Cited by 739SARS-CoV-2 and COVID-19 Researchvaccines and immunoinformatics approachesAnimal Virus Infections Studies

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Identification of SARS-CoV-2 spike mutations that attenuate monoclonal and serum antibody neutralization

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Liu, Zhuoming, VanBlargan, Laura A., Bloyet, Louis-Marie, Rothlauf, Paul W., Chen, Rita E., Stumpf, Spencer, Zhao, Haiyan, Errico, John M., Theel, Elitza S., Liebeskind, Mariel J., Alford, Brynn, Buchser, William J., Ellebedy, Ali H., Fremont, Daved H., Diamond, Michael S., Whelan, Sean P.J.·2021·Cell Host & Microbe

DOI 10.1016/j.chom.2021.01.014PMC PMC7839837

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Abstract

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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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 · cited 1×
“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).”
Background
A 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
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
Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
Lan, J., Ge, J., Yu, J., Shan, S., Zhou, H., Fan, S., Zhang, Q., Shi, X., Wang, Q., Zhang, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2180-5 · Cited by 5,983 · cited 1×
“The impact of SARS-CoV-2 adaptation for infection of other hosts including mice (Dinnon et al., 2020; Gu et al., 2020), mink (Oude Munnink et al., 2021), and domesticated animals (Halfmann et al., 2020; Shi et al., 2020) could also contribute to selection of new variants.”
Background
Structural basis of receptor recognition by SARS-CoV-2
Shang, J., Ye, G., Shi, K., Wan, Y., Luo, C., Aihara, H., Geng, Q., Auerbach, A., & Li, F. (2020) · Nature · doi:10.1038/s41586-020-2179-y · Cited by 3,661 · cited 1×
“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).”
Background
Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses
Letko, M., Marzi, A., & Munster, V. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0688-y · Cited by 3,109 · cited 2×
“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).”
Background
Emergence and rapid spread of a new severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) lineage with multiple spike mutations in South Africa
Tegally, H., Wilkinson, E., Giovanetti, M., Iranzadeh, A., Fonseca, V., Giandhari, J., Doolabh, D., Pillay, S., San, E. J., Msomi, N., et al. (2020) · doi:10.1101/2020.12.21.20248640 · Cited by 2,535 · cited 1×
“a combination of at least two neutralizing antibodies (Baum et al., 2020; Du et al., 2020; 316 Greaney et al., 2020; Group et al., 2020; Li et al., 2020; Weisblum et al., 2020).”
Background
Detection of a SARS-CoV-2 variant of concern in South Africa
Tegally, H., Wilkinson, E., Giovanetti, M., Iranzadeh, A., Fonseca, V., Giandhari, J., Doolabh, D., Pillay, S., San, E. J., Msomi, N., et al. (2021) · Nature · doi:10.1038/s41586-021-03402-9 · Cited by 2,510
Inhibition of SARS-CoV-2 Infections in Engineered Human Tissues Using Clinical-Grade Soluble Human ACE2
Monteil, V., Kwon, H., Prado, P., Hagelkrüys, A., Wimmer, R. A., Stahl, M., Leopoldi, A., Garreta, E., Hurtado del Pozo, C., Prosper, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.04.004 · Cited by 2,122
Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding
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

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Wu, C.-Y., Yang, Y.-H., Lin, Y.-S., Shu, L.-H., Cheng, Y.-C., Liu, H.-T., Lin, Y., Lee, I.-Y., Shih, W.-T., Yang, P.-R., et al. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e17701 · Cited by 2
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Background
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Parry, R. H., Shang, Y., Sng, J. D. J., McMillan, C. L. D., Modhiran, N., Amarilla, A. A., Isaacs, A., Liang, B., Muller, D. A., Rawle, D. J., et al. (2025) · Journal of Medical Virology · doi:10.1002/jmv.70642 · Cited by 1
In Vivo Determinants of Hepatitis C Virus Adaptation and Escape From Neutralizing Antibody AR5A
Velázquez‐Moctezuma, R., Burm, R., Verhoye, L., Collignon, L., Holmbeck, K., Giang, E., Law, M., Bukh, J., Meuleman, P., & Prentoe, J. C. (2025) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2025.101684 · Cited by 1
In Vitro Diagnostics for COVID-19: State-of-the-Art, Future Directions and Role in Pandemic Response
Vashist, S. K., Subramanian, M., & Djoko, G. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.97775 · Cited by 1
Vaccines against COVID-19 – Catching the Rays of Hope
Srinivasamurthy, S. K., & Bairy, L. K. (2021) · Journal of Pharmaceutical Research International · doi:10.9734/jpri/2021/v33i47a33035 · Cited by 1
A proposed workflow for proactive virus surveillance and prediction of variants for vaccine design
Baker, J. J., Mathy, C. J. P., & Schaletzky, J. (2021) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1009624 · Cited by 1
“bodies from people previously infected or vaccinated are tested for efficacy of neutralization [6,7].”
Background
Genomics and epidemiology of SARS-CoV-2 lineage
Sukegawa, S., & Takeuchi, H. (2021) · Uirusu · doi:10.2222/jsv.71.19 · Cited by 1
The Recent Updates on Neoteric Variants of Covid-19 Virus and Therapeutic Effectiveness of Vaccines against the Variants.
Chaudhary, S., El‐Shorbagi, A., Chaudhary, A., Agarwal, G., Tripathi, P. N., & Dumoga, S. (2022) · Biomedical & Pharmacology Journal · doi:10.13005/bpj/2456 · Cited by 1
Cell Entry and Unusual Replication of SARS-CoV-2
McCann, N. R., & Castellino, F. (2022) · Current Drug Targets · doi:10.2174/1389450124666221014102927 · Cited by 1
Analysis of SARS-CoV-2 variants from patient specimens in Nevada from October 2020 to August 2021
Payen, S. H., Gorzalski, A. J., Siao, D. D., Pandori, M., Verma, S. C., & Rossetto, C. C. (2023) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2023.105434 · Cited by 1
Monitoring of SARS-CoV-2 B.1.1.7 variant early-phase spreading in South-Moravian Region in the Czech Republic and evaluation of its pathogenicityPreprint
Diabelko, D., Dvořáčková, M., Dvořáková, M., Forte, G., Čundrle, I., Růžička, F., & Vrbský, J. (2021) · medRxiv · doi:10.1101/2021.05.24.21257365 · Cited by 1
“; https://doi.org/10.1101/2021.05.24.21257365doi: medRxiv preprint Jangra et al. 2021, Liu et al. 2021).”
BackgroundInfluential
Second-Generation Antibodies Neutralize Emerging SARS-CoV-2 Variants of ConcernPreprint
Kovačech, B., Fialova, L., Filipcik, P., Škrabana, R., Zilkova, M., Paulenka-Ivanovova, N., Kováč, A., Palova, D., Rolkova, G. P., Tomková, K., et al. (2021) · bioRxiv · doi:10.1101/2021.06.09.447527
Systems immune profiling of variant-specific vaccination against SARS-CoV-2Preprint
Peng, L., Park, J. J.-Y., Fang, Z., Zhou, X., Dong, M. B., Xiong, Q., Lin, C., & Chen, S. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.02.471028 · Cited by 1
Deep Mutational Engineering of broadly-neutralizing and picomolar affinity nanobodies to accommodate SARS-CoV-1 & 2 antigenic polymorphismPreprint
Laroche, A., Delgado, M. L. O., Cuniasse, P., DuBois, S. G., Sierocki, R., Gallais, F., Debroas, S., Bellanger, L., Simon, S., Maillère, B., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.07.471597 · Cited by 1
Comprehensive Evaluation of ACE2-Fc Combination with Neutralization Antibody on Broad Protection against SARS-CoV-2 and Its VariantsPreprint
Tang, H., Ke, Y., Ma, H., Han, L., Wang, L., Zong, H., Yuan, Y., Wang, Z., He, Y., Chang, Y., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.17.475291 · Cited by 2
“Escape information refers to COG-UK-ME and literatures of corresponding antibodies: Etesevimab [18], Casirivimab [17-20], Tixagevimab [25], ABBV-2B04 [26], Regdanvimab [12], Bamlanivimab [17], Cilgavimab [25], Imdevimab [18,19], ADG20 [17].”
Background
Broadly neutralizing and protective nanobodies against diverse sarbecovirusesPreprint
Li, M., Ren, Y., Aw, Z. Q., Chen, B., Yang, Z., Lei, Y., Cheng, L., Liang, Q., Hong, J., Yang, Y., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.12.488087 · Cited by 1
Investigating the mutations in the SARS-CoV-2 proteins among European countriesPreprint
Abavisani, M., Rahimian, K., Khayami, R., Kodori, M., Sisakht, M. M., Mahmanzar, M., & Meshkat, Z. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.23.497239 · Cited by 1
“found to resist neutralization by monoclonal antibodies (mAb) and convalescent sera [20, 21].”
Background
Identification and Development of Therapeutics for COVID-19.Preprint
Rando, H. M., Wellhausen, N., Ghosh, S., Lee, A. J., Dattoli, A. A., Hu, F., Byrd, J. B., Rafizadeh, D. N., Lordan, R., Qi, Y., et al. (2021) · PubMed · Cited by 1
Computational Analysis of Antibody Binding Mechanisms to the Omicron RBD of SARS-CoV-2 Spike Protein: Identification of Epitopes and Hotspots for Developing Effective Therapeutic Strategies
Alshahrani, M. (2023) · Chapman University Digital Commons (Chapman University) · doi:10.36837/chapman.000491 · Cited by 1
The impact of non-lineage defining mutations in the structural stability for variants of concern of SARS-CoV-2Preprint
Martins, Y., & da Silva, R. D. (2023) · bioRxiv · doi:10.1101/2023.06.22.546079 · Cited by 1
“This behavior was also validated by assays [35, 20] showing that this mutation abolished binding of the monoclonal antibody 2B04, diminished binding by 2C03 but no effect was observed in relation to the monoclonal antibodies 2C02 or 2E06.”
A Fine-tuned ProtGPT2 (transformer model) for Predicting more Virulent SARS-CoV-2 variants and understanding its virulence by biophysical methodsPreprint
Dhamodharan, S. P., Abraham Rebairo, J., Siddalingappa, R., Venkatachalam Rajakannan, B., & Kothandan, G. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.13.632691 · Cited by 1
A glimmer of hope for the most vulnerable
Falsey, A. R. (2021) · Journal of the American Geriatrics Society · doi:10.1111/jgs.17198
“However, the recent evolution of COVID variants with reduced susceptibility to convalescent plasma has raised concerns that monoclonal antibodies that bind to a single epitope would be particularly susceptible to development of resistance.(11) Active vaccination has many advantages compared to monoclonal antibody trea…”
Background
Molecular Epidemiological Insights into Transmission Trends in Nagoya Area Based on SARS-CoV-2 Genome Sequencing (Mar-Oct, 2020)
Nakata, Y., Ode, H., Kubota, M., Matsuoka, K., MATSUDA, M., NAKASUJI, M., Mori, M., Imahashi, M., Yokomaku, Y., & Iwatani, Y. (2021) · Kansenshogaku zasshi · doi:10.11150/kansenshogakuzasshi.95.293
Discovery of nanobodies against SARS-CoV-2 and an uncommon neutralizing mechanismPreprint
Li, T., Zhou, B., Luo, Z., Lai, Y., Huang, S., Zhou, Y., Gautam, A., Bourgeau, S., Wang, S., Bao, J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.20.453054
Broad neutralizing nanobody against SARS-CoV-2 engineered from pre-designed synthetic libraryPreprint
Liu, Q.-Y., Cai, C.-G., Huang, Y., Zhou, L., Guan, Y., Fu, S., Lin, Y.-H., Yang, T.-R., Liang, X.-H., Wang, N., et al. (2021) · bioRxiv · doi:10.1101/2021.08.07.455523
“VHH60 blocks the infection of mutated pseudovirus Given the high mutagenic capacity of SARS-CoV-2 as an RNA virus, escape mutations and variants resistant to current antibodies or vaccines have been studied and described [26-33].”
Background
Delta variant - A new phase of COVID-19 in India
Sreenivas, S. S. (2021) · International Journal of Medical Science · doi:10.14445/23939117/ijms-v8i7p105
A bacteria-based assay to study SARS-CoV-2 protein-protein interactionsPreprint
Springstein, B. L., Deighan, P., Grabe, G., & Hochschild, A. (2021) · bioRxiv · doi:10.1101/2021.10.07.463611
SARS-CoV-2: Genetic variability, mutations and variants of concern for the global world
Cupic, M. D. (2021) · Medicinski podmladak · doi:10.5937/mp72-33322
Peer Review #1 of "EpiCurator: an immunoinformatic workflow to predict and prioritize SARS-CoV-2 epitopes (v0.1)"
(2021) · PeerJ · doi:10.7287/peerj.12548v0.1/reviews/1
Peer Review #3 of "EpiCurator: an immunoinformatic workflow to predict and prioritize SARS-CoV-2 epitopes (v0.1)"
(2021) · PeerJ · doi:10.7287/peerj.12548v0.1/reviews/3
Peer Review #1 of "EpiCurator: an immunoinformatic workflow to predict and prioritize SARS-CoV-2 epitopes (v0.2)"
(2021) · PeerJ · doi:10.7287/peerj.12548v0.2/reviews/1
Dynamic Zero-Covid strategy curtails mutagenesis and emergence of new variants of the SARS-CoV-2Preprint
Cui, L., Zhu, L., Zhang, J., Fan, H., Yi, Y., Zhao, J. F., Ge, Y., Wang, S., Han, X., Gao, X., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-1195945/v1
Peer Review #2 of "EpiCurator: an immunoinformatic workflow to predict and prioritize SARS-CoV-2 epitopes (v0.1)"
(2021) · PeerJ · doi:10.7287/peerj.12548v0.1/reviews/2
SARS-CoV-2 Alpha Variant Infection of a Patient Immunized by Inactive Sinovac (CoronaVac) Vaccine
Özverel, C. S., Tulay, P., Ergören, M. Ç., Güler, E., Baddal, B., Süer, K., & Şanlıdağ, T. (2022) · The EuroBiotech Journal · doi:10.2478/ebtj-2022-0003
ChAdOx1 nCoV-19, BNT162b2 and CoronaVac Vaccines Do Not Induce as Strong Neutralising Antibodies with Broad Variant Protection as Infection and Suggest Vaccines that Induce Broader Sterilising Immunity are Essential to Stop the PandemicPreprint
Chua, J. X., Durrant, L. G., Chok, Y. L., & Lai, O. M. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4062765
A systematic review of the variants of Sars-Cov-2
Qureshi, M. F., & Qureshi, S. (2022) · International Journal of Science and Research Archive · doi:10.30574/ijsra.2022.5.2.0050
nSARS-CoV-2 and COVID-19 Pandemic: From Emergence to Vaccination
Shahid, I. (2022) · Dr Sulaiman Al Habib Medical Journal · doi:10.1007/s44229-022-00006-x
“351, which harbors this mutation, is able to successfully escape the host immune system [35].”
Background
Pathogen-Host Adhesion between SARS-CoV-2 Spike Proteins from Different Variants and Human ACE2 Probed at Single-Molecule and Single-Cell LevelsPreprint
Zhang, X., Chen, J., Hong, B., Xu, H. C., Pei, P., Chen, L., Tong, Y., Luo, S., Fan, H., & He, C. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.05.493249
Fatigue Symptom and Oximetry Sign in a Patient with a Positive Covid-19 Antigen Test for Sars-Cov-2 Síntoma Fatiga y Signo Oximetría en paciente con prueba de Antígeno Covid-19 positivo para Sars-Cov-2
Aguilar, R. (2022) · Research Review · doi:10.52845/jmrhs/2022-5-8-5
Long-term passaging of replication competent pseudo-typed SARS-CoV-2 reveals the antiviral breadth of monoclonal and bispecific antibody cocktailsPreprint
Ma, H.-H., Zong, H., Liu, J.-J., Yue, Y.-L., Ke, Y., Liao, Y.-J., Tang, H.-N., Wang, L., Wang, S., Yuan, Y., et al. (2022) · bioRxiv · doi:10.1101/2022.10.05.511057
Overview and Recommendations on Worrying SARS-CoV-2 Virus Variants (VOC)
Shneine, J. K., & Ahmad, S. M. (2022) · Journal of Al-Nahrain University-Science · doi:10.22401/anjs.25.3.09
Development of pyrosequencing-based assay for genotyping of different coronavirus variants
Chistyakova, A. K., Stepanova, E., Николаевна, И.-С. И., & Георгиевна, Р. Л. (2022) · Medical academic journal · doi:10.17816/maj108988
3’ end hydrolysis activity of the Bst polymerase enables rapid and sensitive identification of SARS-CoV-2 variantsPreprint
Ooi, K. H., Liu, M. M., Burhanudin, S., Thirunavukarasu, S., Oh, Z. Q. V., Kwa, S. N. S., Ng, T. H. V., Nimsamer, P., Payungporn, S., Kaewsapsak, P., et al. (2023) · Research Square · doi:10.21203/rs.3.rs-2607942/v1
Genomic Analysis of S protein in SARS-CoV-2 samples from Washington D.C
SWAMINATHAN, N. (2022) · Journal of Student Research · doi:10.47611/jsrhs.v11i3.3360
SARS-CoV-2: Structure, Pathogenesis, and Diagnosis
Goverdhan, A. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-87539-4.00002-6
An in vitro experimental pipeline to characterize the binding specificity of SARS-CoV-2 neutralizing antibodiesPreprint
Atanasoff, K. E., Brambilla, L., Adelsberg, D. C., Kowdle, S., Stevens, C. S., Hung, C.-T., Fu, Y., Lim, R. K. V., Tran, L., ALLEN, R. D., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.20.537738
“Indeed, substitutions 440 at position 486, including the F486S substitution, confer significant antibody evasion capability 441 in both circulating SARS-CoV-2 variants (34) and laboratory-generated viral escape mutants 442 solicited under nmAb-directed selective pressure (35).”
Background
Identification of SARS-CoV-2 Neutralizing Potency of Human Convalescent Plasma Using Pseudovirus Neutralization AssayPreprint
Tok, Y., Torabfam, G. Ç., Çimen, A. N., Güney-Esken, G., Yücebağ, E., Arslan, N., Sarıbal, D., Doğan, Ö., Kuşkucu, M. A., Mete, B., et al. (2023) · doi:10.22541/au.168903906.67219803/v1
Chronic Shedding of a SARS-CoV-2 Alpha Variant Lineage Q.3/Q.4 in WastewaterPreprint
Conway, M. J., Yang, H., Revord, L. A., Ward, A. S., Abel, J. D., Williams, M. R., Uzarski, R. L., & Alm, E. W. (2023) · medRxiv · doi:10.1101/2023.07.26.23293191
“…was previously observed during a persistent infection in an immunocompromised patient (Greaney et al., 2021a; Greaney et al., 2021b; Gregory et al., 2022; Kimura et al., 2022; Ku et al., 2021; Liu et al., 2021; Tortorici et al., 2020; VanBlargan et al., 2021; Wang et al., 2022; Wang et al., 2023).”
BackgroundInfluential
Virological Diagnosis of SARS-CoV-2 in a Tunisian Orthopedic Institute
(2023) · Translational Medicine Open Access · doi:10.33140/tmoa.01.01.01
Global genomic diversity and conservation of SARS-CoV-2 since the COVID-19 outbreak
Li, H., Ding, L., Liao, R. J., Li, N., Hong, X., Jiang, Z., & Liu, D. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.02826-23
“Whereas mutations L452R, S477N, and E484K may result in decreased antibody-neutralizing activity or increased resistance to vaccine-elicited antibodies (33, 34).”
Background
Generation of SARS‐CoV‐2 spike receptor binding domain mutants and functional screening for immune evaders using a novel lentivirus‐based system
Jia, J., Garbarino, E., Wang, Y., Li, J., Song, M., Zhang, X., Wang, X., Li, L., Chi, J., Cui, L., et al. (2024) · Journal of Medical Virology · doi:10.1002/jmv.29425
“30 Furthermore, our method is also screening broader set of antibodies for selecting escape mutants since it is based on polyclonal anti ‐ RBD inhibition of a nonreplicative lentivirus entry and is thus not limited to use of limited number of available monoclonal antibodies and convalescent sera…”
Method
Differential laboratory passaging of SARS-CoV-2 viral stocks impacts the in vitro assessment of neutralizing antibodies
Avila-Herrera, A., Kimbrel, J. A., Martí, J. M., Thissen, J. B., Saada, E. A., Weisenberger, T., Arrildt, K. T., Segelke, B. W., Allen, J., Zemla, A. T., et al. (2024) · PLoS ONE · doi:10.1371/journal.pone.0289198
“The mutations generated during viral replication occurred at RBD 446 residues associated with polyclonal antiserum and mAb escape (25, 26), and within or adjacent 447 to the known epitopes of the antibodies (3) (Fig 2).”
Background
A Data Analytics-Based Study in SARS-CoV-2 Genome Revealed a Commonality in the Infection Pattern
Dash, M., Kumar, V. S., Meher, P., & Namsa, N. D. (2024) · Lecture notes in electrical engineering · doi:10.1007/978-981-99-6855-8_14

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: Liu, Zhuoming
VanBlargan, Laura A.
Bloyet, Louis-Marie
Rothlauf, Paul W.
Chen, Rita E.
Stumpf, Spencer
Zhao, Haiyan
Errico, John M.
Theel, Elitza S.
Liebeskind, Mariel J.
Buchser, William J.
Ellebedy, Ali H.
Fremont, Daved H.
Diamond, Michael S.
Whelan, Sean P.J.
Venue: Cell Host & Microbe
Publisher: Elsevier BV
Published: 2021-03
Volume: 29
Issue: 3
Pages: 477-488.e4
ISSN: 1931-3128 (ISSN-L)
DOI: 10.1016/j.chom.2021.01.014
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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Identification of SARS-CoV-2 spike mutations that attenuate monoclonal and serum antibody neutralization

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