Analysis of a SARS-CoV-2-Infected Individual Reveals Development of Potent Neutralizing Antibodies with Limited Somatic Mutation
Open accessAbstract
Antibody responses develop following SARS-CoV-2 infection, but little is known about their epitope specificities, clonality, binding affinities, epitopes, and neutralizing activity. We isolated B cells specific for the SARS-CoV-2 envelope glycoprotein spike (S) from a COVID-19-infected subject 21 days after the onset of clinical disease. 45 S-specific monoclonal antibodies were generated. They had undergone minimal somatic mutation with limited clonal expansion, and three bound the receptor-binding domain (RBD). Two antibodies neutralized SARS-CoV-2. The most potent antibody bound the RBD and prevented binding to the ACE2 receptor, while the other bound outside the RBD. Thus, most anti-S antibodies that were generated in this patient during the first weeks of COVID-19 infection were non-neutralizing and target epitopes outside the RBD. Antibodies that disrupt the SARS-CoV-2 S-ACE2 interaction can potently neutralize the virus without undergoing extensive maturation. Such antibodies have potential preventive and/or therapeutic potential and can serve as templates for vaccine design.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Numerous neutralizing anti-RBD monoclonal antibodies have been characterized, the most potent of which block the RBD-ACE2 interaction.
“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 [22]
SARS-CoV-2 infection rapidly elicits nAbs that decline, but remain detectable, over several months.
“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 [22]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
R: A Language and Environment for Statistical Computing
R Core Team (2000) · doi:10.32614/r.manuals · Cited by 355,706 · see citing works
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 · see citing works
An interactive web-based dashboard to track COVID-19 in real time
Dong, E., Du, H., & Gardner, L. (2020) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(20)30120-1 · Cited by 10,048 · cited 1× · see citing works
“5 million documented cases of COVID-19 and over 420,000 deaths (Dong et al., 2020).”
Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., Graham, B. S., & McLellan, J. S. (2020) · Science · doi:10.1126/science.abb2507 · Cited by 8,897 · cited 10× · see citing works
“, 2020), and immunization with SARS S protein can elicit anti-SARS-CoV-2 neutralizing antibodies in wild-type and humanized mice, as well as llamas (Walls et al., 2020; Wang et al., 2020;Wrapp et al., 2020).”
BackgroundMethodResultInfluentialStructure, 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 · see citing works
Self-citationAngiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
Li, W., Moore, M. J., Vasilieva, N., Sui, J., Wong, S. K., Berne, M. A., Somasundaran, M., Sullivan, J. L., Luzuriaga, K., Greenough, T. C., et al. (2003) · Nature · doi:10.1038/nature02145 · Cited by 5,923 · cited 1× · see citing works
“Like SARS-CoV, SARS-CoV-2 utilizes angiotensin-converting enzyme 2 (ACE2) as an entry receptor binding with nM affinity (Li et al., 2003; Walls et al., 2020; Wrapp et al., 2020; Hoffmann et al., 2020; Letko et al., 2020; Ou et al., 2020).”
Wan, Y., Shang, J., Graham, R., Baric, R. S., & Li, F. (2020) · Journal of Virology · doi:10.1128/jvi.00127-20 · Cited by 4,341 · cited 4× · see citing works
“Although SARSCoV and SARS-CoV-2 share extensive amino acid sequence in the RBD (74%), and both viruses utilize human ACE2 for entry, the amino acid identity in the receptor binding motif is only 50% (Wan et al., 2020).”
InfluentialSelf-citationLetko, M., Marzi, A., & Munster, V. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0688-y · Cited by 3,109 · cited 1× · see citing works
“Like SARS-CoV, SARS-CoV-2 utilizes angiotensin-converting enzyme 2 (ACE2) as an entry receptor binding with nM affinity (Li et al., 2003; Walls et al., 2020; Wrapp et al., 2020; Hoffmann et al., 2020; Letko et al., 2020; Ou et al., 2020).”
Ou, X., Liu, Y., Lei, X., Li, P., Mi, D., Ren, L., Guo, L., Guo, R., Chen, T., Hu, J., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15562-9 · Cited by 3,097 · cited 2× · see citing works
“Like SARS-CoV, SARS-CoV-2 utilizes angiotensin-converting enzyme 2 (ACE2) as an entry receptor binding with nM affinity (Li et al., 2003; Walls et al., 2020; Wrapp et al., 2020; Hoffmann et al., 2020; Letko et al., 2020; Ou et al., 2020).”
Okba, N. M. A., Müller, M. A., Li, W., Wang, C., GeurtsvanKessel, C. H., Corman, V. M., Lamers, M. M., Sikkema, R. S., de Bruin, E., Chandler, F. D., et al. (2020) · Emerging Infectious Diseases · doi:10.3201/eid2607.200841 · Cited by 1,614 · cited 3× · see citing works
“Although binding and neutralizing antibody responses are known to develop following SARS-CoV-2 infection (Ni et al., 2020; Okba et al., 2020), no information is currently available on the epitope specificities, clonality, binding affinities, and neutralizing potentials of the antibody response.”
BackgroundResultInfluentialA highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV
Yuan, M., Wu, N. C., Zhu, X., Lee, C.-C. D., So, R. T. Y., Lv, H., Mok, C. K. P., & Wilson, I. A. (2020) · Science · doi:10.1126/science.abb7269 · Cited by 1,405 · cited 2× · see citing works
“In contrast, CV5 and CV43, the other two anti-RBD mAbs and the CR3022 mAb, which binds the RBD outside of the ACE2 binding site, did not (Figure 4C) (ter Meulen et al., 2006; Yuan et al., 2020).”
Brochet, X., Lefranc, M., & Giudicelli, V. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn316 · Cited by 1,220 · cited 1× · see citing works
“The antibody gene usage was assigned using IMGT/V-QUEST (Brochet et al., 2008).”
Corti, D., Voss, J., Gamblin, S. J., Codoni, G., Macagno, A., Jarrossay, D., Vachieri, S. G., Pinna, D., Minola, A., Vanzetta, F., et al. (2011) · Science · doi:10.1126/science.1205669 · Cited by 1,203 · cited 1× · see citing works
“, 2020) and is consistent with the rapid development of neutralizing responses to SARS-CoV infection (Corti et al., 2011).”
A human monoclonal antibody blocking SARS-CoV-2 infection
Wang, C., Li, W., Drabek, D., Okba, N. M. A., van Haperen, R., Osterhaus, A. D. M. E., van Kuppeveld, F. J. M., Haagmans, B. L., Grosveld, F. G., & Bosch, B. (2020) · Nature Communications · doi:10.1038/s41467-020-16256-y · Cited by 1,115 · cited 1× · see citing works
“, 2020), and immunization with SARS S protein can elicit anti-SARS-CoV-2 neutralizing antibodies in wild-type and humanized mice, as well as llamas (Walls et al., 2020; Wang et al., 2020;Wrapp et al., 2020).”
Tiller, T., Meffre, E., Yurasov, S., Tsuiji, M., Nussenzweig, M. C., & Wardemann, H. (2007) · Journal of Immunological Methods · doi:10.1016/j.jim.2007.09.017 · Cited by 1,078 · cited 1× · see citing works
“The VH and VL sequences were recovered using gene specific primers and cycling conditions previously described (Tiller et al., 2008).”
Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen
Pallesen, J., Wang, N., Corbett, K. S., Wrapp, D., Kirchdoerfer, R. N., Turner, H. L., Cottrell, C. A., Becker, M. M., Wang, L., Shi, W., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707304114 · Cited by 1,073 · cited 4× · see citing works
“…SARS-CoV-2 receptor binding domain fused to a monomeric Fc (paH- SARS-CoV-RBD-Fc) as well as a plasmid encoding the human ACE2 ectodomain (amino acids 1-615) with c-terminal His- and strep-tags (paH-ACE2-Hisstrep) were a kind gift from Dr. Jason McLellan (Pallesen et al., 2017; Wrapp et al., 2020).”
BackgroundMethodResultInfluentialDetection of SARS-CoV-2-Specific Humoral and Cellular Immunity in COVID-19 Convalescent Individuals
Ni, L., Ye, F., Cheng, M., Yu, F., Deng, Y., Zhao, H. J., Peng, W., Ge, J., Gou, M., Li, X., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.04.023 · Cited by 1,069 · cited 3× · see citing works
“The development of neutralizing antibody titers at this early time point has been reported for other COVID-19 patients (Ni et al., 2020; Okba et al., 2020) and is consistent with the rapid development of neutralizing responses to SARS-CoV infection (Corti et al.”
InfluentialCharif, D., & Lobry, J. R. (2007) · Biological and medical physics series · doi:10.1007/978-3-540-35306-5_10 · Cited by 1,025 · cited 1× · see citing works
“, 2018), seqinr (Charif and Lobry, 2007), and tidyverse (Wickham, 2017) in R and GraphPad Prism version 7 were used to create graphs.”
Song, W., Gui, M., Wang, X., & Xiang, Y. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007236 · Cited by 842 · cited 1× · see citing works
“High-resolution structures of the SARS-CoV-2 prefusion-stabilized spike (S) ectodomain revealed that it adopts multiple conformations with either one receptor-binding domain (RBD) in the ‘‘up’’ or ‘‘open’’ conformation or all RBDs in the ‘‘down’’ or ‘‘closed’’ conformation, similar to previous reports on both SARS-CoV…”
Yuan, Y., Cao, D., Zhang, Y., Ma, J., Qi, J., Wang, Q., Lu, G., Wu, Y., Yan, J., Shi, Y., et al. (2017) · Nature Communications · doi:10.1038/ncomms15092 · Cited by 761 · see citing works
Crawford, K. H. D., Eguia, R. T., Dingens, A. S., Loes, A. N., Malone, K. D., Wolf, C. R., Chu, H. Y., Tortorici, M. A., Veesler, D., Murphy, M., et al. (2020) · Viruses · doi:10.3390/v12050513 · Cited by 727 · cited 1× · see citing works
“Neutralization Assay HIV-1 derived viral particles were pseudotyped with full length wild-type SARS CoV-2 S (Crawford et al., 2020).”
Self-citationTraggiai, E., Becker, S., Subbarao, K., Kolesnikova, L., Uematsu, Y., Gismondo, M. R., Murphy, B. R., Rappuoli, R., & Lanzavecchia, A. (2004) · Nature Medicine · doi:10.1038/nm1080 · Cited by 697 · cited 1× · see citing works
“Potent anti-SARS-CoV neutralizing mAbs that bind RBD are derived from different VH genes (VH1-18, VH1-69, or VH3-30) than CV30 (Prabakaran et al., 2006; Sui et al., 2004; Traggiai et al., 2004; Walls et al., 2019).”
ter Meulen, J., van den Brink, E. N., Poon, L. L. M., Marissen, W. E., Leung, C. S.-W., Cox, F., Cheung, C. Y., Bakker, A. Q., Bogaards, J. A., van Deventer, E., et al. (2006) · PLoS Medicine · doi:10.1371/journal.pmed.0030237 · Cited by 599 · see citing works
Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion
Walls, A. C., Xiong, X., Park, Y.-J., Tortorici, M. A., Snijder, J., Quispe, J., Cameroni, E., Gopal, R., Dai, M., Lanzavecchia, A., et al. (2019) · Cell · doi:10.1016/j.cell.2018.12.028 · Cited by 582 · see citing works
Gui, M., Song, W., Zhou, H., Xu, J., Chen, S., Xiang, Y., & Wang, X. (2016) · Cell Research · doi:10.1038/cr.2016.152 · Cited by 577 · cited 1× · see citing works
“High-resolution structures of the SARS-CoV-2 prefusion-stabilized spike (S) ectodomain revealed that it adopts multiple conformations with either one receptor-binding domain (RBD) in the ‘‘up’’ or ‘‘open’’ conformation or all RBDs in the ‘‘down’’ or ‘‘closed’’ conformation, similar to previous reports on both SARS-CoV…”
Commonality despite exceptional diversity in the baseline human antibody repertoire
Briney, B., Inderbitzin, A., Joyce, C., & Burton, D. R. (2019) · Nature · doi:10.1038/s41586-019-0879-y · Cited by 544 · cited 1× · see citing works
“Rather, they were derived from a diverse VH/ VL gene repertoire, with frequencies similar to those reported in healthy uninfected individuals (Briney et al., 2019; DeKosky et al., 2016; Soto et al., 2019; Vázquez Bernat et al., 2019).”
Sui, J., Li, W., Murakami, A., Tamin, A., Matthews, L. J., Wong, S. K., Moore, M. J., Tallarico, A. S. C., Olurinde, M., Choe, H., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307140101 · Cited by 540 · cited 4× · see citing works
“Largely unmutated antibodies against SARS-CoV S (Prabakaran et al., 2006; Sui et al., 2004) and MERS-CoV S (Jiang et al.”
InfluentialKirchdoerfer, R. N., Wang, N., Pallesen, J., Wrapp, D., Turner, H. L., Cottrell, C. A., Corbett, K. S., Graham, B. S., McLellan, J. S., & Ward, A. B. (2018) · Scientific Reports · doi:10.1038/s41598-018-34171-7 · Cited by 466 · cited 1× · see citing works
“High-resolution structures of the SARS-CoV-2 prefusion-stabilized spike (S) ectodomain revealed that it adopts multiple conformations with either one receptor-binding domain (RBD) in the ‘‘up’’ or ‘‘open’’ conformation or all RBDs in the ‘‘down’’ or ‘‘closed’’ conformation, similar to previous reports on both SARS-CoV…”
Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation
Mouquet, H., Scheid, J. F., Zöller, M., Krogsgaard, M., Ott, R. G., Shukair, S. A., Artyomov, M. N., Pietzsch, J., Connors, M., Pereyra, F., et al. (2010) · Nature · doi:10.1038/nature09385 · Cited by 426 · cited 1× · see citing works
“, 2018) or subcloned into the pT4-341 HC vector (Mouquet et al., 2010) using inFusion cloning.”
High frequency of shared clonotypes in human B cell receptor repertoires
Soto, C., Bombardi, R. G., Branchizio, A., Kose, N., Matta, P., Sevy, A. M., Sinkovits, R. S., Gilchuk, P., Finn, J. A., & Crowe, J. E. (2019) · Nature · doi:10.1038/s41586-019-0934-8 · Cited by 294 · cited 1× · see citing works
“Rather, they were derived from a diverse VH/ VL gene repertoire, with frequencies similar to those reported in healthy uninfected individuals (Briney et al., 2019; DeKosky et al., 2016; Soto et al., 2019; Vázquez Bernat et al., 2019).”
Ying, T., Du, L., Ju, T. W., Prabakaran, P., Lau, C. C. Y., Lu, L., Liu, Q., Wang, L., Feng, Y., Wang, Y., et al. (2014) · Journal of Virology · doi:10.1128/jvi.00912-14 · Cited by 233 · cited 1× · see citing works
“The RBD of MERS-CoV is also a target of potent neutralizing antibodies (Jiang et al., 2014; Niu et al., 2018; Tang et al., 2014; Ying et al., 2014), highlighting the importance of receptor blocking antibodies for coronavirus vaccine development.”
Prabakaran, P., Gan, J., Feng, Y., Zhu, Z., Choudhry, V., Xiao, X., Ji, X., & Dimitrov, D. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600697200 · Cited by 232 · cited 3× · see citing works
“Largely unmutated antibodies against SARS-CoV S (Prabakaran et al., 2006; Sui et al., 2004) and MERS-CoV S (Jiang et al.”
Tang, X.-C., Agnihothram, S. S., Jiao, Y., Stanhope, J., Graham, R. L., Peterson, E. C., Avnir, Y., Tallarico, A. S. C., Sheehan, J., Zhu, Q., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402074111 · Cited by 232 · cited 3× · see citing works
“The RBD of MERS-CoV is also a target of potent neutralizing antibodies (Jiang et al., 2014; Niu et al., 2018; Tang et al., 2014; Ying et al., 2014), highlighting the importance of receptor blocking antibodies for coronavirus vaccine development.”
Jiang, L., Wang, N., Zuo, T., Shi, X., Poon, V. K., Wu, Y., Gao, F., Li, D., Wang, R., Guo, J., et al. (2014) · Science Translational Medicine · doi:10.1126/scitranslmed.3008140 · Cited by 215 · cited 4× · see citing works
“The RBD of MERS-CoV is also a target of potent neutralizing antibodies (Jiang et al., 2014; Niu et al., 2018; Tang et al., 2014; Ying et al., 2014), highlighting the importance of receptor blocking antibodies for coronavirus vaccine development.”
InfluentialHwang, W. C., Lin, Y., Santelli, E., Sui, J., Jaroszewski, L., Stec, B., Farzan, M., Marasco, W. A., & Liddington, R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603275200 · Cited by 203 · cited 1× · see citing works
“Several neutralizing mAbs that block the interaction of SARS-CoV with the ACE2 receptor have been described (Hwang et al., 2006; Prabakaran et al., 2006; Rockx et al., 2008; Sui et al., 2004; Walls et al., 2019).”
DeKosky, B. J., Lungu, O. I., Park, D., Johnson, E. L., Charab, W., Chrysostomou, C., Kuroda, D., Ellington, A. D., Ippolito, G. C., Gray, J. J., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1525510113 · Cited by 189 · cited 1× · see citing works
“Rather, they were derived from a diverse VH/ VL gene repertoire, with frequencies similar to those reported in healthy uninfected individuals (Briney et al., 2019; DeKosky et al., 2016; Soto et al., 2019; Vázquez Bernat et al., 2019).”
Snijder, J., Ortego, M. S., Weidle, C., Stuart, A. B., Gray, M. D., McElrath, M. J., Pancera, M., Veesler, D., & McGuire, A. T. (2018) · Immunity · doi:10.1016/j.immuni.2018.03.026 · Cited by 140 · cited 1× · see citing works
“Paired VH and VL sequences from S2P positive B cells were codon optimized for human expression using the Integrated DNA Technologies (IDT) codon optimization tool, synthesized as eBlocks (IDT) and cloned into full-length pTT3 derived IgL and IgK expression vectors (Snijder et al., 2018) or subcloned into the pT4-341 H…”
Self-citationRockx, B., Corti, D., Donaldson, E., Sheahan, T., Stadler, K., Lanzavecchia, A., & Baric, R. (2008) · Journal of Virology · doi:10.1128/jvi.02377-07 · Cited by 134 · cited 2× · see citing works
“Moreover, the neutralizing potency correlated with the degree of S-ACE2 inhibition (Rockx et al., 2008).”
Ying, T., Prabakaran, P., Du, L., Shi, W., Feng, Y., Wang, Y., Wang, L., Li, W., Jiang, S., Dimitrov, D. S., et al. (2015) · Nature Communications · doi:10.1038/ncomms9223 · Cited by 110 · see citing works
Structural Approaches to Sequence Evolution
Bastolla, U., Porto, M., Roman, H. E., & Vendruscolo, M. (2007) · Biological and medical physics series · doi:10.1007/978-3-540-35306-5 · Cited by 109 · see citing works
Bernat, N. V., Corcoran, M., Hardt, U., Kaduk, M., Phad, G. E., Martin, M., & Hedestam, G. B. K. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00660 · Cited by 83 · see citing works
Niu, P., Zhang, S., Zhou, P.-P., Huang, B., Deng, Y. L., Qin, K., Wang, P., Wang, W., Wang, X., Zhou, J., et al. (2018) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiy311 · Cited by 73 · cited 2× · see citing works
“The RBD of MERS-CoV is also a target of potent neutralizing antibodies (Jiang et al., 2014; Niu et al., 2018; Tang et al., 2014; Ying et al., 2014), highlighting the importance of receptor blocking antibodies for coronavirus vaccine development.”
Cao, Z., Liu, L., Du, L., Zhang, C., Jiang, S., Li, T., & He, Y. (2010) · Virology Journal · doi:10.1186/1743-422x-7-299 · Cited by 72 · cited 1× · see citing works
“The RBD is a major target of neutralizing antibodies in SARS-CoV infection (Cao et al., 2010).”
Flagged first, then by citations
1 of the 44 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Starr, T. N., Greaney, A. J., Hilton, S. K., Ellis, D., Crawford, K. H. D., Dingens, A. S., Navarro, M. J., Bowen, J. E., Tortorici, M. A., Walls, A. C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.012 · Cited by 1,956 · see citing works
“The RBD is the dominant target of neutralizing antibodies (Cao et al., 2020; Ju et al., 2020; Pinto et al., 2020; Rogers et al., 2020; Seydoux et al., 2020; Shi et al., 2020; Wu et al., 2020b; Zost et al., 2020), and so any antigenic drift will be constrained by its mutational tolerance.”
Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies
Cao, Y., Wang, J., Jian, F., Xiao, T., Song, W., Yisimayi, A., Huang, W., Li, Q., Wang, P., An, R., et al. (2022) · Nature · doi:10.1038/s41586-021-04385-3 · Cited by 2,006 · see citing works
Robust T Cell Immunity in Convalescent Individuals with Asymptomatic or Mild COVID-19
Sekine, T., Perez-Potti, A., Rivera-Ballesteros, O., Strålin, K., Gorin, J.-B., Olsson, A., Llewellyn-Lacey, S., Kamal, H., Bogdanovic, G., Muschiol, S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.017 · Cited by 1,788 · see citing works
Evolution of antibody immunity to SARS-CoV-2
Gaebler, C., Wang, Z., Lorenzi, J. C. C., Muecksch, F., Finkin, S., Tokuyama, M., Cho, A., Jankovic, M., Schaefer-Babajew, D., Oliveira, T. Y., et al. (2021) · Nature · doi:10.1038/s41586-021-03207-w · Cited by 1,674 · see citing works
SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies
Barnes, C. O., Jette, C. A., Abernathy, M. E., Dam, K.-M. A., Esswein, S. R., Gristick, H. B., Malyutin, A. G., Sharaf, N. G., Huey-Tubman, K. E., Lee, Y. E., et al. (2020) · Nature · doi:10.1038/s41586-020-2852-1 · Cited by 1,599 · see citing works
Escape from neutralizing antibodies by SARS-CoV-2 spike protein variants
Weisblum, Y., Schmidt, F., Zhang, F., DaSilva, J., Poston, D., Lorenzi, J. C., Muecksch, F., Rutkowska, M., Hoffmann, H.-H., Michailidis, E., et al. (2020) · eLife · doi:10.7554/elife.61312 · Cited by 1,308 · see citing works
Seow, J., Graham, C., Merrick, B., Acors, S., Pickering, S., Steel, K. J. A., Hemmings, O., O’Byrne, A., Kouphou, N., Galao, R. P., et al. (2020) · Nature Microbiology · doi:10.1038/s41564-020-00813-8 · Cited by 1,419 · see citing works
Greaney, A. J., Loes, A. N., Crawford, K. H. D., Starr, T. N., Malone, K. D., Chu, H. Y., & Bloom, J. D. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.02.003 · Cited by 1,178 · see citing works
“relatively modest proportion of all spike-binding IgG plasma antibodies in naturally infected individuals, consistent with studies reporting that less than half of spike-reactive B cells and monoclonal antibodies bind to RBD (Brouwer et al., 2020; Huang et al., 2020; Seydoux et al., 2020; Voss et al., 2020).”
Self-citationGreaney, A. J., Starr, T. N., Gilchuk, P., Zost, S. J., Binshtein, E., Loes, A. N., Hilton, S. K., Huddleston, J., Eguia, R., Crawford, K. H. D., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2020.11.007 · Cited by 1,016 · see citing works
“Many of the most potently neutralizing anti-SARS-CoV-2 antibodies target the receptor-binding domain (RBD) of the viral spike protein, often competing with its binding to the ACE2 receptor (Brouwer et al., 2020; Cao et al., 2020; Ju et al., 2020; Liu et al., 2020; Rogers et al., 2020; Seydoux et al., 2020; Wec et al.…”
N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2
McCallum, M., De Marco, A., Lempp, F. A., Tortorici, M. A., Pinto, D., Walls, A. C., Beltramello, M., Chen, A., Liu, Z., Zatta, F., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.028 · Cited by 901 · see citing works
Barnes, C. O., West, A. P., Huey-Tubman, K. E., Hoffmann, M. A. G., Sharaf, N. G., Hoffman, P. R., Koranda, N., Gristick, H. B., Gaebler, C., Muecksch, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.025 · Cited by 795 · see citing works
“Other studies have also reported anti-SARS-CoV-2 mAbs derived from these genes (Brouwer et al., 2020; Cao et al., 2020; Chi et al., 2020; Ju et al., 2020; Rogers et al., 2020; Seydoux et al., 2020; Wu et al., 2020c; Zost et al., 2020).”
Persistence of serum and saliva antibody responses to SARS-CoV-2 spike antigens in COVID-19 patients
Isho, B., Abe, K. T., Zuo, M., Jamal, A. J., Rathod, B., Wang, J. H., Li, Z., Chao, G., Rojas, O. L., Bang, Y. M., et al. (2020) · Science Immunology · doi:10.1126/sciimmunol.abe5511 · Cited by 822 · see citing works
Comprehensive mapping of immune perturbations associated with severe COVID-19
Kuri-Cervantes, L., Pampena, M. B., Meng, W., Rosenfeld, A. M., Ittner, C. A. G., Weisman, A. R., Agyekum, R. S., Mathew, D., Baxter, A. E., Vella, L. A., et al. (2020) · Science Immunology · doi:10.1126/sciimmunol.abd7114 · Cited by 723 · see citing works
Structural basis of a shared antibody response to SARS-CoV-2
Yuan, M., Liu, H., Wu, N. C., Lee, C.-C. D., Zhu, X., Zhao, F., Huang, D., Yu, W., Hua, Y., Tien, H., et al. (2020) · Science · doi:10.1126/science.abd2321 · Cited by 589 · see citing works
Measuring SARS-CoV-2 neutralizing antibody activity using pseudotyped and chimeric viruses
Schmidt, F., Weisblum, Y., Muecksch, F., Hoffmann, H.-H., Michailidis, E., Lorenzi, J. C. C., Mendoza, P., Rutkowska, M., Bednarski, E., Gaebler, C., et al. (2020) · Journal of Experimental Medicine · doi:10.1084/jem.20201181 · Cited by 572 · see citing works
mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection
Stamatatos, L., Czartoski, J., Wan, Y.-H., Homad, L. J., Rubin, V., Glantz, H., Neradilek, M., Seydoux, E., Jennewein, M. F., MacCamy, A. J., et al. (2021) · Science · doi:10.1126/science.abg9175 · Cited by 557 · see citing works
Self-citationLarge-Scale Multi-omic Analysis of COVID-19 Severity
Overmyer, K. A., Shishkova, E., Miller, I. J., Balnis, J., Bernstein, M. N., Peters-Clarke, T. M., Meyer, J. G., Quan, Q., Muehlbauer, L. K., Trujillo, E. A., et al. (2020) · Cell Systems · doi:10.1016/j.cels.2020.10.003 · Cited by 584 · see citing works
“To better understand production of protective or possibly injurious antibodies, serial studies and characterization of the properties of individual antibodies is required (Ju et al., 2020; Seydoux et al., 2020).”
BackgroundImmunity, endothelial injury and complement-induced coagulopathy in COVID-19
Perico, L., Benigni, A., Casiraghi, F., Ng, L. F. P., Rénia, L., & Remuzzi, G. (2020) · Nature Reviews Nephrology · doi:10.1038/s41581-020-00357-4 · Cited by 603 · see citing works
Walls, A. C., Fiala, B., Schäfer, A., Wrenn, S., Pham, M. N., Murphy, M., Tse, L. V., Shehata, L., O’Connor, M. A., Chen, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.043 · Cited by 532 · see citing works
Self-citationCerutti, G., Guo, Y., Zhou, T., Gorman, J., Lee, M., Rapp, M., Reddem, E. R., Yu, J., Bahna, F., Bimela, J., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.03.005 · Cited by 519 · see citing works
REGN-COV2 antibodies prevent and treat SARS-CoV-2 infection in rhesus macaques and hamsters
Baum, A., Ajithdoss, D., Copin, R., Zhou, A., Lanza, K., Negron, N., Ni, M., Wei, Y., Mohammadi, K., Musser, B., et al. (2020) · Science · doi:10.1126/science.abe2402 · Cited by 517 · see citing works
Weisberg, S. P., Connors, T. J., Zhu, Y., Baldwin, M. R., Lin, W.-H. W., Wontakal, S. N., Szabo, P. A., Wells, S. B., Dogra, P., Gray, J. I., et al. (2020) · Nature Immunology · doi:10.1038/s41590-020-00826-9 · Cited by 540 · see citing works
A systematic review of SARS-CoV-2 vaccine candidates
Dong, Y., Dai, T., Wei, Y., Zhang, L., Zheng, M., & Zhou, F. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00352-y · Cited by 541 · see citing works
Enhanced SARS-CoV-2 neutralization by dimeric IgA
Wang, Z., Lorenzi, J. C. C., Muecksch, F., Finkin, S., Viant, C., Gaebler, C., Cipolla, M., Hoffmann, H.-H., Oliveira, T. Y., Oren, D. A., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abf1555 · Cited by 475 · see citing works
Cohen, K. W., Linderman, S. L., Moodie, Z., Czartoski, J., Lai, L., Mantus, G., Norwood, C., Nyhoff, L. E., Edara, V. V., Floyd, K., et al. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100354 · Cited by 441 · see citing works
Self-citationThe first 12 months of COVID-19: a timeline of immunological insights
Carvalho, T., Krammer, F., & Iwasaki, A. (2021) · Nature reviews. Immunology · doi:10.1038/s41577-021-00522-1 · Cited by 448 · see citing works
Mosaic nanoparticles elicit cross-reactive immune responses to zoonotic coronaviruses in mice
Cohen, A. A., Gnanapragasam, P. N. P., Lee, Y. E., Hoffman, P. R., Ou, S. K.-H., Kakutani, L. M., Keeffe, J. R., Wu, H., Howarth, M. R., West, A. P., et al. (2021) · Science · doi:10.1126/science.abf6840 · Cited by 392 · see citing works
Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants
Yuan, M., Huang, D., Lee, C.-C. D., Wu, N. C., Jackson, A. M., Zhu, X., Liu, H., Peng, L., van Gils, M. J., Sanders, R. W., et al. (2021) · doi:10.1101/2021.02.16.430500 · Cited by 364 · see citing works
Zhou, T., Tsybovsky, Y., Gorman, J., Rapp, M., Cerutti, G., Chuang, G., Katsamba, P. S., Sampson, J. M., Schön, A., Bimela, J. S., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.11.004 · Cited by 340 · see citing works
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) · Cell · doi:10.1016/j.cell.2021.03.029 · Cited by 397 · see citing works
“Most neutralizing SARS-CoV-2 mAbs block RBD interactions with ACE2 (Brouwer et al., 2020; Cao et al., 2020; Ju et al., 2020; Liu et al., 2020a; Rogers et al., 2020; Seydoux et al., 2020; Wec et al., 2020; Wu et al., 2020; Zost et al., 2020a, 2020b).”
Evolution of immune responses to SARS-CoV-2 in mild-moderate COVID-19
Wheatley, A. K., Juno, J. A., Wang, J. J., Selva, K. J., Reynaldi, A., Tan, H.-X., Lee, W. S., Wragg, K. M., Kelly, H. G., Esterbauer, R., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21444-5 · Cited by 351 · see citing works
Maturation and persistence of the anti-SARS-CoV-2 memory B cell response
Sokal, A., Chappert, P., Barba-Spaeth, G., Roeser, A., Fourati, S., Azzaoui, I., Vandenberghe, A., Fernandez, I., Meola, A., Bouvier-Alias, M., et al. (2021) · Cell · doi:10.1016/j.cell.2021.01.050 · Cited by 340 · see citing works
Molecular mechanism of interaction between SARS-CoV-2 and host cells and interventional therapy
Zhang, Q., Xiang, R., Huo, S., Zhou, Y., Jiang, S., Wang, Q., & Yu, F. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00653-w · Cited by 341 · see citing works
Kreer, C., Zehner, M., Weber, T., Ercanoglu, M. S., Gieselmann, L., Rohde, C., Halwe, S., Korenkov, M., Schommers, P., Vanshylla, K., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.044 · Cited by 313 · see citing works
Defining variant-resistant epitopes targeted by SARS-CoV-2 antibodies: A global consortium study
Hastie, K. M., Li, H., Bedinger, D., Schendel, S. L., Dennison, S. M., Li, K., Rayaprolu, V., Yu, X., Mann, C. J., Zandonatti, M. A., et al. (2021) · Science · doi:10.1126/science.abh2315 · Cited by 299 · see citing works
Self-citationAutoinflammatory and autoimmune conditions at the crossroad of COVID-19
Rodríguez, Y., Novelli, L., Rojas, M., Santis, M. D., Acosta‐Ampudia, Y., Monsalve, D. M., Ramı́rez-Santana, C., Costanzo, A., Ridgway, W. M., Ansari, A. A., et al. (2020) · Journal of Autoimmunity · doi:10.1016/j.jaut.2020.102506 · Cited by 312 · see citing works
“Up to now, there are several reports that confirm that NAbs against RBD can interrupt the interaction between SARS-CoV-2 and ACE2, thus controlling the infection [115,118].”
Hartley, G. E., Edwards, E. S. J., Aui, P. M., Varese, N., Stojanovic, S., McMahon, J., Peleg, A. Y., Boo, I., Drummer, H. E., Hogarth, P. M., et al. (2020) · Science Immunology · doi:10.1126/sciimmunol.abf8891 · Cited by 296 · see citing works
“These antibodies are detectable from approximately 6 days after PCR confirmation of infection, and those directed against spike receptor binding domain (RBD) show neutralizing capacity and hence, can prevent infection ( 15 , 16 ).”
BackgroundSARS-CoV-2 mRNA Vaccines: Immunological Mechanism and Beyond
Bettini, E., & Locci, M. (2021) · Vaccines · doi:10.3390/vaccines9020147 · Cited by 283 · see citing works
Muecksch, F., Weisblum, Y., Barnes, C., Schmidt, F., Schaefer-Babajew, D. J., Wang, Z.-J., Lorenzi, J. C. C., Flyak, A., DeLaitsch, A. T., Huey-Tubman, K. E., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.07.008 · Cited by 256 · see citing works
“The receptor-binding domains (RBDs) of the SARS-CoV-2 Spike trimer are key neutralization targets, and potent RBDspecific antibodies have been isolated from many convalescent donors (Brouwer et al., 2020; Cao et al., 2020; Chen et al., 2020; Chi et al., 2020; Hansen et al., 2020; Ju et al., 2020; Kreer et al., 2020; R…”
BackgroundThe total number and mass of SARS-CoV-2 virions
Sender, R., Bar‐On, Y. M., Gleizer, S., Bernshtein, B., Flamholz, A. I., Phillips, R., & Milo, R. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2024815118 · Cited by 278 · see citing works
Anti-SARS-CoV-2 receptor-binding domain antibody evolution after mRNA vaccination
Cho, A., Muecksch, F., Schaefer-Babajew, D. J., Wang, Z., Finkin, S., Gaebler, C., Ramos, V., Cipolla, M., Mendoza, P., Agudelo, M., et al. (2021) · Nature · doi:10.1038/s41586-021-04060-7 · Cited by 254 · see citing works
Tebas, P., Yang, S., Boyer, J., Reuschel, E. L., Patel, A. R., Christensen-Quick, A., Andrade, V. M., Morrow, M. P., Kraynyak, K. A., Agnes, J. T., et al. (2020) · EClinicalMedicine · doi:10.1016/j.eclinm.2020.100689 · Cited by 265 · see citing works
Mosaic RBD nanoparticles protect against challenge by diverse sarbecoviruses in animal models
Cohen, A. A., van Doremalen, N., Greaney, A. J., Andersen, H., Sharma, A., Starr, T. N., Keeffe, J. R., Fan, C., Schulz, J. E., Gnanapragasam, P. N. P., et al. (2022) · Science · doi:10.1126/science.abq0839 · Cited by 259 · see citing works
Du, S., Cao, Y., Zhu, Q., Yü, P., Qi, F., Wang, G., Du, X., Bao, L., Deng, W., Zhu, H., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.035 · Cited by 238 · see citing works
“SARS-CoV-2NAbs targeting theRBD, aswell as theNTD,were reported extensively (Barnes et al., 2020; Brouwer et al., 2020; Cao et al., 2020; Chi et al., 2020; Hansen et al., 2020; Ju et al., 2020; Liu et al., 2020; Pinto et al., 2020; Robbiani et al., 2020; Rogers et al., 2020; Seydoux et al., 2020; Shi et al., 2020; Wan…”
Humoral Responses and Serological Assays in SARS-CoV-2 Infections
Galipeau, Y., Greig, M., Liu, C., Driedger, M., & Langlois, M. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.610688 · Cited by 239 · see citing works
Monoclonal antibodies for COVID-19 therapy and SARS-CoV-2 detection
Hwang, Y., Lu, R., Su, S.-C., Chiang, P.-Y., Ko, S.-H., Ke, F.-Y., Liang, K.-H., Hsieh, T.-Y., & Wu, H. (2022) · Journal of Biomedical Science · doi:10.1186/s12929-021-00784-w · Cited by 236 · see citing works
Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies
Cao, Y., Wang, J., Jian, F., Xiao, T., Song, W., Yisimayi, A., Huang, W., Li, Q., Wang, P., An, R., et al. (2021) · Nature · doi:10.1038/d41586-021-03796-6 · Cited by 227 · see citing works
Tregoning, J. S., Brown, E. S., Cheeseman, H. M., Flight, K. E., Higham, S. L., Lemm, N.-M., Pierce, B. F., Stirling, D. C., Wang, Z., & Pollock, K. M. (2020) · Clinical & Experimental Immunology · doi:10.1111/cei.13517 · Cited by 222 · see citing works
Liu, H., Wu, N. C., Yuan, M., Bangaru, S., Torres, J., Caniels, T., van Schooten, J., Zhu, X.-Y., Lee, C. D., Brouwer, P., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.10.023 · Cited by 39 · see citing works
“Many humanmonoclonal antibodies have now been shown to target the SARS-CoV2 S protein (Andreano et al., 2020; Barnes et al., 2020; Brouwer et al., 2020; Cao et al., 2020; Chi et al., 2020; Ju et al., 2020; Li et al., 2020; Liu et al., 2020; Pinto et al., 2020; Robbiani et al., 2020; Rogers et al., 2020; Seydoux et al.…”
Ullah, I., Prévost, J., Ladinsky, M., Stone, H., Lu, M.-L., Anand, S., Beaudoin-Bussières, G., Symmes, K., Benlarbi, M., Ding, S.-L., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.08.015 · Cited by 152 · see citing works
“Human antibodies The human antibodies (CV3-1 and CV3-25) used in the work were isolated from blood of male convalescent donor S006 (male) recovered 41 days after symptoms onset using fluorescent recombinant stabilized Spike ectodomains (S2P) as probes to identify antigenspecific B cells as previously described (Jennew…”
Self-citationGreaney, A. J., Loes, A. N., Crawford, K. H. D., Starr, T. N., Malone, K. D., Chu, H. Y., & Bloom, J. D. (2021) · doi:10.1101/2020.12.31.425021 · Cited by 1,178 · see citing works
Self-citationCarsetti, R., Zaffina, S., Mortari, E. P., Terreri, S., Corrente, F., Capponi, C., Palomba, P., Mirabella, M., Cascioli, S., Palange, P., et al. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.610300 · Cited by 195 · see citing works
“In addition, neutralizing IgG MBCs isolated from COVID-19 patients may have none or very few somatic mutations (97) thus suggesting that the preimmune or innate MBC repertoire may contain SARS-CoV-2 specificities (82).”
BackgroundSARS-CoV-2 evolution in an immunocompromised host reveals shared neutralization escape mechanisms
Clark, S. A., Clark, L. E., Pan, J., Coscia, A., McKay, L. G. A., Shankar, S., Johnson, R. I., Brusic, V., Choudhary, M. C., Regan, J., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.027 · Cited by 189 · see citing works
“VH3-53 and VH3-66 antibody genes are identical except for a single amino acid change in an antibody framework region (FWR) (Lefranc and Lefranc, 2001), and potent neutralizing antibodies derived from these germline genes have been isolated from multiple COVID-19 convalescent individuals (Du et al., 2020; Robbiani et a…”
Recognition of the SARS-CoV-2 receptor binding domain by neutralizing antibodies
Yuan, M., Liu, H., Wu, N. C., & Wilson, I. A. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.10.012 · Cited by 181 · see citing works
Structural basis for broad coronavirus neutralization
Sauer, M. M., Tortorici, M. A., Park, Y., Walls, A. C., Homad, L. J., Acton, O. J., Bowen, J. E., Wang, C., Xiong, X., de van der Schueren, W., et al. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00596-4 · Cited by 174 · see citing works
“…2020; Corti et al., 2015; Hansen et al., 2020; Hassan et al., 2020a; Liu et al., 2020; Piccoli et al., 2020; Pinto et al., 2020; Rockx et al., 2008; Rockx et al., 2010; Rogers et al., 2020; Seydoux et al., 2020; Tortorici et al., 2020; Walls et al., 2019; Wang et al., 2020a; Zost et al., 2020).”
Self-citationDesigned proteins assemble antibodies into modular nanocages
Divine, R., Dang, H. V., Ueda, G., Fallas, J. A., Vulovic, I., Sheffler, W., Saini, S., Zhao, Y. T., Raj, I. X., Morawski, P. A., et al. (2021) · Science · doi:10.1126/science.abd9994 · Cited by 184 · see citing works
“1) formed with the SARS-CoV-2 S-binding antibodies CV1 or CV30 ( 38 ) were more effective at neutralizing pseudovirus entry into angiotensin-converting enzyme 2 (ACE2) – expressing cells than freeCV1 or CV30, dropping the apparent median inhibitory concentration (IC 50 ) by more than 200-fold and…”
Self-citationMolecular determinants and mechanism for antibody cocktail preventing SARS-CoV-2 escape
Ku, Z., Xie, X., Davidson, E., Ye, X., Su, H., Menachery, V. D., Li, Y., Yuan, Z., Zhang, X., Muruato, A. E., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20789-7 · Cited by 160 · see citing works
Germinal center responses to SARS-CoV-2 mRNA vaccines in healthy and immunocompromised individuals
(2022) · doi:10.1016/j.cell.2022.01.027 · Cited by 179 · see citing works
“Multiple groups reported that several near-germline nAbs, endowed with potent in vitro neutralizing activity, are elicited during natural SARS-CoV-2 infection in humans (Brouwer et al., 2020; Kreer et al., 2020; Schultheiß et al., 2020; Seydoux et al., 2020).”
Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation
Hurlburt, N. K., Seydoux, E., Wan, Y.-H., Edara, V. V., Stuart, A. B., Feng, J., Suthar, M. S., McGuire, A. T., Stamatatos, L., & Pancera, M. (2020) · Nature Communications · doi:10.1038/s41467-020-19231-9 · Cited by 162 · see citing works
Self-citationImmunity to SARS‐CoV‐2 induced by infection or vaccination
Dopico, X. C., Ols, S., Loré, K., & Hedestam, G. B. K. (2021) · Journal of Internal Medicine · doi:10.1111/joim.13372 · Cited by 164 · see citing works
Antibodies and Vaccines Target RBD of SARS-CoV-2
Min, L., & Sun, Q. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.671633 · Cited by 152 · see citing works
Shan, S., Luo, S., Yang, Z., Hong, J., Su, Y., Ding, F., Fu, L., Li, C., Chen, P., Ma, J., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2122954119 · Cited by 157 · see citing works
An Alternative Binding Mode of IGHV3-53 Antibodies to the SARS-CoV-2 Receptor Binding Domain
Wu, N. C., Yuan, M., Liu, H., Lee, C.-C. D., Zhu, X., Bangaru, S., Torres, J. L., Caniels, T. G., Brouwer, P. J. M., van Gils, M. J., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108274 · Cited by 157 · see citing works
Graham, C., Seow, J., Huettner, I., Khan, H., Kouphou, N., Acors, S., Winstone, H., Pickering, S., Galão, R. P., Dupont, L., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.03.023 · Cited by 130 · see citing works
“RBD-specific nAbs isolated here targeted epitopes similar to those reported previously (Barnes et al., 2020; Brouwer et al., 2020; Piccoli et al., 2020; Seydoux et al., 2020; Yuan et al., 2020b; Zost et al., 2020) and included nAbs that directly block ACE2 binding through binding RBM and nAbs targeting epitopes distal…”
Focosi, D., & Maggi, F. (2021) · Reviews in Medical Virology · doi:10.1002/rmv.2231 · Cited by 148 · see citing works
Antibody-mediated neutralization of SARS-CoV-2
Gruell, H., Vanshylla, K., Weber, T., Barnes, C. O., Kreer, C., & Klein, F. (2022) · Immunity · doi:10.1016/j.immuni.2022.05.005 · Cited by 145 · see citing works
Nanomaterials for photothermal and photodynamic cancer therapy
Nasseri, B., Alizadeh, E., Bani, F., Davaran, S., Akbarzadeh, A., Rabiee, N., Bahadori, A., Ziaei, M., Bagherzadeh, M., Saeb, M. R., et al. (2022) · Applied Physics Reviews · doi:10.1063/5.0047672 · Cited by 145 · see citing works
Galson, J. D., Schätzle, S., Bashford-Rogers, R. J. M., Raybould, M. I. J., Kovaltsuk, A., Kilpatrick, G. J., Minter, R., Finch, D. K., Dias, J. C., James, L. K., et al. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.605170 · Cited by 140 · see citing works
Neerukonda, S. N., Vassell, R. A., Herrup, R., Liu, S., Wang, T. T., Takeda, K., Yang, Y., Lin, T.-L., Wang, W., & Weiss, C. D. (2021) · PLoS ONE · doi:10.1371/journal.pone.0248348 · Cited by 130 · see citing works
Zhou, Y., Liu, Z., Li, S. N., Xu, W., Zhang, Q., da Silva, I. T., Li, C., Wu, Y., Jiang, Q., Liu, Z., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108699 · Cited by 134 · see citing works
“, 2020), and single B cell antibody cloning from SARS-CoV-2 convalescent donors (Andreano et al., 2020; Brouwer et al., 2020; Cao et al., 2020; Chen et al., 2020; Chi et al., 2020; Ju et al., 2020; Kreer et al., 2020; Liu et al., 2020a; Robbiani et al., 2020; Rogers et al., 2020; Seydoux et al., 2020; Wan et al., 2020…”
Dogan, M., Kozhaya, L., Placek, L., Gunter, C., Yi̇ği̇t, M., Hardy, R., Plassmeyer, M., Coatney, P., Lillard, K., Bukhari, Z., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-01649-6 · Cited by 95 · see citing works
Zhang, Q., Ju, B., Ge, J., Chan, J. F., Cheng, L., Wang, R., Huang, W., Fang, M., Chen, P., Zhou, B., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24514-w · Cited by 112 · see citing works
Emerging SARS-CoV-2 Variants of Concern (VOCs): An Impending Global Crisis
Thye, A. Y.-K., Law, J. W., Pusparajah, P., Letchumanan, V., Chan, K., & Lee, L. (2021) · Biomedicines · doi:10.3390/biomedicines9101303 · Cited by 116 · see citing works
King, R. G., Silva-Sánchez, A., Peel, J. N., Botta, D., Dickson, A. M., Pinto, A. K., Meza‐Perez, S., Allie, S. R., Schultz, M. D., Liu, M., et al. (2021) · Vaccines · doi:10.3390/vaccines9080881 · Cited by 133 · see citing works
Beaudoin-Bussières, G., Chen, Y., Ullah, I., Prévost, J., Tolbert, W. D., Symmes, K., Ding, S., Benlarbi, M., Gong, S. Y., Tauzin, A., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110368 · Cited by 120 · see citing works
“…CV3-13) used in the work were isolated from blood of male convalescent donor CV3 recovered 41 days after symptoms onset using fluorescent recombinant stabilized Spike ectodomains (S2P) as probes to identify antigen-specific B cells as previously described (Lu et al., 2020; Seydoux et al., 2020).”
Self-citationJette, C. A., Cohen, A. A., Gnanapragasam, P. N. P., Muecksch, F., Lee, Y. E., Huey‐Tubman, K. E., Schmidt, F., Hatziioannou, T., Bieniasz, P. D., Nussenzweig, M. C., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109760 · Cited by 99 · see citing works
“Consistent with their obligate role in viral entry, sarbecovirus S trimers are the primary targets of neutralizing antibodies (Brouwer et al., 2020; Cao et al., 2020; Fung and Liu, 2019; Kreer et al., 2020; Liu et al., 2020b; Robbiani et al., 2020; Rogers et al., 2020; Seydoux et al., 2020; Shi et al., 2020; Zost et a…”
Carrillo, J., Izquierdo‐Useros, N., Ávila‐Nieto, C., Pradenas, E., Clotet, B., & Blanco, J. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.10.108 · Cited by 114 · see citing works
Neutralizing antibodies targeting SARS-CoV-2 spike protein
Shi, X.-J., Yu, L., Lei, Y., Guang, Y., & Min, Q. (2020) · Stem Cell Research · doi:10.1016/j.scr.2020.102125 · Cited by 122 · see citing works
“and potently neutralize the virus without undergoing extensive maturation (Seydoux et al., 2020).”
Johnson, M., Wagstaffe, H. R., Gilmour, K. C., Mai, A., Lewis, J. E. A., Hunt, A., Sirr, J., Bengt, C., Grandjean, L., & Goldblatt, D. (2020) · Journal of Clinical Virology · doi:10.1016/j.jcv.2020.104572 · Cited by 107 · see citing works
Isolation and characterization of cross-neutralizing coronavirus antibodies from COVID-19+ subjects
Jennewein, M. F., MacCamy, A. J., Akins, N. R., Feng, J., Homad, L. J., Hurlburt, N., Seydoux, E., Wan, Y.-H., Stuart, A., Edara, V., et al. (2021) · bioRxiv · doi:10.1016/j.celrep.2021.109353 · Cited by 128 · see citing works
“We recently reported an initial characterization of the anti-S antibody responses generated by CV1 (Seydoux et al., 2020).”
InfluentialSelf-citationDual Nature of Type I Interferons in SARS-CoV-2-Induced Inflammation
King, C., & Sprent, J. (2021) · Trends in Immunology · doi:10.1016/j.it.2021.02.003 · Cited by 101 · see citing works
Chen, E. C., Gilchuk, P., Zost, S. J., Suryadevara, N., Winkler, E. S., Cabel, C. R., Binshtein, E., Chen, R. E., Sutton, R. E., Rodriguez, J. L., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109604 · Cited by 76 · see citing works
Pandemic Preparedness: Developing Vaccines and Therapeutic Antibodies For COVID-19
Sempowski, G. D., Saunders, K. O., Acharya, P., Wiehe, K. J., & Haynes, B. F. (2020) · Cell · doi:10.1016/j.cell.2020.05.041 · Cited by 100 · see citing works
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 · see citing works
Markers of Polyfunctional SARS-CoV-2 Antibodies in Convalescent Plasma
Natarajan, H., Crowley, A. R., Butler, S. E., Xu, S., Weiner, J. A., Bloch, E. M., Littlefield, K. E., Wieland‐Alter, W., Connor, R. I., Wright, P. F., et al. (2021) · mBio · doi:10.1128/mbio.00765-21 · Cited by 98 · see citing works
Signatures in SARS-CoV-2 spike protein conferring escape to neutralizing antibodies
Alenquer, M., Ferreira, F., Lousa, D., Valério, M., Medina-Lopes, M., Bergman, M., Gonçalves, J., Demengeot, J., Leite, R. B., Lilue, J., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009772 · Cited by 99 · see citing works
Stamatatos, L., Czartoski, J., Wan, Y.-H., Homad, L. J., Rubin, V., Glantz, H., Neradilek, M., Seydoux, E., Jennewein, M. F., MacCamy, A. J., et al. (2021) · doi:10.1101/2021.02.05.21251182 · Cited by 559 · see citing works
“As a consequence, several mAbs that potently neutralize SARS CoV-2 fail to bind SARS-CoV-1 (16, 22-24).”
BackgroundMethodInfluentialSelf-citationEvaluation of Cell-Based and Surrogate SARS-CoV-2 Neutralization Assays
Sholukh, A. M., Fiore-Gartland, A. J., Ford, E. S., Miner, M. D., Hou, Y. J., Tse, L. V., Kaiser, H., Zhu, H., Lu, J., Madarampalli, B., et al. (2021) · Journal of Clinical Microbiology · doi:10.1128/jcm.00527-21 · Cited by 119 · see citing works
“This is not surprising, as much of the immunodominant response associated with neutralization involves binding and/or blocking the spike RBD to inhibit viral entry to host cells (26, 28, 47).”
Self-citationChallenges and opportunities for antiviral monoclonal antibodies as COVID-19 therapy
Cruz-Teran, C. A., Tiruthani, K., McSweeney, M. D., Ma, A. D., Pickles, R., & Lai, S. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.12.004 · Cited by 77 · see citing works
COVID-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 86 · see citing works
Identification of immunodominant linear epitopes from SARS-CoV-2 patient plasma
Soler, L. F., Daguer, J., Barluenga, S., Vadas, O., Cohen, P., Pagano, S., Yerly, S., Kaiser, L., Vuilleumier, N., & Winssinger, N. (2020) · PLoS ONE · doi:10.1371/journal.pone.0238089 · Cited by 89 · see citing works
SARS-CoV-2 induces robust germinal center CD4 T follicular helper cell responses in rhesus macaques
Lakshmanappa, Y. S., Elizaldi, S. R., Roh, J. W., Schmidt, B., Carroll, T. D., Weaver, K. D., Smith, J. C., Verma, A., Deere, J., Dutra, J. C., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20642-x · Cited by 70 · see citing works
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 81 · see citing works
“CV30 Human mAb Neutralizes SARS-2 SARS-2 RBD but not with SARS RBD Competes with hACE-2 Blocks hACE2 RBD binding N/A N/A [79]”
Li, W., Chen, C., Drelich, A. K., Martinez, D. R., Gralinski, L. E., Sun, Z., Schäfer, A., Kulkarni, S. S., Liu, X., Leist, S. R., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2010197117 · Cited by 81 · see citing works
“Interestingly, Fab ab1 had only several somatic mutations compared to the closest germline predecessor genes, which was also observed for many neutralizing antibodies from COVID-19 patients (36 – 38).”
A global picture: therapeutic perspectives for COVID-19
Chavda, V., Kapadia, C., Soni, S., Prajapati, R., Chauhan, S., Yallapu, M., & Apostolopoulos, V. (2022) · Immunotherapy · doi:10.2217/imt-2021-0168 · Cited by 66 · see citing works
“Examples of some monoclonal antibodies under review for the management of COVID-19 are summarized in Supplementary Table 4 [147,148,149,150,151,152,153,154,155,156,157,158,159].”
BackgroundSilva-Cayetano, A., Foster, W. S., Innocentin, S., Belij-Rammerstorfer, S., Spencer, A. J., Burton, O. T., Fra-Bidó, S., Le Lee, J., Thakur, N., Conceicao, C., et al. (2021) · Med · doi:10.1016/j.medj.2020.12.006 · Cited by 84 · see citing works
Sequence 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 · see citing works
The immunodominant and neutralization linear epitopes for SARS-CoV-2
Lu, S., Xie, X.-X., Zhao, L., Wang, B., Zhu, J., Yang, T.-R., Yang, G.-W., Ji, M., Lv, C.-P., Xue, J., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2020.108666 · Cited by 76 · see citing works
“To assess neutralization antibodies induced by S protein epitopes, we incubated the immunization sera with D614 or G614 SARS-CoV-2 pseudo-viruses and then the mixture was added to ACE2-293FT cells which stably expressed ACE2.”
BackgroundInfluentialStructural definition of a pan-sarbecovirus neutralizing epitope on the spike S2 subunit
Hurlburt, N. K., Homad, L. J., Sinha, I. R., Jennewein, M. F., MacCamy, A. J., Wan, Y.-H., Boonyaratanakornkit, J. B., Sholukh, A. M., Jackson, A. M., Zhou, P.-P., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03262-7 · Cited by 77 · see citing works
“…cDNA for the HKU1 spike was PCR amplified from pCMV-HCoV-HKU1 (SinoBiological Cat# VG40606-UT) and subcloned into pTT3. pTT3-SARS-CoV-2-S (Seydoux et al., 2020), pHDM-MERS-CoV-Spike, pTWist-WIV1-CoV, pHDM-MERS-CoV-1 Spike, pTT3-HKU1 or pTT3-OC43 Spike were transfected into…”
MethodSelf-citationTang, J., Ravichandran, S., Lee, Y., Grubbs, G., Coyle, E. M., Klenow, L., Genser, H., Golding, H., & Khurana, S. (2021) · Nature Communications · doi:10.1038/s41467-021-21463-2 · Cited by 81 · see citing works
- Authors
- Seydoux, E., Homad, L. J., MacCamy, A. J., Parks, K. R., Hurlburt, N. K., Jennewein, M. F., Akins, N. R., Stuart, A. B., Wan, Y.-H., Feng, J., Whaley, R. E., Singh, S., Boeckh, M., Cohen, K. W., McElrath, M. J., Englund, J. A., Chu, H. Y., Pancera, M., McGuire, A. T., & Stamatatos, L.
- Affiliations
- Fred Hutch Cancer Center (US)
- University of Washington (US)
- National Institutes of Health (US)
- Corresponding author
- Pancera, Marie
- McGuire, Andrew T.
- Stamatatos, Leonidas
- ORCID
- Seydoux, Emilie
- Homad, Leah J.
- MacCamy, Anna J.
- Parks, K. Rachael
- Hurlburt, Nicholas K.
- Jennewein, Madeleine F.
- Akins, Nicholas R.
- Wan, Yu-Hsin
- Feng, Junli
- Whaley, Rachael E.
- Singh, Suruchi
- Boeckh, Michael
- Cohen, Kristen W.
- McElrath, M. Juliana
- Englund, Janet A.
- Chu, Helen Y.
- Pancera, Marie
- McGuire, Andrew T.
- Stamatatos, Leonidas
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2020-07
- Volume
- 53
- Issue
- 1
- Pages
- 98-105.e5
- ISSN
- 1074-7613 (ISSN-L)
- PMC
- PMC7276322
- OpenAlex
- W3033450058
- Cited by
- 364
- References
- 44
- Citations by year
- 2026: 9 · 2025: 12 · 2024: 13 · 2023: 27 · 2022: 70 · 2021: 143 · 2020: 89
- FWCI
- 10.79
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Immunity (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Fred Hutchinson Cancer Research Center
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- SARS-CoV-2, COVID-19 pandemic, neutralizing antibodies, spike protein, receptor binding domain, ACE2 receptor, somatic mutations, B-cell clonality, monoclonal antibodies, antibody epitope specificity, antibody affinity, antibody maturation, vaccine design
- MeSH terms
- Betacoronavirus, Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, Antibodies, Monoclonal, Antibodies, Viral, B-Lymphocytes, Binding Sites, Humans, Peptidyl-Dipeptidase A, Pneumonia, Viral, Protein Binding, Receptors, Virus, Viral Vaccines, Coronavirus Infections, Epitopes, B-Lymphocyte, Somatic Hypermutation, Immunoglobulin, Antibodies, Neutralizing, Pandemics, Spike Glycoprotein, Coronavirus
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
