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Identification of SARS-CoV-2 spike mutations that attenuate monoclonal and serum antibody neutralization
Open accessAbstract
Neutralizing antibodies against the SARS-CoV-2 spike (S) protein are a goal of COVID-19 vaccines and have received emergency use authorization as therapeutics. However, viral escape mutants could compromise efficacy. To define immune-selected mutations in the S protein, we exposed a VSV-eGFP-SARS-CoV-2-S chimeric virus, in which the VSV glycoprotein is replaced with the S protein, to 19 neutralizing monoclonal antibodies (mAbs) against the receptor-binding domain (RBD) and generated 50 different escape mutants. Each mAb had a unique resistance profile, although many shared residues within an epitope of the RBD. Some variants (e.g., S477N) were resistant to neutralization by multiple mAbs, whereas others (e.g., E484K) escaped neutralization by convalescent sera. Additionally, sequential selection identified mutants that escape neutralization by antibody cocktails. Comparing these antibody-mediated mutations with sequence variation in circulating SARS-CoV-2 revealed substitutions that may attenuate neutralizing immune responses in some humans and thus warrant further investigation.
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In the citing paper
“F490S mutation helps the Lambda variant to escape convalescent sera and neutralizing antibodies from the CoronaVac vaccine and also reduced in vitro susceptibility to neutralization [54].”
From Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe (2022) · cites this paper as [54]
Experimental — accuracy not yet measuredIn the citing paper
“several were previously shown to modulate ACE2 binding and/or antibody evasion”
From The Omicron variant is highly resistant against antibody-mediated neutralization: Implications for control of the COVID-19 pandemic (2022) · cites this paper as Liu et al., 2021
In the citing paper
“Our results establishing the E484K substitution as a vulnerability for multiple neutralizing mAbs are consistent with deep mutational scanning or VSV-SARS-CoV-2-based neutralization escape screening campaigns31,33,34.”
From Resistance of SARS-CoV-2 variants to neutralization by monoclonal and serum-derived polyclonal antibodies (2021) · cites this paper as [34]
In the citing paper
“E484K has resulted in 3-fold to 10-fold reduced susceptibility to about 30% and >10-fold reduced susceptibility to about 10% of convalescent plasma samples”
From The biological and clinical significance of emerging SARS-CoV-2 variants (2021) · cites this paper as [160]
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Cites
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“Processing of S by host cell proteases, typically TMPRSS2, TMPRSS4, or endosomal cathepsins, facilitates the S2-dependent fusion of viral and host-cell membranes (Hoffmann et al., 2020; Zang et al., 2020).”
BackgroundA new coronavirus associated with human respiratory disease in China
Wu, F., Zhao, S., Yu, B., Chen, Y.-M., Wang, W., Song, Z.-G., Hu, Y., Tao, Z.-W., Tian, J.-H., Pei, Y.-Y., et al. (2020) · Nature · doi:10.1038/s41586-020-2008-3 · Cited by 11,688
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Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
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“Residue F486 is located on the top of the hACE2 contact loop of RBD, and the presence of a large hydrophobic residue facilitates efficient receptor engagement (Lan et al., 2020; Shang et al., 2020).”
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“During viral entry into cells, the receptor-binding domain (RBD) of S1 engages the primary receptor, human angiotensin converting enzyme 2 (hACE2) (Letko et al., 2020).”
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“In an escape mutation study, which using 19 monoclonal antibodies, substitutions were found at E484 with higher incidence than at any other residue, and four variants at this position (E484A, E484D, E484G, and E484K) exhibited resistance to each of the human convalescent sera tested.(10) There is a gap in our current…”
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“The rapid dissemination of these variants, combined with the ability of viruses harboring the mutation E484K to potentially escape from neutralizing antibodies mounted for older lineages (13,16), should raise concern about the potential effect on infectivity, pathogenicity, and reinfection.”
BackgroundNeutralization of SARS-CoV-2 Variants of Concern Harboring Q677H
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“2 variant, which carries the E484K mutation [2], was detected in this study.”
Genetic Analysis of SARS-CoV-2 Variants in Mexico during the First Year of the COVID-19 Pandemic
Taboada, B., Zárate, S., Iša, P., Boukadida, C., Vázquez-Pérez, J. A., Muñoz‐Medina, J. E., Ramírez–González, J. E., Comas‐García, A., Grajales-Muñíz, C., Rincón-Rubio, A., et al. (2021) · Viruses · doi:10.3390/v13112161 · Cited by 41
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“However, numerous reported neutralizing mAbs targeting the RBD to block the interaction with ACE2 fail to neutralize many of the clinical variants because multiple mutations occur in the highly variable RBD, allowing the virus to escape neutralization (14–16).”
SARS-CoV-2 intra-host evolution during prolonged infection in an immunocompromised patient
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“…resistance to class 1, 2 and 3 antibodies in cell culture has repeatedly identified K417, E484 and N501 substitutions, with E484K giving the most pervasive effects against polyclonal plasma (Baum et al., 2020; Greaney et al., 2021; Liu et al., 2021; Wang et al., 2021; Weisblum et al., 2020).”
BackgroundAllosteric perspective on the mutability and druggability of the SARS-CoV-2 Spike protein
Tan, Z. W., Tee, W.-V., Samsudin, F., Guarnera, E., Bond, P. J., & Berezovsky, I. N. (2022) · Structure · doi:10.1016/j.str.2021.12.011 · Cited by 38
“, 2020) at the binding interface with the ACE2 receptor was found to confer resistance to neutralization by multiple monoclonal antibodies (mAbs) (Liu et al., 2021) and to improve binding affinity to ACE2 (Starr et al.”
BackgroundStrohl, W. R., Ku, Z., An, Z., Carroll, S. F., Keyt, B. A., & Strohl, L. M. (2022) · BioDrugs · doi:10.1007/s40259-022-00529-7 · Cited by 35
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“While several highly effective neutralizing antibodies have been identified and are currently tested in humans, antibody administration could result in the rapid occurrence of resistant mutations in viral spike.(31,32) As a matter of fact, a series of such antibody-resistant mutations have already been identified, whi…”
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The localized rise of a B.1.526 SARS-CoV-2 variant containing an E484K mutation in New York StatePreprint
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Coincident rapid expansion of two SARS-CoV-2 lineages with enhanced infectivity in Nigeria
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Novel and emerging mutations of SARS-CoV-2: Biomedical implications
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“The most common of these substitutions is M/T2634V in nonstructural protein 5, NS5, the RNA-dependent RNA polymerase (RdRp).”
InfluentialAntigenic evolution of SARS coronavirus 2
Mykytyn, A. Z., Fouchier, R. A. M., & Haagmans, B. L. (2023) · Current Opinion in Virology · doi:10.1016/j.coviro.2023.101349 · Cited by 36
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“…point mutant pseudoviruses, chimeric viruses, or recombinant infectious clone-derived SARS-CoV-2 have demonstrated that this mutation displays resistance to neutralization by infection- and vaccine-induced antibodies (Johnson et al., 2021; Liu et al., 2021; Shen et al., 2021; Xie et al., 2021).”
BackgroundSimulation-driven design of stabilized SARS-CoV-2 spike S2 immunogens
Nuqui, X., Casalino, L., Zhou, L., Shehata, M., Wang, A., Tse, A. L., Ojha, A. A., Kearns, F. L., Rosenfeld, M. A., Miller, E. H., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50976-9 · Cited by 33
“…does not signi fi cantly change for HexaPro-SS-V991W [ k opening =(1.1±0.5) × 10 5 s − 1 ], it becomes smaller for HexaPro-SS-2W [ k opening =(7.0±2.3) × 10 3 s − 1 ]andHexaPro-SS-T998W[ k opening = (3.4± 0.1)×10 3 s − 1 ],indicating that T998W induces a roughly 10-fold slower trimer opening.”
BackgroundMethodInfluentialLiu, Z., Xu, W., Chen, Z., Fu, W., Zhan, W., Gao, Y., Zhou, J., Zhou, Y., Wu, J., Wang, Q., et al. (2021) · Protein & Cell · doi:10.1007/s13238-021-00871-6 · Cited by 38
“…angiotensin-converting enzyme-2 (ACE2) and confer resistance to vaccine sera and many monoclonal antibodies (Hou et al., 2020; Korber et al., 2020; Starr et al., 2020; Yurkovetskiy et al., 2020; Greaney et al., 2021; Gupta, 2021; Liu et al., 2021; Plante et al., 2021; Wang et al., 2021c, d).”
Self-citationA class II MHC-targeted vaccine elicits immunity against SARS-CoV-2 and its variants
Pishesha, N., Harmand, T. J., Rothlauf, P. W., Praest, P., Alexander, R., van den Doel, R., Liebeskind, M. J., Vakaki, M. A., McCaul, N., Wijne, C., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2116147118 · Cited by 35
“Neutralization assays were performed similarly to what has been described (19, 20).”
MethodSelf-citationLusvarghi, S., Wang, W., Herrup, R., Neerukonda, S. N., Vassell, R. A., Bentley, L., Eakin, A. E., Erlandson, K. J., & Weiss, C. D. (2021) · Journal of Virology · doi:10.1128/jvi.01110-21 · Cited by 33
“Consistent with many reports (38, 52-60), the E484K substitution present in many lineages had a major impact on many nAbs, leading to a loss of potency for five nAbs (nAbs.”
ResultZhang, J. Z., Yeh, A. H.-W., Walls, A. C., Wicky, B. I. M., Sprouse, K. R., VanBlargan, L. A., Treger, R. S., Quijano‐Rubio, A., Pham, M. N., Kraft, J. C., et al. (2022) · Nature Biotechnology · doi:10.1038/s41587-022-01280-8 · Cited by 37
Self-citationEmergence of SARS-CoV-2 Spike Mutations during Prolonged Infection in Immunocompromised Hosts
Ko, K. K. K., Yingtaweesittikul, H., Tan, T. T., Wijaya, L., Cao, D. Y., Goh, S. S., Rahman, N. B. A., Chan, K. X. L., Tay, H. M., Sim, J. H. C., et al. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.00791-22 · Cited by 37
“were shown to be associated with broad resistance to monoclonal antibody panels (31).”
BackgroundChen, R. E., Gorman, M. J., Zhu, D. Y., Carreño, J. M., Yuan, D., VanBlargan, L. A., Burdess, S., Lauffenburger, D. A., Kim, W., Turner, J. S., et al. (2021) · Med · doi:10.1016/j.medj.2021.11.004 · Cited by 37
Self-citationWhole genome sequencing of SARS-CoV2 strains circulating in Iran during five waves of pandemic
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Cold atmospheric plasma for preventing infection of viruses that use ACE2 for entry
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“In fact, mutated viruses could partly (E484K, Alpha, Beta, Gamma, Epsilon, Eta, Iota, Zeta and Theta) and (E484Q, Kappa) or completely (S477N, Iota) escape from NAb-mediated neutralization[8,16], and positive COVID-19 cases have been reported among vaccinated individuals[17].”
BackgroundCorrelates of Neutralization against SARS-CoV-2 Variants of Concern by Early Pandemic Sera
Vidal, S. J., Collier, A.-R. Y., Yu, J., McMahan, K., Tostanoski, L. H., Ventura, J. D., Aïd, M., Peter, L. E., Jacob-Dolan, C., Anioke, T., et al. (2021) · Journal of Virology · doi:10.1128/jvi.00404-21 · Cited by 34
Innate Immune Response in SARS-CoV-2 Infection
Schiuma, G., Beltrami, S., Bortolotti, D., Rizzo, S., & Rizzo, R. (2022) · Microorganisms · doi:10.3390/microorganisms10030501 · Cited by 39
“As APCs, also SARS-CoV-2 effect on Human Leukocyte Antigen [89] expression on monocyte and macrophage is crucial in the control of the infection.”
BackgroundInfluentialNag, A., Banerjee, R., Paul, S., & Kundu, R. (2022) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2022.105552 · Cited by 34
Halfmann, P., Minor, N. R., Haddock, L. A., Maddox, R., Moreno, G. K., Braun, K. M., Baker, D. A., Riemersa, K. K., Prasad, A., Alman, K. J., et al. (2022) · Virus Evolution · doi:10.1093/ve/veac104 · Cited by 36
Omicron: a drug developer’s perspective
Fang, F., & Shi, P. (2021) · Emerging Microbes & Infections · doi:10.1080/22221751.2021.2023330 · Cited by 34
Single domain shark VNAR antibodies neutralize SARS‐CoV‐2 infection in vitro
Gauhar, A., Privezentzev, C. V., Demydchuk, M., Gerlza, T., Rieger, J., Kungl, A. J., Walsh, F. S., Rutkowski, J. L., & Stocki, P. (2021) · The FASEB Journal · doi:10.1096/fj.202100986rr · Cited by 30
Booster vaccination strategy: Necessity, immunization objectives, immunization strategy, and safety
Meng, H., Mao, J., & Ye, Q. (2022) · Journal of Medical Virology · doi:10.1002/jmv.27590 · Cited by 35
“In addition, along with the circulating variants to some degree escaping from the immune response, the existing neutralizing activity might be insufficient for effective immune protection.(8,9) According to the World Health Organization (WHO), only when the protective efficacy of the COVID‐19 vaccine reaches at least…”
BackgroundMutational dynamics of SARS-CoV-2: Impact on future COVID-19 vaccine strategies
Faraji, N., Zeinali, T., Joukar, F., Aleali, M. S., Eslami, N., Shenagari, M., & Mansour‐Ghanaei, F. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e30208 · Cited by 32
Tracking SARS-CoV-2 Mutations & Variants Through the COG-UK-Mutation Explorer
Wright, D. W., Harvey, W. T., Hughes, J., Cox, M., Peacock, T. P., Colquhoun, R., Jackson, B., Orton, R. J., Nielsen, M., Hsu, S. N., et al. (2022) · Virus Evolution · doi:10.1093/ve/veac023 · Cited by 31
Liu, X., Mostafavi, H., Ng, W. H., Freitas, J. R., King, N. J. C., Zaid, A., Taylor, A., & Mahalingam, S. (2022) · mBio · doi:10.1128/mbio.00683-22 · Cited by 31
Bedotto, M., Fournier, P., Houhamdi, L., Levasseur, A., Delerce, J., Pinault, L., Padane, A., Chamieh, A., Tissot‐Dupont, H., Brouqui, P., et al. (2021) · Journal of Clinical Virology · doi:10.1016/j.jcv.2021.104814 · Cited by 27
Olsen, R. J., Christensen, P. A., Long, S. W., Subedi, S., Hodjat, P., Olson, R., Nguyen, M., Davis, J. J., Yerramilli, P., Saavedra, M. O., et al. (2021) · American Journal Of Pathology · doi:10.1016/j.ajpath.2021.07.002 · Cited by 30
Pan, X., Shi, J. R., Hu, X., Wu, Y. L., Zeng, L., Yao, Y., Shang, W., Liu, K., Gao, G., Guo, W., et al. (2021) · Cell Discovery · doi:10.1038/s41421-021-00320-y · Cited by 30
Rapid detection of multiple SARS-CoV-2 variants of concern by PAM-targeting mutations
Ning, B., Youngquist, B. M., Li, D. D., Lyon, C. J., Zelazny, A. M., Maness, N. J., Tian, D., & Hu, Y. (2022) · Cell Reports Methods · doi:10.1016/j.crmeth.2022.100173 · Cited by 29
“Liu et al., 2021; Wang et al., 2021a).”
Chouikha, A., Farès, W., Lamari, A., Boubaker, S., Belaiba, Z., Ghedira, K., Rebai, W. K., Ayouni, K., Khedhiri, M., Halima, S. B., et al. (2022) · Viruses · doi:10.3390/v14030624 · Cited by 29
The Emergence and Spread of Novel SARS-CoV-2 Variants
Yi, H., Wang, J., Wang, J., Lu, Y., Zhang, Y., Peng, R., Lu, J., & Chen, Z. (2021) · Frontiers in Public Health · doi:10.3389/fpubh.2021.696664 · Cited by 29
Li, X., Zhang, L., Chen, S. E., Ji, W., Li, C., & Ren, L. (2021) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2021.104971 · Cited by 30
Mouse Models for the Study of SARS-CoV-2 Infection
Knight, A. C., Montgomery, S. A., Fletcher, C., & Baxter, V. K. (2021) · Comparative Medicine · doi:10.30802/aalas-cm-21-000031 · Cited by 31
Hoffmann, M., Sidarovich, A., Arora, P., Krüger, N., Nehlmeier, I., Kempf, A. M., Graichen, L., Winkler, M. S., Niemeyer, D., Goffinet, C., et al. (2022) · mBio · doi:10.1128/mbio.00364-22 · Cited by 30
“1), harbor mutation E484K, which has been associated with neutralization resistance (2, 3).”
BackgroundResultGorman, M. J., Patel, N., Guebre‐Xabier, M., Zhu, A. L., Atyeo, C. G., Pullen, K. M., Loos, C., Goez-Gazi, Y., Carrion, R., Tian, J.-H., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.05.429759 · Cited by 29
Structural understanding of SARS-CoV-2 virus entry to host cells
Le, K. P. U., Kannappan, S., Kim, T., Lee, J. H., Lee, H.-R., & Kim, K. K. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1288686 · Cited by 34
Potential immune evasion of the severe acute respiratory syndrome coronavirus 2 Omicron variants
Chen, L., He, Y., Liu, H., Shang, Y., & Guo, G. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1339660 · Cited by 32
Perspective: diagnostic laboratories should urgently develop T cell assays for SARS-CoV-2 infection
Ameratunga, R., Woon, S., Jordan, A., Longhurst, H. J., Leung, E. Y., Steele, R. H., Lehnert, K., Snell, R. G., & Brooks, A. E. S. (2021) · Expert Review of Clinical Immunology · doi:10.1080/1744666x.2021.1905525 · Cited by 28
“and indevimab may be rendered ineffective against new variants including those bearing the E484K mutation [57,58].”
BackgroundÇeli̇k, İ., Khan, A., Dwivany, F. M., Fatimawali, F., Wei, D., & Tallei, T. E. (2022) · Molecular Diversity · doi:10.1007/s11030-022-10392-x · Cited by 30
“The F490S mutation was suspected to be associated with decreased antibody neutralization susceptibility [14].”
BackgroundCD8+ T-cell immune escape by SARS-CoV-2 variants of concern
Kombe, A. J. K., Biteghe, F. A. N., Ndoutoume, Z. N., & Jin, T. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.962079 · Cited by 29
“(14) reported that mutations in the receptor binding domain (RBD) and N-terminal domain (NTD) play a crucial role in variant resistance to humoral immunity.”
BackgroundInfluentialNeutralizing activity of Sputnik V vaccine sera against SARS-CoV-2 variantsPreprint
Ikegame, S., Siddiquey, M. N. A., Hung, C.-T., Haas, G. D., Brambilla, L., Oguntuyo, K. Y., Kowdle, S., Vilardo, A. E., Edelstein, A., Perandones, C., et al. (2021) · medRxiv · doi:10.1101/2021.03.31.21254660 · Cited by 30
Mertens, J. C., Coppens, J., Loens, K., Mercier, M. L., Xavier, B. B., Lammens, C., Vandamme, S., Jansens, H., Goossens, H., & Matheeussen, V. (2021) · Clinical Microbiology and Infection · doi:10.1016/j.cmi.2021.09.007 · Cited by 28
Role of spike in the pathogenic and antigenic behavior of SARS-CoV-2 BA.1 OmicronPreprint
Chen, D.-Y., Kenney, D., Chin, C., Tavares, A. H., Khan, N., Conway, H. L., Liu, G., Choudhary, M., Gertje, H., O'Connell, A., et al. (2022) · bioRxiv · doi:10.1101/2022.10.13.512134 · Cited by 14
Liu, Z., Wu, H., Egland, K. A., Gilliland, T. C., Dunn, M. D., Luke, T. C., Sullivan, E. J., Klimstra, W. B., Bausch, C. L., & Whelan, S. P. J. (2021) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2021.1940652 · Cited by 26
Self-citationSuratekar, R., Ghosh, P., Niesen, M. J. M., Donadio, G., Anand, P., Soundararajan, V., & Venkatakrishnan, A. (2022) · Molecular Systems Biology · doi:10.15252/msb.202110673 · Cited by 28
Rajpal, V. R., Sharma, S., Kumar, A., Chand, S., Joshi, L., Chandra, A., Babbar, S., Goel, S., Raina, S. N., & Shiran, B. (2022) · Journal of Medical Virology · doi:10.1002/jmv.27749 · Cited by 26
“Mutations K417N, T478K, N501Y, D614G, and others have been found to be associated with reinfection, partial resistance to vaccines and increased transmissibility.(5,24) S1/S2 cleavage site mutations H655Y, N679K, and P681H result in increased S1/S2 furin cleavage and facilitate efficient viral entry into the host.”
BackgroundSertraline Is an Effective SARS-CoV-2 Entry Inhibitor Targeting the Spike Protein
Chen, Y., Wu, Y., Chen, S., Zhan, Q., Wu, D., Yang, C., He, X., Qiu, M., Zhang, N., Li, Z., et al. (2022) · Journal of Virology · doi:10.1128/jvi.01245-22 · Cited by 27
Neutralizing activity of Sputnik V vaccine sera against SARS-CoV-2 variantsPreprint
Ikegame, S., Siddiquey, M. N. A., Hung, C.-T., Haas, G. D., Brambilla, L., Oguntuyo, K. Y., Kowdle, S., Vilardo, A. E., Edelstein, A., Perandones, C., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-400230/v1 · Cited by 27
“As expected, the P.1 and B.1.351 variants escape or resist neutralization by first wave convalescent sera, as well as antibodies elicited by COVID-19 vaccines (Garcia-Beltran et al. , 2021; Wang et al. , 2021; Wibmer et al. , 2021; Y. Liu et al. , 2021; Zhou et al. , 2021).”
InfluentialS glycoprotein diversity of the Omicron variantPreprint
Sarkar, R., Lo, M., Saha, R., Dutta, S., & Chawla‐Sarkar, M. (2021) · medRxiv · doi:10.1101/2021.12.04.21267284 · Cited by 26
“The K477N has been shown to confer resistant against monoclonal antibodies, but not convalescent plasma [32].”
BackgroundLind, A., Barlinn, R., Landaas, E. T., Andresen, L. L., Jakobsen, K., Fladeby, C., Nilsen, M., Bjørnstad, P. M., Sundaram, A. Y. M., Ribarska, T., et al. (2021) · Journal of Clinical Virology · doi:10.1016/j.jcv.2021.104906 · Cited by 26
“4 with immune evasion or attenuated immune responses, respectively [22, 23].”
Lee, J., Lee, J., Kim, H. J., Ko, M., Jee, Y., & Kim, S. (2021) · Microbiology Spectrum · doi:10.1128/spectrum.00472-21 · Cited by 28
“Indeed, several results are being published, 60 which demonstrated reduced neutralization capacity of convalescent plasma, vaccine sera, 61 and monoclonal antibodies against these variants (6)(7)(8)(9).”
BackgroundRapid test to assess the escape of SARS-CoV-2 variants of concern
Heggestad, J. T., Britton, R. J., Kinnamon, D., Wall, S. A., Joh, D. Y., Hucknall, A., Olson, L. B., Anderson, J. G., Mazur, A., Wolfe, C. R., et al. (2021) · Science Advances · doi:10.1126/sciadv.abl7682 · Cited by 25
Dynamics of SARS-CoV-2 Alpha (B.1.1.7) variant spread: The wastewater surveillance approach
Carcereny, A., García-Pedemonte, D., Martínez-Velázquez, A., Quer, J., García‐Cehic, D., Gregori, J., Antón, A., Andrés, C., Pumarola, T., Chacón-Villanueva, C., et al. (2022) · Environmental Research · doi:10.1016/j.envres.2022.112720 · Cited by 24
Greaney, A. J., Eguia, R. T., Starr, T. N., Khan, K., Franko, N., Logue, J. K., Lord, S. M., Speake, C., Chu, H. Y., Sigal, A., et al. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010592 · Cited by 29
Zhang, Y., Lu, M., Mahesh, K. C., Kim, E., Shamseldin, M. M., Ye, C., Dravid, P., Chamblee, M., Park, J., Hall, J. M., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2201616119 · Cited by 26
Costacurta, F., Dodaro, A., Bante, D., Schöppe, H., Peng, J.-Y., Sprenger, B., He, X. C., Moghadasi, S. A., Egger, L. M., Fleischmann, J., et al. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012522 · Cited by 26
“Chimeric VSV-Spike, where the VSV glycoprotein G was replaced by the SARS-CoV-2 spike, has been used previously to predict antibody escape mutations [62–64].”
MethodInagaki, H., Saito, A., Kaneko, C., Sugiyama, H., Okabayashi, T., & Fujimoto, S. (2021) · Pathogens · doi:10.3390/pathogens10060754 · Cited by 26
Saied, A. A., Metwally, A. A., Alobo, M., Shah, J., Sharun, K., & Dhama, K. (2022) · International Journal of Surgery · doi:10.1016/j.ijsu.2022.106233 · Cited by 25
Obermair, F.-J., Renoux, F., Heer, S., Lee, C. H.-J., Cereghetti, N., Loi, M., Maestri, G., Haldner, Y., Wuigk, R., Iosefson, O., et al. (2022) · Science Advances · doi:10.1126/sciadv.abl5394 · Cited by 26
Identification and Development of Therapeutics for COVID-19
Rando, H. M., Wellhausen, N., Ghosh, S., Lee, A. J., Dattoli, A. A., Hu, F., Byrd, J. B., Rafizadeh, D. N., Qi, Y., Sun, Y., et al. (2021) · Lund University Publications (Lund University) · Cited by 26
Ahamad, S., Ali, H., Secco, I., Giacca, M., & Gupta, D. K. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.866474 · Cited by 25
“Several of these mutations occur in the highly antigenic S protein, which endows several of the variants with the ability to escape part of the neutralizing antibody response (Weisblum et al., 2020; Liu et al., 2021; Planas et al., 2021; Rees-Spear et al., 2021; Starr et al., 2021).”
Background
Metadata
- Authors
- Liu, Z., VanBlargan, L. A., Bloyet, L.-M., Rothlauf, P. W., Chen, R. E., Stumpf, S., Zhao, H., Errico, J. M., Theel, E. S., Liebeskind, M. J., Alford, B., Buchser, W. J., Ellebedy, A. H., Fremont, D. H., Diamond, M. S., & Whelan, S. P. J.
- Affiliations
- Washington University in St. Louis (US)
- Harvard University (US)
- Mayo Clinic (US)
- Corresponding author
- Diamond, Michael S.
- Whelan, Sean P.J.
- ORCID
- Venue
- Cell Host & Microbe
- Publisher
- Elsevier BV
- Published
- 2021-03
- Volume
- 29
- Issue
- 3
- Pages
- 477-488.e4
- ISSN
- 1931-3128 (ISSN-L)
- PMC
- PMC7839837
- OpenAlex
- W3121995178
- Cited by
- 725
- References
- 38
- Citations by year
- 2026: 11 · 2025: 22 · 2024: 57 · 2023: 77 · 2022: 255 · 2021: 302
- FWCI
- 55.27
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 374 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell Host & Microbe (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Washington University in St. Louis
- University of Washington
- Saint Louis University
- National Institutes of Health (75N93019C00062, R01 AI127828, R01 AI157155, R37 AI059371)
- AbbVie
- Defense Advanced Research Projects Agency (HR001117S0019)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Keywords
- SARS-CoV-2 spike protein, antibody escape mutants, neutralizing monoclonal antibodies, receptor binding domain, E484K mutation
- MeSH terms
- Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, COVID-19 Vaccines, Animals, Antibodies, Monoclonal, Antibodies, Viral, Chlorocebus aethiops, Female, Humans, Mice, Inbred BALB C, Models, Molecular, Mutation, Neutralization Tests, Protein Binding, Receptors, Virus, Vero Cells, Amino Acid Substitution, Mice, Antibodies, Neutralizing, Spike Glycoprotein, Coronavirus
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