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.”
BackgroundResultInfluential
Flagged first, then by citations
1 of the 44 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 201–300 of 369
The ACE2-binding Interface of SARS-CoV-2 Spike Inherently Deflects Immune Recognition
Hattori, T., Koide, A., Noval, M. G., Panchenko, T., Romero, L. A., Teng, K. W., Tada, T., Landau, N. R., Stapleford, K. A., & Koide, S. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.166748 · Cited by 20
“The structure and conformational dynamics of the spike protein offer possible mechanistic basis for the low immunogenicity of the RBD.”
InfluentialVaisman‐Mentesh, A., Dror, Y., Tur‐Kaspa, R., Markovitch, D., Kournos, T., Dicker, D., & Wine, Y. (2020) · medRxiv · doi:10.1101/2020.08.23.20179796 · Cited by 20
Serwanga, J., Ankunda, V., Sembera, J., Kato, L., Oluka, G. K., Baine, C., Odoch, G., Kayiwa, J. T., Auma, B. O., Jjuuko, M., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1152522 · Cited by 20
Adams, L. J., VanBlargan, L. A., Liu, Z., Gilchuk, P., Zhao, H., Chen, R. E., Raju, S., Chong, Z., Whitener, B. M., Shrihari, S., et al. (2023) · Cell Reports Medicine · doi:10.1016/j.xcrm.2023.101305 · Cited by 18
Benning, L., Klein, K., Morath, C. P., Bartenschlager, M., Kim, H., Buylaert, M., Reineke, M., Töllner, M., Nußhag, C., Kälble, F., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.840136 · Cited by 18
Mulchandani, R., Taylor-Philips, S., Jones, H. E., Ades, A. E., Borrow, R., Linley, E., Kirwan, P., Stewart, R., Moore, P., Boyes, J., et al. (2021) · Journal of Infection · doi:10.1016/j.jinf.2021.03.019 · Cited by 18
de Campos‐Mata, L., Vaquero, S. T., Tachó‐Piñot, R., Piñero, J., Grasset, E. K., Arrieta‐Aldea, I., Melero, N. R., Carolis, C., Horcajada, J. P., Cerutti, A., et al. (2021) · Clinical & Translational Immunology · doi:10.1002/cti2.1339 · Cited by 17
“The median length of stay from hospitalization to discharge was 16 days [5-90].”
Neutralizing Antibodies to SARS‐CoV‐2 Selected from a Human Antibody Library Constructed Decades Ago
Qiang, M., Ma, P., Li, Y., Liu, H., Harding, A. C., Min, C., Wang, F., Liu, L., Yuan, M., Ji, Q., et al. (2021) · Advanced Science · doi:10.1002/advs.202102181 · Cited by 20
Mustapha, J. O., Abdullahi, I. N., Ajagbe, O., Emeribe, A. U., Fasogbon, S. A., Onoja, S. O., Ugwu, C. E., Umeozuru, C. M., Ajayi, F. O., Tanko, W. N., et al. (2021) · Heliyon · doi:10.1016/j.heliyon.2021.e05951 · Cited by 17
RetractedStructural Analysis of the Novel Variants of SARS-CoV-2 and Forecasting in North America
Quinonez, E., Vahed, M., Shahraki, A. H., & Mirsaeidi, M. S. (2021) · Viruses · doi:10.3390/v13050930 · Cited by 16
“The neutralizing monoclonal CV30 antibody was isolated from a patient infected with SARS-CoV-2, in complex with the receptor S-RBD [28].”
BackgroundAiello, A., Grossi, A., Meschi, S., Meledandri, M., Vanini, V., Petrone, L., Casetti, R., Cuzzi, G., Salmi, A., Altera, A. M. G., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.920227 · Cited by 18
“Pool M responders [N (% among positive Tcell responders)] 1 (25) 2 (100) 3(50) 4 (57.”
Protein nanoparticle vaccines induce potent neutralizing antibody responses against MERS-CoV
Chao, C. W., Sprouse, K. R., Miranda, M. C., Catanzaro, N., Hubbard, M. L., Addetia, A., Stewart, C., Brown, J. T., Dosey, A. M., Valdez, A., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.115036 · Cited by 18
Self-citationLi, N., Zhao, B., Stavins, R. A., Peinetti, A. S., Chauhan, N., Bashir, R., Cunningham, B. T., King, W. P., Lu, Y., Wang, X., et al. (2021) · Current Opinion in Solid State and Materials Science · doi:10.1016/j.cossms.2021.100966 · Cited by 17
Schultz, M. D., Suschak, J. J., Botta, D., Silva-Sánchez, A., King, R. G., Detchemendy, T. W., Meshram, C. D., Foote, J. B., Zhou, F., Tipper, J. L., et al. (2022) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2022.2127292 · Cited by 16
Mosaic nanoparticles elicit cross-reactive immune responses to zoonotic coronaviruses in micePreprint
Cohen, A. A., Gnanapragasam, P. N. P., Lee, Y. E., Hoffman, P. R., Ou, S., Kakutani, L. M., Keeffe, J. R., Wu, H.-J., Howarth, M. R., West, A. P., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.17.387092 · Cited by 19
“Consistent with its function in viral entry, S is the primary target of neutralizing antibodies (13-22), with many targeting the RBD (14-18, 21-26).”
Gayvert, K. M., McKay, S., Lim, W. K., Baum, A., Kyratsous, C. A., Copin, R., & Atwal, G. S. (2023) · npj Viruses · doi:10.1038/s44298-023-00007-z · Cited by 17
Rubio, A. A., Baharani, V. A., Dadonaite, B., Parada, M., Abernathy, M. E., Wang, Z., Lee, Y. E., Eso, M. R., Phung, J. L., Ramos, I., et al. (2025) · Science Translational Medicine · doi:10.1126/scitranslmed.adq5720 · Cited by 21
Cheng, Z. J., Li, B., Zhan, Z., Zhao, Z., Xue, M., Zheng, P., Lyu, J., Hu, C., He, J., Chen, R., et al. (2022) · Clinical Reviews in Allergy & Immunology · doi:10.1007/s12016-021-08912-y · Cited by 15
Advances in antibody discovery from human BCR repertoires
Xu, Z., Ismanto, H. S., Zhou, H., Saputri, D. S., Sugihara, F., & Standley, D. M. (2022) · Frontiers in Bioinformatics · doi:10.3389/fbinf.2022.1044975 · Cited by 18
Frequent use of IGHV3-30-3 in SARS-CoV-2 neutralizing antibody responses
Pushparaj, P., Nicoletto, A., Dopico, X. C., Sheward, D. J., Kim, S., Ekström, S., Murrell, B., Corcoran, M., & Hedestam, G. B. K. (2023) · Frontiers in Virology · doi:10.3389/fviro.2023.1128253 · Cited by 16
“Several antibodies that use these genes bind and neutralize the virus even in their germline state, suggesting a role for the germline-encoded residues in epitope binding (17).”
BackgroundDeciphering Fc-effector functions against SARS-CoV-2
Beaudoin-Bussières, G., & Finzi, A. (2024) · Trends in Microbiology · doi:10.1016/j.tim.2024.01.005 · Cited by 19
Smith, I., Callum, G. J. M., Sabljic, A. V., Marfía, J. I., Bombicino, S. S., Trabucchi, A., Iacono, R. F., Birenbaum, J. M., Vázquez, S., Minoia, J. M., et al. (2021) · Biotechnology and Bioengineering · doi:10.1002/bit.27889 · Cited by 15
SARS-CoV-2 S2P spike ages through distinct states with altered immunogenicity
Olia, A. S., Tsybovsky, Y., Chen, S. J., Liu, C., Nazzari, A. F., Ou, L., Wang, L., Kong, W., Leung, K., Liu, T. W. B., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101127 · Cited by 14
New insights into human immune memory from SARS‐CoV ‐2 infection and vaccination
Hartley, G. E., Edwards, E. S. J., O’Hehir, R. E., & van Zelm, M. C. (2022) · Allergy · doi:10.1111/all.15502 · Cited by 15
Jayaraj, J. M., Jothimani, M., Palanisamy, C. P., Pentikäinen, O. T., Pannipara, M., Al-Sehemi, A. G., Muthusamy, K., & Gopinath, K. (2022) · Bioinorganic Chemistry and Applications · doi:10.1155/2022/8635054 · Cited by 14
“civet cats, swine, cats, ferrets, nonhuman primates (NHPs), and humans as a receptor [4, 5].”
BackgroundRetractedThe role of inflammatory gene polymorphisms in severe COVID-19: a review
Yip, J. Q., Oo, A., Ng, Y. L., Chin, K. L., Tan, K., Chu, J. J. H., AbuBakar, S., & Zainal, N. (2024) · Virology Journal · doi:10.1186/s12985-024-02597-3 · Cited by 15
The development of neutralizing antibodies against SARS-CoV-2 and their common features
Liu, L. D., Lian, C., Yeap, L.-S., & Meng, F. (2020) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjaa070 · Cited by 14
“CV30, which shows only 2-amino acid difference from the germline sequence have increased binding affinity by 100-fold (Hurlburt et al., 2020).”
BackgroundInfluentialWhaley, R. E., Ameny, S., Arkatkar, T., Seese, A. M., Wall, A., Khan, I., Carter, J. J., Scherer, E. M., Rawlings, D. J., Galloway, D. A., et al. (2020) · Journal of Immunological Methods · doi:10.1016/j.jim.2020.112901 · Cited by 14
“Importantly, the rapid isolation of mAbs is a powerful method that can be used to understand the human immune response to infection in the context of rapidly emerging infections, such as the current COVID-19 pandemic (Pinto et al., 2020; Traggiai et al., 2004; Seydoux et al., 2020; Ju et al., 2020; Shi et al., 2020).”
Self-citationAbernathy, M. E., Dam, K.-M. A., Esswein, S. R., Jette, C. A., & Björkman, P. J. (2021) · Viruses · doi:10.3390/v13102106 · Cited by 12
Moustafa, R. I., Faraag, A. H. I., El‐Shenawy, R., Agwa, M. M., & Elsayed, H. (2023) · Saudi Journal of Biological Sciences · doi:10.1016/j.sjbs.2023.103661 · Cited by 14
“…were discovered in the sera of COVID-19 convalescent individuals (Ni et al., 2020), and antibodies targeting the S-protein, isolated from SARS-CoV-2 diseased patients, exhibited neutralizing potency and hence might be protective against reinfection (Seydoux et al., 2020; Suthar et al., 2020).”
Florova, M., Abreu-Mota, T., Paesen, G. C., Beetschen, A. S., Cornille, K., Marx, A., Narr, K., Sahin, M., Dimitrova, M., Swarnalekha, N., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2318657121 · Cited by 13
Diociaiuti, A., Giancristoforo, S., Terreri, S., Corbeddu, M., Concato, C., Atti, M. L. C. D., Zambruno, G., Carsetti, R., & Hachem, M. E. (2020) · Journal of the European Academy of Dermatology and Venereology · doi:10.1111/jdv.16934 · Cited by 12
Ilinykh, P. A., Periasamy, S., Huang, K., Kuzmina, N. A., Ramanathan, P., Meyer, M. N., Mire, C. E., Kuzmin, I. V., Bharaj, P., Endsley, J. R., et al. (2022) · npj Vaccines · doi:10.1038/s41541-022-00471-3 · Cited by 14
Ghotloo, S., Maghsood, F., Golsaz‐Shirazi, F., Amiri, M. M., Moog, C., & Shokri, F. (2022) · Reviews in Medical Virology · doi:10.1002/rmv.2347 · Cited by 13
Broadly neutralizing human antibodies against Omicron subvariants of SARS-CoV-2
Chiang, H.-L., Liang, K.-H., Lu, R., Kuo, T.-W., Lin, Y., & Wu, H. (2023) · Journal of Biomedical Science · doi:10.1186/s12929-023-00955-x · Cited by 12
“Typically, the RBD-specific neutralizing antibodies isolated during early convalescence exhibit very limited or even no SHM [22, 30, 37, 53].”
BackgroundInfluentialGuerra, D., Beaumont, T., Radić, L., Kerster, G., van der Straten, K., Yuan, M., Torres, J. L., Lee, W.-H., Liu, H., Poniman, M., et al. (2023) · iScience · doi:10.1016/j.isci.2023.108009 · Cited by 13
Li, W., Wang, F., Li, Y., Yan, L., Liu, L., Zhu, W., Ma, P., Shi, X., & Yang, G. (2023) · Vaccines · doi:10.3390/vaccines11040771 · Cited by 11
Gruca, A., Ziemska-Legięcka, J., Jarnot, P., Sarnowska, E. A., Sarnowski, T. J., & Grynberg, M. (2021) · BMC Bioinformatics · doi:10.1186/s12859-021-04017-7 · Cited by 11
Diamanti, A. P., Rosado, M. M., Nicastri, E., Sesti, G., Pioli, C., & Laganà, B. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.708848 · Cited by 11
A Novel Mathematical Model That Predicts the Protection Time of SARS-CoV-2 Antibodies
Xu, Z., Wei, D., Zhang, H., & Jacques Demongeot, A. (2023) · Viruses · doi:10.3390/v15020586 · Cited by 12
Validation of Ligand Tetramers for the Detection of Antigen-Specific Lymphocytes
Fitzpatrick, K. S., Degefu, H. N., Poljakov, K., Bibby, M. G., Remington, A. J., Searles, T. G., Gray, M. D., Boonyaratanakornkit, J. B., Rosato, P. C., & Taylor, J. J. (2023) · The Journal of Immunology · doi:10.4049/jimmunol.2200934 · Cited by 12
Beaudoin-Bussières, G., Chen, Y.-Z., Ullah, I., Prévost, J., Tolbert, W., Symmes, K., Ding, S.-L., Benlarbi, M., Gong, S., Tauzin, A., et al. (2021) · bioRxiv · doi:10.1101/2021.09.08.459408 · Cited by 15
Self-citationYan, Q., Zhang, Y., Hou, R., Pan, W., Liang, H., Gao, X., Deng, W., Huang, X., Qu, L., Tang, C., et al. (2023) · Emerging Microbes & Infections · doi:10.1080/22221751.2023.2290841 · Cited by 9
“The most common clonotype cl.142, and two other clonotypes cl.143 and cl.144, encoded by IGHV3-30, are S2-targeting non-neutralizing antibody lineages [34] (Figure 4A and C; Figure S6).”
BackgroundCOVID-19 antibody development fueled by HIV-1 broadly neutralizing antibody research
Mendoza, P., Lorenzi, J. C. C., & Gaebler, C. (2020) · Current Opinion in HIV and AIDS · doi:10.1097/coh.0000000000000657 · Cited by 10
No substantial preexisting B cell immunity against SARS-CoV-2 in healthy adults
Ercanoglu, M. S., Gieselmann, L., Dähling, S., Poopalasingam, N., Detmer, S., Koch, M., Korenkov, M., Halwe, S., Klüver, M., Cristanziano, V. D., et al. (2022) · iScience · doi:10.1016/j.isci.2022.103951 · Cited by 9
Detection of SARS‐CoV‐2‐specific memory B cells to delineate long‐term COVID‐19 immunity
Thieme, C. J., Abou‐El‐Enein, M., Fritsche, E., Anft, M., Paniskaki, K., Skrzypczyk, S., Doevelaar, A., Elsallab, M., Brindle, N. R., Blazquez‐Navarro, A., et al. (2021) · Allergy · doi:10.1111/all.14827 · Cited by 10
Leach, A., Miller, A., Bentley, E. M., Mattiuzzo, G., Thomas, J. C., McAndrew, C., van Montfort, R., & Rabbitts, T. H. (2021) · Scientific Reports · doi:10.1038/s41598-021-89887-w · Cited by 11
Sulbarán, G., Maisonnasse, P., Amen, A., Effantin, G., Guilligay, D., Dereuddre‐Bosquet, N., Burger, J. A., Poniman, M., Grobben, M., Buisson, M., et al. (2022) · Cell Reports Medicine · doi:10.1016/j.xcrm.2022.100528 · Cited by 11
But does it work? Improving evaluations of sexuality education.
Haffner, D. W., & Goldfarb, E. S. (1997) · PubMed · Cited by 10
Elizaldi, S. R., Lakshmanappa, Y. S., Roh, J. W., Schmidt, B., Carroll, T. D., Weaver, K. D., Smith, J. C., Deere, J., Dutra, J. C., Stone, M., et al. (2020) · bioRxiv · doi:10.1101/2020.07.07.191007 · Cited by 10
Corcoran, M., Narang, S., Kaduk, M., Chernyshev, M., Färnert, A., Sundling, C., & Hedestam, G. B. K. (2026) · Immunity · doi:10.1016/j.immuni.2026.01.026 · Cited by 10
Inada, M., Ishikane, M., Terada, M., Matsunaga, A., Maeda, K., Tsuchiya, K., Miura, K., Sairenji, Y., Kinoshita, N., Ujiie, M., et al. (2021) · Journal of Infection and Chemotherapy · doi:10.1016/j.jiac.2021.04.017 · Cited by 9
Younes, N., Al‐Sadeq, D. W., Shurrab, F. M., Zedan, H. T., Abou-Saleh, H., Halawa, B. Y. A., AlHamaydeh, F. M., Elsharafi, A. E., Daas, H. I., Thomas, S., et al. (2022) · Vaccines · doi:10.3390/vaccines10081318 · Cited by 9
Antibodies, epicenter of SARS-CoV-2 immunology
Pecetta, S., Pizza, M., Sala, C., Andreano, E., Pileri, P., Troisi, M., Pantano, E., Manganaro, N., & Rappuoli, R. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-020-00711-w · Cited by 9
“These observations are supported by studies that investigated the DNA sequences of the genes encoding the circulating antibodies and showed that neutralizing antibodies are only few mutations distant from their respective germline sequence, suggesting absence of affinity maturation in germinal centers and low capacity…”
INFECTION-ACQUIRED VERSUS VACCINE-INDUCED IMMUNITY AGAINST COVID-19
Velikova, T. V. (2021) · Central Asian Journal of Medical Hypotheses and Ethics · doi:10.47316/cajmhe.2021.2.1.05 · Cited by 9
Antibody Display of cell surface receptor Tetraspanin12 and SARS-CoV-2 spike proteinPreprint
Hsieh, F.-L., & Chang, T.-H. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.29.446300 · Cited by 9
Wang, J., Ni, S., Chen, Q., Wang, C., Liu, H., Huang, L., Nasir, M. W., Wang, W. J., Zhang, X., Wu, J., et al. (2024) · Journal of Medical Virology · doi:10.1002/jmv.70073 · Cited by 8
“Other germlines, such as IGHV1 ‐ 69 [43, 44] and IGHV3 ‐ 30 [43], also generate antibodies that recognize different viral components.”
The immunological impact of revaccination in a hybrid-immune world
Bausch-Jurken, M. T., & Alter, G. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1588259 · Cited by 11
Structural basis of spike RBM-specific human antibodies counteracting broad SARS-CoV-2 variants
Shitaoka, K., Higashiura, A., Kawano, Y., Yamamoto, A., Mizoguchi, Y., Hashiguchi, T., Nishimichi, N., Huang, S., Ito, A., Ohki, S., et al. (2023) · Communications Biology · doi:10.1038/s42003-023-04782-6 · Cited by 9
RISK-TAKING BEHAVIOR IN RECOVERED COVID-19 PATIENTS
EGELİ, A., Adıgüzel, S., Kapıcı, Y., Güc, B., Tekin, A. Y., Private Psychological Counselor, A., & Tekın, A. (2021) · Psychiatria Danubina · doi:10.24869/psyd.2021.107 · Cited by 7
“Moreover, some studies have shown recovered patients produce antibodies and this may lead them to a favorable position in a reinfection circumstance (Ni et al. 2020, Seydoux et al. 2020).”
BackgroundZhu, X., Yu, F., Wu, Y., & Ying, T. (2021) · Antibody Therapeutics · doi:10.1093/abt/tbab008 · Cited by 8
“[64] isolated 45 S-specific mAbs from a COVID-19-infected individual 21 days post the onset of clinical disease.”
BackgroundAkhtar, M., Basher, S. R., Nizam, N. N., Kamruzzaman, M., Khaton, F., Banna, H. A., Kaisar, M. H., Karmakar, P. C., Hakim, A., Akter, A., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1052374 · Cited by 8
Isolation and Characterization of Cross-Neutralizing Coronavirus Antibodies from COVID-19+ SubjectsPreprint
Jennewein, M. F., MacCamy, A. J., Akins, N. R., Feng, J., Homad, L. J., Hurlburt, N. K., Seydoux, E., Wan, Y.-H., Stuart, A. B., Edara, V. V., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.23.436684 · Cited by 9
Self-citationAlenquer, M., Ferreira, F., Lousa, D., Valério, M., Medina-Lopes, M., Bergman, M., Gonçalves, J., Demengeot, J., Leite, R. B., Lilue, J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.22.441007 · Cited by 8
Rochman, N. D., Faure, G., Wolf, Y. I., Freddolino, P. L., Zhang, F., & Koonin, E. V. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.08.30.458225 · Cited by 8
Mosaic RBD nanoparticles protect against multiple sarbecovirus challenges in animal modelsPreprint
Cohen, A. A., van Doremalen, N., Greaney, A. J., Andersen, H., Sharma, A., Starr, T. N., Keeffe, J., Fan, C.-H., Schulz, J. E., Gnanapragasam, P. N. P., et al. (2022) · bioRxiv · doi:10.1101/2022.03.25.485875 · Cited by 5
“Many of the most potent neutralizing antibodies against SARS-2 block binding ACE2 to the RBD (16-20, 23-29), and RBD targeting”
Broad‐Spectrum Engineered Multivalent Nanobodies Against SARS‐CoV‐1/2
Wang, Z., Shi, Z., Liao, X., Quan, G., Dong, H., Zhao, P., Zhou, Y., Shi, N., Wang, J., Wu, Y., et al. (2024) · Advanced Science · doi:10.1002/advs.202402975 · Cited by 8
Self-citationLv, H., Tsang, O. T., So, R. T. Y., Wang, Y., Yuan, M., Liu, H., Yip, G. K., Teo, Q. W., Lin, Y., Liang, W., et al. (2021) · European Journal of Immunology · doi:10.1002/eji.202149234 · Cited by 6
Sokullu, E., Pinard, M., Gauthier, M., & Coulombe, B. (2021) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2021.1909566 · Cited by 7
Ueno, M., Iwata‐Yoshikawa, N., Matsunaga, A., Okamura, T., Saito, S., Ashida, S., Yoshida, I., Nagashima, M., Asakura, H., Yaoita, Y., et al. (2022) · Antiviral Research · doi:10.1016/j.antiviral.2022.105297 · Cited by 7
“Potent RBD-specific 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; Robbiani et al., 2020; Rogers et al., 2020; Seydoux et al., 2020; Shi et al., 2020; Wec et al., 2020; Wu et al., 2020b; Zos…”
Bartlett, M. L., Suwanmanee, S., Akindele, N. P., Ghimire, S., Chan, A. K. P., Guo, C., Gould, S. J., Cox, A. L., & Griffin, D. E. (2022) · Viral Immunology · doi:10.1089/vim.2021.0191 · Cited by 7
“Despite a lack of germinal center processing and somatic hypermutation for these ASCs, previous studies have shown that the rapid S-specific response includes cells producing potent virus neutralizing antibody likely to be important for early virus control (41,72).”
Kulemzin, S. V., Sergeeva, M. V., Baranov, K. O., Gorchakov, A. A., Guselnikov, S. V., Николаевна, Б. Т., Volkova, O. Y., Najakshin, A. M., Chikaev, N. A., Danilenko, D., et al. (2022) · Journal of Personalized Medicine · doi:10.3390/jpm12060895 · Cited by 7
“Recombinant CV30 was produced in-house based on the published sequences [14].”
MethodInfluentialEffects of Prior Infection with SARS-CoV-2 on B Cell Receptor Repertoire Response during Vaccination
Fraley, E., Khanal, S., Pierce, S. H., LeMaster, C., McLennan, R., Pastinen, T., & Bradley, T. (2022) · Vaccines · doi:10.3390/vaccines10091477 · Cited by 8
“, no mutations) have been observed early in naïve response to SARS-CoV-2 infection [31].”
BackgroundMüller, K., Girl, P., Ruhnke, M., Spranger, M., Kaier, K., von Buttlar, H., Dobler, G., & Borde, J. (2021) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph18083910 · Cited by 7
Qiang, M., Ma, P., Li, Y., Liu, H., Harding, A. C., Min, C., Liu, L., Yuan, M., Ji, Q., Tao, P., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.06.370676 · Cited by 7
“CoV-2 convalescent patients contain only a few amino-acid mutations (3, 8, 9, 36, 37).”
BackgroundElevated SARS-CoV-2 Antibodies Distinguish Severe Disease in Early COVID-19 InfectionPreprint
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. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.04.410589 · Cited by 7
Regulators and Conductors of Immunity: Natural Immune System in Health and Autoimmunity
Böröcz, K., Szinger, D., Simon, D., Berki, T., & Németh, P. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26115413 · Cited by 9
Chuang, G., Shen, C., Cheung, C. S., Gorman, J., Creanga, A., Joyce, M. G., Leung, K., Rawi, R., Wang, L., Yang, E. S., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.662909 · Cited by 6
The characteristics of BCR‐CDR3 repertoire in COVID‐19 patients and SARS‐CoV‐2 vaccinated volunteers
Xiao, J., Luo, Y. Q., Li, Y., & Yao, X. (2024) · Journal of Medical Virology · doi:10.1002/jmv.29488 · Cited by 6
“15,16 Innate immunity may play a significant role in mild or asymptomatic infection; 17 its failure and/or acquired immunity development would cause pathological damage to the severe infection individual.”
BackgroundTherapeutic and Vaccine Options for COVID-19: Status after Six Months of the Disease Outbreak
Maciorowski, D., Ogaugwu, C., Durvasula, S. R., Durvasula, R. V., & Kunamneni, A. (2020) · SLAS DISCOVERY · doi:10.1177/2472555220979579 · Cited by 6
Tjan, L. H., Nagano, T., Furukawa, K., Nishimura, M., Arii, J., Fujinaka, S., Iwata, S., Sano, S., Tohma, Y., Nishimura, Y., et al. (2021) · JMA Journal · doi:10.31662/jmaj.2020-0083 · Cited by 6
“Similarly, it has been reported that the neutralizing antibody titer detected in a young man with mild SARS-CoV-2 infection rapidly increased from day 4 until day 20 ((22)).”
BackgroundFocosi, D., Maggi, F., Franchini, M., Aguzzi, A., Lanza, M., Mazzoni, A., & Menichetti, F. (2021) · Clinical Microbiology and Infection · doi:10.1016/j.cmi.2021.04.003 · Cited by 6
SARS-CoV-2 Epitopes following Infection and Vaccination Overlap Known Neutralizing Antibody Sites
Yang, L., Liang, T., Pierson, L. M., Wang, H., Fletcher, J. K., Wang, S., Bao, D., Zhang, L., Huang, Z. J., Zheng, W., et al. (2022) · Research · doi:10.34133/2022/9769803 · Cited by 7
Lunderberg, J. M., Dutta, S., Collier, A.-R. Y., Lee, J.-S., Hsu, Y., Wang, Q., Zheng, W., Hao, S., Zhang, H., Feng, L., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1032574 · Cited by 7
Zhu, W., Zheng, Y., Yu, M., Wei, J., Zhang, Y., Topchyan, P., Nguyen, C. P., Janecke, R., Kreuziger, L. B., White, G. C., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-462080/v1 · Cited by 6
Piccoli, L., Park, Y.-J., Tortorici, M. A., Czudnochowski, N., Walls, A. C., Beltramello, M., Silacci-Fregni, C., Pinto, D., Rosen, L. E., Bowen, J. E., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.037 · Cited by 1,395
Optical Detection of SARS-CoV-2 Utilizing Antigen-Antibody Binding Interactions
Ahmad, M. A., Mustafa, F., Panicker, N. G., & Rizvi, T. A. (2021) · Sensors · doi:10.3390/s21196596 · Cited by 5
Monoclonal antibodies: a remedial approach to prevent SARS-CoV-2 infection
Kumar, S., Dutta, D., Ravichandiran, V., & Sukla, S. (2022) · 3 Biotech · doi:10.1007/s13205-022-03281-5 · Cited by 5
How Protective are Antibodies to SARS-CoV-2, the Main Weapon of the B-Cell Response?
Pons, S., Uhel, F., Frapy, E., Sérémé, Y., Zafrani, L., Aschard, H., & Skurnik, D. (2022) · Stem Cell Reviews and Reports · doi:10.1007/s12015-022-10477-y · Cited by 6
“Only two antibodies seemed to efficiently neutralize the virus with the more potent directed against the RBD, suggesting that monoclonal antibodies targeting the RBD could be more efficient in preventing or treating SARS-CoV-2 infection [54].”
BackgroundAguilar, R., Li, X., Crowell, C. S., Burrell, T., Vidal, M., Rubio, R., Jiménez, A., Hernández-Luis, P., Hofmann, D., Mijočević, H., et al. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.03165-22 · Cited by 5
“This is not surprising, as much of the immunodominant response associated with neutralization involves binding and/or blocking the S RBD to inhibit viral entry to host cells (12, 14).”
BackgroundFiedler, S., Piziorska, M. A., Denninger, V., Morgunov, A., Ilsley, A., Malik, A. Y., Schneider, M. M., Devenish, S., Meisl, G., Aguzzi, A., et al. (2020) · bioRxiv · doi:10.1101/2020.12.20.422820 · Cited by 4
B Cell Receptor Repertoire Kinetics after SARS-CoV-2 Infection and VaccinationPreprint
Kotagiri, P., Mescia, F., Rae, W. M., Bergamaschi, L., Tuong, Z. K., Turner, L., Hunter, K., Gerber, F. P. P., Hosmillo, M. D. T., Hess, C., et al. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3910805 · Cited by 5
Barroso‐Arévalo, S., Sánchez‐Morales, L., Domínguez, M., García‐Seco, T., Risalde, M. Á., García‐Bocanegra, I., Domı́nguez, L., & Sánchez‐Vizcaíno, J. M. (2022) · Research in Veterinary Science · doi:10.1016/j.rvsc.2022.05.003 · Cited by 4
Development of SARS‐CoV‐2 animal vaccines using a stable and efficient NDV expression system
He, L., Zhong, J., Li, G., Lin, Z., Zhao, P., Yang, C., Wang, H., Zhang, Y., Yang, X., & Wang, Z. (2022) · Journal of Medical Virology · doi:10.1002/jmv.28237 · Cited by 4
“With the coordination of humoral and cellular immunity, antibodies, especially neutralizing antibodies, can be maintained for a long period according to several studies.(33,34) Memory B cells require T follicular helper cells to transmit signals to facilitate preferential”
Background多賀谷, 悦., Kikuchi, K., Mitsuda, T., Ebihara, F., Maruyama, T., Hamada, Y., Kimura, T., Unagami, K., Kanzawa, T., Sekiguchi, H., et al. (2022) · Transplant Immunology · doi:10.1016/j.trim.2022.101777 · Cited by 5
A Testimony of the Surgent SARS-CoV-2 in the Immunological Panorama of the Human Host
Minakshi, R., Jan, A. T., Rahman, S., & Kim, J. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.575404 · Cited by 4
Neutralizing monoclonal antibodies against highly pathogenic coronaviruses
Xiang, R., Wang, Y., Wang, L., Deng, X., Huo, S., Jiang, S., & Yu, F. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.12.015 · Cited by 4
Boldova, A. E., Korobkin, J.-J. D., Nechipurenko, Y. D., & Sveshnikova, A. N. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911364 · Cited by 4
Machine Learning Identifies Ponatinib as a Potent Inhibitor of SARS-CoV2-induced Cytokine StormPreprint
Chan, M., Vijay, S., McElrath, M. J., Holland, E. C., & Gujral, T. S. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.07.438871 · Cited by 4
Self-citationYuan, S., Jiang, S., Zhang, Z., Fu, Y., Yang, X., Li, Z.-L., Hu, J., Du, J., Yuan, M., & Chen, Y. (2022) · Journal of Infection · doi:10.1016/j.jinf.2022.04.033 · Cited by 4
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