinger, S., Gorman, M. J., Bowman, K. A., Kang, J., Dayal, D., Martin, P., Nowak, R. P., et al. (2021) · Science Immunology · doi:10.1126/sciimmunol.abj2901 · Cited by 77
Structural basis for continued antibody evasion by the SARS-CoV-2 receptor binding domain
Smith, K. N., Clark, S. A., Shankar, S., Pan, J., Clark, L. E., Yang, P., Coscia, A., McKay, L. G. A., Varnum, H., Brusic, V., et al. (2022) · Science · doi:10.1126/science.abl6251 · Cited by 77
SARS-CoV-2 Omicron sublineages exhibit distinct antibody escape patterns
Gruell, H., Vanshylla, K., Korenkov, M., Tober‐Lau, P., Zehner, M., Münn, F., Janicki, H., Augustin, M., Schommers, P., Sander, L. E., et al. (2022) · Cell Host & Microbe · doi:10.1016/j.chom.2022.07.002 · Cited by 77
Influenza Vaccination to Reduce Cardiovascular Morbidity and Mortality in Patients With COVID-19
Behrouzi, B., Campoverde, M. V. A., Liang, K., Talbot, H. K., Bogoch, I. I., McGeer, A., Fröbert, O., Loeb, M. B., Vardeny, O., Solomon, S. D., et al. (2020) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2020.08.028 · Cited by 76
SARS-CoV-2 elicits robust adaptive immune responses regardless of disease severity
Nielsen, S. S. F., Vibholm, L. K., Monrad, I., Olesen, R., Frattari, G. S., Pahus, M. H., Højen, J. F., Gunst, J. D., Erikstrup, C., Holleufer, A., et al. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103410 · Cited by 76
Patel, A. R., Walters, J. N., Reuschel, E. L., Schultheis, K., Parzych, E. M., Gary, E. N., Maricic, I., Purwar, M., Eblimit, Z., Walker, S. N., et al. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100420 · Cited by 76
COVID-19 Vaccines: Adenoviral Vectors
Jacob-Dolan, C., & Barouch, D. H. (2021) · Annual Review of Medicine · doi:10.1146/annurev-med-012621-102252 · Cited by 76
Thuluva, S., Paradkar, V. M., Gunneri, S., Yerroju, V., Mogulla, R. R., Turaga, K., Kyasani, M., Manoharan, S. K., Medigeshi, G. R., Singh, J., et al. (2022) · EBioMedicine · doi:10.1016/j.ebiom.2022.104217 · Cited by 76
Potent Neutralizing Antibodies Directed to Multiple Epitopes on SARS-CoV-2 SpikePreprint
Liu, L., Wang, P., Nair, M. S., Yu, J., Rapp, M., Wang, Q., Luo, Y., Chan, J. F.-W., Sahi, V., Figueroa, A., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.17.153486 · Cited by 76
Suryadevara, N., Shrihari, S., Gilchuk, P., VanBlargan, L. A., Binshtein, E., Zost, S. J., Nargi, R. S., Sutton, R. E., Winkler, E. S., Chen, E. C., et al. (2021) · doi:10.1101/2021.01.19.427324 · Cited by 361
Li, C., Yu, D., Wu, X. J., Hong, L., Zhou, Z., Xie, Y., Li, T., Wu, J., Lu, F., Feng, L. Z., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24230-5 · Cited by 75
Self-citationKoerber, N., Priller, A., Yazici, S., Bauer, T., Cheng, C., Mijočević, H., Wintersteller, H., Jeske, S. D., Vogel, E., Feuerherd, M., et al. (2022) · Nature Communications · doi:10.1038/s41467-021-27649-y · Cited by 75
Broad anti–SARS-CoV-2 antibody immunity induced by heterologous ChAdOx1/mRNA-1273 vaccination
Kaku, C. I., Champney, E. R., Normark, J., García, M., Johnson, C. E., Ahlm, C., Christ, W., Sakharkar, M., Ackerman, M. E., Klingström, J., et al. (2022) · Science · doi:10.1126/science.abn2688 · Cited by 75
SARS-CoV-2 Beta variant infection elicits potent lineage-specific and cross-reactive antibodies
Reincke, S. M., Yuan, M., Kornau, H., Corman, V. M., van Hoof, S., Sánchez-Sendín, E., Ramberger, M., Yu, W., Hua, Y., Tien, H. J., et al. (2022) · Science · doi:10.1126/science.abm5835 · Cited by 75
Planchais, C., Fernández, I., Bruel, T., de Melo, G. D., Prot, M., Beretta, M., Guardado‐Calvo, P., Dufloo, J., Molinos-Albert, L. M., Backović, M., et al. (2022) · The Journal of Experimental Medicine · doi:10.1084/jem.20220638 · Cited by 75
The role of B cells in COVID-19 infection and vaccination
Chen, S., Guan, F., Candotti, F., Benlagha, K., Câmara, N. O. S., Herrada, A. A., James, L. K., Lei, J., Miller, H., Kubo, M., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.988536 · Cited by 75
Self-citationSequence signatures of two public antibody clonotypes that bind SARS-CoV-2 receptor binding domain
Tan, T. J. C., Yuan, M., Kuzelka, K., Padron, G. C., Beal, J. R., Chen, X., Wang, Y., Rivera-Cardona, J., Zhu, X., Stadtmueller, B. M., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24123-7 · Cited by 75
Yi, C., Sun, X., Lin, Y., Gu, C., Ding, L., Lü, X., Yang, Z., Zhang, Y., Ma, L., Gu, W., et al. (2021) · Genome Medicine · doi:10.1186/s13073-021-00985-w · Cited by 74
Cryo-EM: the resolution revolution and drug discovery
de Oliveira, T. M., van Beek, L., Shilliday, F., Debreczeni, J. É., & Phillips, C. (2021) · SLAS DISCOVERY · doi:10.1177/2472555220960401 · Cited by 73
Self-citationCurrent Status of COVID‐19 (Pre)Clinical Vaccine Development
Ye, T., Zhong, Z., García‐Sastre, A., Schotsaert, M., & Geest, B. G. D. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202008319 · Cited by 73
Dynamics of CD4 T Cell and Antibody Responses in COVID-19 Patients With Different Disease Severity
Koblischke, M., Traugott, M. T., Medits, I., Spitzer, F. S., Zoufaly, A., Weseslindtner, L., Simonitsch, C., Seitz, T., Hoepler, W., Puchhammer‐Stöckl, E., et al. (2020) · Frontiers in Medicine · doi:10.3389/fmed.2020.592629 · Cited by 73
Innate lymphoid cells and COVID-19 severity in SARS-CoV-2 infection
Silverstein, N. J., Wang, Y., Manickas-Hill, Z., Carbone, C., Dauphin, A., Boribong, B. P., Loiselle, M., Davis, J., Leonard, M. M., Kuri-Cervantes, L., et al. (2022) · eLife · doi:10.7554/elife.74681 · Cited by 73
Multiscale PHATE identifies multimodal signatures of COVID-19
Kuchroo, M., Huang, J., Wong, P., Grenier, J.-C., Shung, D., Tong, A., Lucas, C., Klein, J., Burkhardt, D. B., Gigante, S., et al. (2022) · Nature Biotechnology · doi:10.1038/s41587-021-01186-x · Cited by 72
A public vaccine-induced human antibody protects against SARS-CoV-2 and emerging variants
Schmitz, A. J., Turner, J. S., Liu, Z., Aziati, I. D., Chen, R. E., Joshi, A., Bricker, T. L., Darling, T. L., Adelsberg, D. C., Alsoussi, W. B., et al. (2021) · doi:10.1101/2021.03.24.436864 · Cited by 72
COVID-19 Vaccine: Critical Questions with Complicated Answers
Haidere, M. F., Ratan, Z. A., Nowroz, S., Zaman, S. B., Jung, Y.-J., Hosseinzadeh, H., & Cho, J. Y. (2020) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2020.178 · Cited by 72
Gan, H. H., Twaddle, A., Marchand, B., & Gunsalus, K. C. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167051 · Cited by 72
Lee, C.-Y., & Lowen, A. C. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.03.009 · Cited by 71
Lau, E. H. Y., Hui, D. S. C., Tsang, O. T., Chan, W. H., Kwan, M. Y. W., Chiu, S. S. S., Cheng, S. M. S., Ko, R. L., Li, J. K., Chaothai, S., et al. (2021) · EClinicalMedicine · doi:10.1016/j.eclinm.2021.101174 · Cited by 71
Immunogenicity of COVID-19 vaccines in patients with diabetes mellitus: A systematic review
Boroumand, A. B., Forouhi, M., Karimi, F., Moghadam, A. S., Naeini, L. G., Kokabian, P., & Naderi, D. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.940357 · Cited by 71
COVID‐19 Pandemic: Applying a Multisystemic Lens
Rolland, J. S. (2020) · Family Process · doi:10.1111/famp.12584 · Cited by 70
Henß, L., Scholz, T., von Rhein, C., Wieters, I., Borgans, F., Eberhardt, F., Zacharowski, K. D., Ciesek, S., Rohde, G. G. U., Vehreschild, M. J. G. T., et al. (2020) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiaa680 · Cited by 70
Newell, K. L., Clemmer, D. C., Cox, J. B., Kayode, Y. I., Zoccoli-Rodriguez, V., Taylor, H. E., Endy, T. P., Wilmore, J. R., & Winslow, G. M. (2021) · PLoS ONE · doi:10.1371/journal.pone.0244855 · Cited by 70
Evolution of antibody immunity following Omicron BA.1 breakthrough infection
Kaku, C. I., Starr, T. N., Zhou, P.-P., Dugan, H. L., Khalifé, P., Song, G., Champney, E. R., Mielcarz, D. W., Geoghegan, J. C., Burton, D. R., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38345-4 · Cited by 70
SARS-CoV-2 seroprevalence in Spain – Authors' reply
Pollán, M., Pérez‐Gómez, B., Pastor‐Barriuso, R., Oteo, J., Pérez‐Olmeda, M., & Yotti, R. (2020) · The Lancet · doi:10.1016/s0140-6736(20)32266-2 · Cited by 70
Dingens, A. S., Crawford, K. H. D., Adler, A., Steele, S. L., Lacombe, K., Eguia, R. T., Amanat, F., Walls, A. C., Wolf, C. R., Murphy, M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18178-1 · Cited by 69
Bertoletti, A., Tan, A. T., & Bert, N. L. (2021) · Oxford Open Immunology · doi:10.1093/oxfimm/iqab006 · Cited by 69
A haemagglutination test for rapid detection of antibodies to SARS-CoV-2
Townsend, A., Rijal, P., Xiao, J. H., Tan, T. K., Huang, K.-Y. A., Schimanski, L. M., Huo, J., Gupta, N., Rahikainen, R., Matthews, P. C., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22045-y · Cited by 69
Convalescent Plasma Therapy for COVID-19: A Graphical Mosaic of the Worldwide Evidence
Klassen, S. A., Senefeld, J. W., Senese, K. A., Johnson, P. W., Wiggins, C. C., Baker, S. E., van Helmond, N., Bruno, K. A., Pirofski, L., Shoham, S., et al. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.684151 · Cited by 69
Highly synergistic combinations of nanobodies that target SARS-CoV-2 and are resistant to escape
Mast, F. D., Fridy, P. C., Ketaren, N. E., Wang, J., Jacobs, E. Y., Olivier, J. P., Sanyal, T., Molloy, K. R., Schmidt, F., Rutkowska, M., et al. (2021) · eLife · doi:10.7554/elife.73027 · Cited by 69
Self-citationFernández, M. L., Santiago, G. C., Martín-Dunn, A. M., Gonzalez-Roche, D., Béquet‐Romero, M., Márquez, G., González-Moya, I., Canaán-Haden, C., Cabrales, A., Espinosa, L. A., et al. (2022) · New Biotechnology · doi:10.1016/j.nbt.2022.08.002 · Cited by 69
Zhou, T., Teng, I., Olia, A. S., Cerutti, G., Gorman, J., Nazzari, A. F., Shi, W., Tsybovsky, Y., Wang, L., Wang, S., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108322 · Cited by 69
Presence of antibody-dependent cellular cytotoxicity (ADCC) against SARS-CoV-2 in COVID-19 plasma
Tso, F. Y., Lidenge, S. J., Poppe, L. K., Peña, P. B., Privatt, S. R., Bennett, S. J., Ngowi, J. R., Mwaiselage, J., Belshan, M., Siedlik, J. A., et al. (2021) · PLOS ONE · doi:10.1371/journal.pone.0247640 · Cited by 68
Durability of neutralizing antibodies and T-cell response post SARS-CoV-2 infection
Tan, Y., Liu, F., Xu, X., Ling, Y., Huang, W., Zhu, Z., Guo, M., Lin, Y., Fu, Z., Liang, D., et al. (2020) · Frontiers of Medicine · doi:10.1007/s11684-020-0822-5 · Cited by 68
Self-citationGrossberg, A. N., Koza, L. A., Ledreux, A., Prusmack, C. J., Krishnamurthy, H. K., Jayaraman, V., Granholm, A., & Linseman, D. A. (2021) · Nature Communications · doi:10.1038/s41467-021-21040-7 · Cited by 68
Terpos, E., Stellas, D., Rosati, M., Sergentanis, T. Ν., Hu, X., Politou, M., Pappa, V., Ntanasis‐Stathopoulos, I., Karaliota, S., Bear, J., et al. (2021) · European Journal of Internal Medicine · doi:10.1016/j.ejim.2021.05.010 · Cited by 68
Epistasis lowers the genetic barrier to SARS-CoV-2 neutralizing antibody escape
Witte, L., Baharani, V. A., Schmidt, F., Wang, Z., Cho, A., Raspe, R., Guzmán-Cardozo, C., Muecksch, F., Canis, M., Park, D., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-35927-0 · Cited by 68
Self-citationOjeda, D. S., Ledesma, M. M. G. L., Pallarés, H. M., Navarro, G. S. C., Sánchez, L., Perazzi, B. E., Villordo, S. M., Alvarez, D. E., BioBanco Working Group, Echavarría, M., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009161 · Cited by 67
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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