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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.
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“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]
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Self-citationDurability of Immunity to SARS-CoV-2 and Other Respiratory Viruses
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“Reduced SHM has been seen in SARS-CoV-2 infection by others (Galson et al., 2020; Kreer et al., 2020; KuriCervantes et al., 2020; Nielsen et al., 2020; Schultheiß et al., 2020; Seydoux et al., 2020), and this is confirmed in our cohort (Figures 2A and S2A).”
InfluentialLagoumintzis, G., Chasapis, C. T., Alexandris, N., Kouretas, D., Tzartos, S. J., Eliopoulos, E., Farsalinos, K. E., & Poulas, K. A. (2021) · Food and Chemical Toxicology · doi:10.1016/j.fct.2021.112009 · Cited by 55
“Up to n w, several human Abs are found to recognize the SARS-CoV-2 S protein [30-45], however , cross-neutralizing Abs are rarely found in patients with COVID-19 [32,33,40,46].”
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“RBDspecific cells primarily include IgMIgD non-classswitched Bmem cells, and to a lesser extent, classswitched IgG Bmem cells.(11) Isolated antigenspecific Bmem cells were used as a source of Ig”
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“However, antibodies produced after SARS-CoV-2 infection inconsistently carry neutralizing activity (Seydoux et al., 2020).”
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“The neutralizing Abs have different epitopes, but many of them share the heavy-chain coding genes originating from similar germ lines of V-segments belonging to the VH3 family (VH3-23, VH3-30, VH3-53, or VH366), as well as VH169, VH2-70, and VH5-51 [16, 32, 135, 136, 138, 140, 142, 144, 145].”
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Otsubo, R., & Yasui, T. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108233 · Cited by 55
Variations within the Glycan Shield of SARS-CoV-2 Impact Viral Spike Dynamics
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“This provides a functional context for results of studies of SARS-CoV-2 S protein antibodies sequences from COVID-19 patients, which showed that no single clone dominates the antibody response; rather, a diverse collection of variable heavy- and light-chain genes are used in different individuals (Brouwer et al., 2020…”
Self-citationTranscriptomic Signature Differences Between SARS-CoV-2 and Influenza Virus Infected Patients
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“The CoVs which can infect humans (HCoVs) were classed into alpha and beta CoVs, especially the latter, such as HCoV-HKU1, HCoV-OC43, MERS-CoV, SARS-CoV, and SARS-CoV-2, pose serious health threats to human beings [66].”
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“Overall, the low levels of SHM across all the SARS-CoV-2-Article speci fi c B cells that we isolated is consistent with prior reports 13,23,29 and further demonstrates that the human immune system can readily generate antibodies capable of cross-binding multiple variants, regardless of infecting…”
InfluentialKumar, V. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2020.106980 · Cited by 42
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“reported SARS-CoV-2-specific mAbs have no or few somatic hypermutations [5,10,12].”
BackgroundAntibody Affinity Governs the Inhibition of SARS-CoV-2 Spike/ACE2 Binding in Patient Serum
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“…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; Robbiani et al., 2020; Rogers et al., 2020; Seydoux et al., 2020; Shi et al., 2020; Wec et al., 2020; Wu et al., 2020b; Zost et al., 2020).”
What could explain the late emergence of COVID-19 in Africa?
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“…in the generation of SARS-CoV-2 epitope-specific B cells (Galson et al., 2020; Kaneko et al., 2020; Kreer et al., 2020; Schultheiss et al., 2020; Seydoux et al., 2020;Woodruff et al., 2020) may be one of the determinants of the relatively short half-life of protective antibodies in this disease.”
Anti- SARS-CoV-2 Receptor Binding Domain Antibody Evolution after mRNA Vaccination
Cho, A., Muecksch, F., Schaefer-Babajew, D., Wang, Z., Finkin, S., Gaebler, C., Ramos, V., Cipolla, M., Mendoza, P., Agudelo, M., et al. (2021) · doi:10.1101/2021.07.29.454333 · Cited by 275
COVID-19 Immunobiology: Lessons Learned, New Questions Arise
Kaklamanos, A., Belogiannis, K., Skendros, P., Gorgoulis, V. G., Vlachoyiannopoulos, P. G., & Tzioufas, A. G. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.719023 · Cited by 37
“minimally mutated, suggesting a limited affinity maturation and, consequently, low binding affinity towards SARS-CoV-2 (131).”
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Nanoparticle and virus-like particle vaccine approaches against SARS-CoV-2
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“Structure 3 spike immunization are directed primarily against the N-terminal domain (NTD) or receptor-bindingdomain (RBD) on theS1 subunit of the trimeric viral surface spike glycoprotein (spike) (Barneset al., 2020; Brouwer et al., 2020; Cao et al., 2020; Cerutti et al., 2021; Ju et al., 2020; Liu et al., 2020; McCal…”
mRNA COVID-19 Vaccines and Long-Lived Plasma Cells: A Complicated Relationship
Giannotta, G., & Giannotta, N. (2021) · Vaccines · doi:10.3390/vaccines9121503 · Cited by 33
“Furthermore, in adult subjects, the persistence of BCRs that are specific for the spike protein and not excessively mutated [64] may allow early virus recognition and improve the anti-SARS-CoV-2 defense mechanisms.”
BackgroundEnhanced SARS-CoV-2 Neutralization by Secretory IgA in vitroPreprint
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. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.09.288555 · Cited by 35
Chan, M., Vijay, S., McNevin, J. P., McElrath, M. J., Holland, E. C., & Gujral, T. S. (2021) · Molecular Systems Biology · doi:10.15252/msb.202110426 · Cited by 33
“Consis-tently, treatment with CV30 (Seydoux et al , 2020) (a highly potent antibody targeting RBD of SARS-CoV-2) did not change S1 protein-induced expression of cytokines in PBMCs (Fig 1E).”
BackgroundSelf-citationFerrara, F., Erasmus, M. F., D’Angelo, S., Leal‐Lopes, C., Teixeira, A. A. R., Choudhary, A. K., Honnen, W. J., Calianese, D. C., Huang, D., Peng, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-021-27799-z · Cited by 36
Ortega, M. R., Spisak, N., Mora, T., & Walczak, A. M. (2023) · PLoS Genetics · doi:10.1371/journal.pgen.1010652 · Cited by 34
Korenkov, M., Zehner, M., Cohen‐Dvashi, H., Borenstein-Katz, A., Kottege, L., Janicki, H., Vanshylla, K., Weber, T., Gruell, H., Koch, M., et al. (2023) · Immunity · doi:10.1016/j.immuni.2023.11.004 · Cited by 36
Gorchakov, A. A., Kulemzin, S. V., Guselnikov, S. V., Baranov, K. O., Николаевна, Б. Т., Mechetina, L. V., Volkova, O. Y., Najakshin, A. M., Chikaev, N. A., Chikaev, A. N., et al. (2021) · Cell Discovery · doi:10.1038/s41421-021-00340-8 · Cited by 33
Wang, Z., Yang, X., Mei, X., Zhou, Y., Tang, Z., Li, G., Zhong, J., Yu, M., Huang, M., Su, X., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00978-0 · Cited by 33
“Seydoux et al.5 sequenced circulating antibodies and showed that only a few somatic mutations in potent neutralizing antibodies occurred within a SARS-CoV-2-infected individual.”
BackgroundZhou, X., Ma, F., Xie, J., Yuan, M., Li, Y., Shaabani, N., Zhao, F., Huang, D., Wu, N. C., Lee, C.-C. D., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109109 · Cited by 31
“(A) IGHV genes of SARS-CoV-2 neutralizing antibodies in this and other studies (Brouwer et al., 2020; Chi et al., 2020; Ju et al., 2020; Kreer et al., 2020; Pinto et al., 2020; Rogers et al., 2020; Seydoux et al., 2020; Shi et al., 2020; Wu et al., 2020b; Yuan et al., 2020b; Zost et al., 2020b).”
Jacob-Dolan, C., Feldman, J. E., McMahan, K., Yu, J., Zahn, R. C., Wegmann, F., Schuitemaker, H., Schmidt, A. G., & Barouch, D. H. (2021) · Journal of Virology · doi:10.1128/jvi.00117-21 · Cited by 32
“Current evidence suggests that RBD-directed antibodies are often potent neutralizing antibodies (21, 37, 38).”
BackgroundRecent advances in antibody‐based immunotherapy strategies for COVID‐19
Esmaeilzadeh, A., Rostami, S. M., Yeganeh, P. M., Tahmasebi, S., & Ahmadi, M. (2021) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30017 · Cited by 29
Wagner, A., Guzek, A., Ruff, J., Jasińska, J., Scheikl, U., Zwazl, I., Kundi, M., Stockinger, H. S. J., Farcet, M. R., Kreil, T. R., et al. (2021) · Communications Medicine · doi:10.1038/s43856-021-00012-4 · Cited by 28
Chen, J., Wang, B., Caserto, J. S., Shariati, K., Cao, P., Pan, Y., Xu, Q., & Ma, M. (2021) · Advanced Healthcare Materials · doi:10.1002/adhm.202101714 · Cited by 30
SARS -CoV-2 T-cell immunity to variants of concern following vaccinationPreprint
Gallagher, K., Leick, M. B., Larson, R. C., Berger, T. R., Katsis, K., Yam, J. Y., Brini, G., Grauwet, K., MGH COVID-19 Collection & Processing Team, & Maus, M. V. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.03.442455 · Cited by 32
Antibody Binding to SARS-CoV-2 S Glycoprotein Correlates with but Does Not Predict Neutralization
Ding, S., Laumaea, A., Benlarbi, M., Beaudoin-Bussières, G., Gasser, R., Medjahed, H., Pancera, M., Stamatatos, L., McGuire, A. T., Bazin, R., et al. (2020) · Viruses · doi:10.3390/v12111214 · Cited by 30
Self-citationSalzer, R., Clark, J. J., Vaysburd, M., Chang, V. T.-C., Albecka, A., Kiss, L., Sharma, P., Llamazares, A. G., Kipar, A., Hiscox, J. A., et al. (2021) · FEBS Letters · doi:10.1002/1873-3468.14171 · Cited by 31
Germinal center responses to SARS-CoV-2 mRNA vaccines in healthy and immunocompromised individuals
Lederer, K., Parvathaneni, K., Painter, M. M., Bettini, E., Agarwal, D., Lundgreen, K. A., Weirick, M., Goel, R. R., Xu, X., Drapeau, E. M., et al. (2021) · doi:10.1101/2021.09.16.21263686 · Cited by 179
“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).”
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) · CaltechAUTHORS (California Institute of Technology) · Cited by 29
Yuan, T. Z., Garg, P., Wang, L., Willis, J. R., Kwan, E., Hernandez, A. G. L., Tuscano, E., Sever, E. N., Rivera, E. K., Soto, C. S., et al. (2021) · mAbs · doi:10.1080/19420862.2021.2002236 · Cited by 31
Sholukh, A. M., Fiore-Gartland, A., Ford, E. S., Hou, Y., Tse, L.-P. V., Lempp, F., Kaiser, H., Germain, R. S., Bossard, E. L., Jia, J.-K., et al. (2020) · medRxiv · doi:10.1101/2020.12.07.20245431 · Cited by 25
“Alternatively, SARS-CoV-2 152 spike glycoprotein was produced as described elsewhere (23).”
MethodSelf-citationGraham, C., Seow, J., Huettner, I., Khan, H., Kouphou, N., Acors, S., Winstone, H., Pickering, S., Galao, R. P., Lista, M. J., et al. (2021) · doi:10.1101/2021.02.03.429355 · Cited by 27
Seroprevalence of SARS-CoV2 in IBD Patients Treated with Biologic Therapy
Bertè, R., Mazza, S., Stefanucci, M. R., Noviello, D., Costa, S., Ciafardini, C., Mileti, E., Mapelli, M., Pasqualato, S., Pinto, S. W. L., et al. (2020) · Journal of Crohn s and Colitis · doi:10.1093/ecco-jcc/jjaa237 · Cited by 27
“Humoral immune response against SARS-CoV2 proteins, including the receptor binding domain (RBD) of the spike (S) protein, leads the production of antibodies of different classes [6, 7].”
BackgroundTracking B cell responses to the SARS-CoV-2 mRNA-1273 vaccine
de Assis, F. L., Hoehn, K. B., Zhang, X., Kardava, L., Smith, C. D., Merhebi, O. E., Buckner, C. M., Trihemasava, K., Wang, W., Seamon, C. A., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112780 · Cited by 28
“61,62 Nonetheless, with the inclusion of oligo-tagged RBD and S1 within ADTs at the last two timepoints where there were enough cells to perform the ADT step post sort, we observed similar binding and temporal dynamics for the three spike proteins within MBC-C5.”
DNA-launched RNA replicon vaccines induce potent anti-SARS-CoV-2 immune responses in mice
Szurgot, I., Hanke, L., Sheward, D. J., Vidakovics, L. P., Murrell, B., McInerney, G. M., & Liljeström, P. (2021) · Scientific Reports · doi:10.1038/s41598-021-82498-5 · Cited by 26
Emerging Human Coronavirus Infections (SARS, MERS, and COVID-19): Where They Are Leading Us
Kumar, V. (2020) · International Reviews of Immunology · doi:10.1080/08830185.2020.1800688 · Cited by 29
“The non-neutralizing antibodies generate within the first week of the infection and target epitopes outside the RBD of the S protein to disrupt the SARSCoV2 S-ACE2 interaction without undergoing extensive maturation [357].”
BackgroundCrippling life support for SARS-CoV-2 and other viruses through synthetic lethality
Mast, F. D., Navare, A., van der Sloot, A. M., Coulombe‐Huntington, J., Rout, M. P., Baliga, N. S., Kaushansky, A., Chait, B. T., Aderem, A. A., Rice, C. M., et al. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202006159 · Cited by 25
“…and Pirofski, 2020; Casadevall et al., 2020), monoclonal antibodies cloned from COVID-19 patients (Liu et al., 2020a; Pinto et al., 2020; Robbiani et al., 2020; Rogers et al., 2020; Seydoux et al., 2020) and nanobodies, single-domain antibody fragments derived from the variable heavy domain”
BackgroundPaschold, L., Simnica, D., Willscher, E., Vehreschild, M. J. G. T., Dutzmann, J., Sedding, D., Schultheiß, C., & Binder, M. (2020) · Journal of Clinical Investigation · doi:10.1172/jci142966 · Cited by 26
Trimeric SARS-CoV-2 Spike Proteins Produced from CHO Cells in Bioreactors Are High-Quality Antigens
Pino, P., Kint, J., Kiseljak, D., Agnolon, V., Corradin, G., Kajava, A. V., Rovero, P., Dijkman, R., den Hartog, G., McLellan, J. S., et al. (2020) · Processes · doi:10.3390/pr8121539 · Cited by 28
Konrath, K. M., Liaw, K., Wu, Y., Zhu, X., Walker, S. N., Xu, Z., Schultheis, K., Chokkalingam, N., Chawla, H., Du, J., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110318 · Cited by 26
“…glycan variants, we utilized 14 RBD-directed nAbs, 2 Abs with inconsistent neutralization (Huo et al., 2020; Yuan et al., 2020b; Zhou et al., 2020a; Seydoux et al., 2020), and 6 non-nAbs (Hansen et al., 2020; Wu et al., 2020b; Seydoux et al., 2020; Shi et al., 2020; Rogers et al., 2020; Pinto et…”
The mutational dynamics of the SARS-CoV-2 virus in serial passages in vitro
Sonnleitner, S. T., Sonnleitner, S., Hinterbichler, E., Halbfurter, H., Kopecky, D. B. C., Koblmüller, S., Sturmbauer, C., Posch, W., & Walder, G. (2022) · Virologica Sinica · doi:10.1016/j.virs.2022.01.029 · Cited by 23
“Therefore, the spike protein represents the main target for neutralizing antibodies and thus is exposed to strong selective pressure (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., 2020; Wu et al., 2020; Zost et al., 2020; Verkhivker et…”
Converting non-neutralizing SARS-CoV-2 antibodies into broad-spectrum inhibitors
Weidenbacher, P. A. B., Waltari, E., Kobara, I. D. L. R., Bell, B. N., Morris, M. K., Cheng, Y.-C., Hanson, C. V., Pak, J. E., & Kim, P. S. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01140-1 · Cited by 23
Antibodies at work in the time of severe acute respiratory syndrome coronavirus 2
Sajna, K. V., & Kamat, S. (2020) · Cytotherapy · doi:10.1016/j.jcyt.2020.08.009 · Cited by 22
One-Stop Serum Assay Identifies COVID-19 Disease Severity and Vaccination Responses
Haddad, N. S., Nguyen, D. C., Kuruvilla, M. E., Morrison-Porter, A., Anam, F. A., Cashman, K. S., Ramonell, R. P., Kyu, S. Y., Saini, A. S., Cabrera-Mora, M., et al. (2021) · ImmunoHorizons · doi:10.4049/immunohorizons.2100011 · Cited by 29
Self-citationWendel, S., Fontão‐Wendel, R., Fachini, R. M., Candelaria, G. D. T. P., Scuracchio, P., Achkar, R., Brito, M., Reis, L. F. L., Camargo, A. A., Amano, M. T., et al. (2021) · Transfusion · doi:10.1111/trf.16323 · Cited by 21
Characterization of the SARS-CoV-2 Neutralization Potential of COVID-19–Convalescent Donors
Jahrsdörfer, B., Groß, R. M., Seidel, A., Wettstein, L., Ludwig, C., Schwarz, T., Körper, S., Rojewski, M., Lotfi, R., Weinstock, C., et al. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2100036 · Cited by 22
“It is known that most Abs produced against SARS-CoV-2 are not binding to the RBD of the spike protein (21).”
BackgroundSeow, J., Graham, C., Hallett, S. R., Lechmere, T., Maguire, T. J. A., Huettner, I., Cox, D., Khan, H., Pickering, S., Roberts, R., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110757 · Cited by 18
“…SARS-CoV-2-in-fected individuals, allowing identification of key neutralizing epitopes on Spike (Andreano et al., 2021a; Barnes et al., 2020; Brouwer et al., 2020; Graham et al., 2021; Piccoli et al., 2020; Robbiani et al., 2020; Rogers et al., 2020; Seydoux et al., 2020; Tortorici et al., 2020).”
Immune features of COVID-19 convalescent individuals revealed by a single-cell RNA sequencing
Zhao, P., Zou, J., Zhou, F., Zhu, Y., Song, Q., Yu, D., & Li, X. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.108767 · Cited by 21
Multi-omics for COVID-19: driving development of therapeutics and vaccines
Guo, M., Xiong, M., Peng, J., Guan, T., Su, H., Huang, Y., Yang, C., Li, Y., Boraschi, D., Pillaiyar, T., et al. (2023) · National Science Review · doi:10.1093/nsr/nwad161 · Cited by 24
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Cross-reactive sarbecovirus antibodies induced by mosaic RBD nanoparticles
Fan, C., Keeffe, J. R., Malecek, K. E., Cohen, A. A., West, A. P., Baharani, V. A., Rorick, A. V., Gao, H., Gnanapragasam, P. N. P., Rho, S., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2501637122 · Cited by 23
“…- SARS - 2 mAbs have been isolated from infected and/or immunized human donors ( 78 ), in whom immune responses generally focus on the immunodominant, but variable, class 1 and class 2 RBD regions ( 4 – 8 , 11 , 12 , 21 – 25 ), thus usually resulting in mAbs that are sensitive to VOC substitutions.”
Takano, T., Sato, T., Kotaki, R., Moriyama, S., Fukushi, S., Shinoda, M., Kabasawa, K., Shimada, N., Kousaka, M., Adachi, Y., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37128-1 · Cited by 26
Drug discovery and development targeting the life cycle of SARS-CoV-2
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Bell, B. N., Powell, A. E., Rodríguez, C., Cochran, J. R., & Kim, P. S. (2021) · Protein Science · doi:10.1002/pro.4044 · Cited by 18
Kombe, A. J. K., Zahid, A., Mohammed, A., Shi, R., & Jin, T. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.670815 · Cited by 19
Schuster, D. J., Karuna, S., Brackett, C., Wesley, M. S., Li, S. S., Eisel, N., Tenney, D., Hilliard, S., Yates, N. L., Heptinstall, J., et al. (2022) · JCI Insight · doi:10.1172/jci.insight.158402 · Cited by 20
“Monoclonal antibodies CV23 IgG1 and CV30 IgG1 (40) and CR3022 IgG1 served as positive controls, while CH65 IgG1 served as a negative control (41).”
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
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