The DOI matches its Crossref record; 43 of the 44 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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]
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 [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.
Citations
Cites
R: A Language and Environment for Statistical Computing
R Core Team (2000) · doi:10.32614/r.manuals · Cited by 355,893
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
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×
“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×
“, 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
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×
“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×
“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×
“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×
“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×
“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 1,429 · cited 2×
“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×
“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×
“, 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 1,128 · cited 1×
“, 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).”
Detection 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 1,085 · cited 3×
“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.”
InfluentialTiller, 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×
“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×
“…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).”
BackgroundMethodResultInfluentialCharif, D., & Lobry, J. R. (2007) · Biological and medical physics series · doi:10.1007/978-3-540-35306-5_10 · Cited by 941 · cited 1×
“, 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×
“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 756
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 744 · cited 1×
“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×
“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
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 587 · cited 1×
“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…”
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
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×
“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 542 · cited 4×
“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×
“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 432 · cited 1×
“, 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×
“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).”
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 235 · cited 3×
“Largely unmutated antibodies against SARS-CoV S (Prabakaran et al., 2006; Sui et al., 2004) and MERS-CoV S (Jiang et al.”
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×
“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.”
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×
“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×
“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 195 · cited 1×
“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×
“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 136 · cited 1×
“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×
“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
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
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
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×
“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×
“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
“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
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
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
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
Metadata
- 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
- Life Sciences › Immunology and Microbiology › Immunology › 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