PreprintCited by 1,178SARS-CoV-2 and COVID-19 Researchvaccines and immunoinformatics approachesSARS-CoV-2 detection and testing

The DOI matches its Crossref record; 74 of the 74 references it cites were found in a registry or an index.

Comprehensive mapping of mutations to the SARS-CoV-2 receptor-binding domain that affect recognition by polyclonal human serum antibodies

Open access

Greaney, Allison J., Loes, Andrea N., Crawford, Katharine H.D., Starr, Tyler N., Malone, Keara D., Chu, Helen Y., Bloom, Jesse D.·2021·Cell Host & Microbe

DOI 10.1101/2020.12.31.425021PMC PMC7869748

Preprint — published as 10.1016/j.chom.2021.02.003 · Paper page

Open this paper in CoChat — free account Open PDF

Abstract

The evolution of SARS-CoV-2 could impair recognition of the virus by human antibody-mediated immunity. To facilitate prospective surveillance for such evolution, we map how convalescent serum antibodies are impacted by all mutations to the spike’s receptor-binding domain (RBD), the main target of serum neutralizing activity. Binding by polyclonal serum antibodies is affected by mutations in three main epitopes in the RBD, but there is substantial variation in the impact of mutations both among individuals and within the same individual over time. Despite this inter- and intra-person heterogeneity, the mutations that most reduce antibody binding usually occur at just a few sites in the RBD’s receptor binding motif. The most important site is E484, where neutralization by some sera is reduced >10-fold by several mutations, including one in emerging viral lineages in South Africa and Brazil. Going forward, these serum escape maps can inform surveillance of SARS-CoV-2 evolution.

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

Crossref · 10.1101/2020.12.31.425021

Cites

74 of 74 references verified0 citation errors · 0 not checkable

Statistics

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

MAFFT Multiple Sequence Alignment Software Version 7: Improvements in Performance and Usability
Katoh, K., & Standley, D. M. (2013) · Molecular Biology and Evolution · doi:10.1093/molbev/mst010 · Cited by 46,209 · cited 1×
“Analysis of RBD mutations among circulating SARS-CoV-2 isolates All 283,908 spike sequences on GISAID as of Dec-23-2020 were downloaded and aligned via mafft (Katoh and Standley, 2013).”
Method
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 2×
“Two views of the RBD are shown: the surface of the RBD that is buried in the “down” conformation, and the surface that is always exposed and accessible (Walls et al., 2020; Wrapp et al., 2020).”
Background
Structure, 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 · cited 4×
“Because the RBD is usually in the “down” conformation (Cai et al., 2020; Ke et al., 2020; Walls et al., 2020) , we speculate that while sites accessible in this conformation can be targeted by neutralizing antibodies, they may be subdominant in the context of polyclonal serum binding to full spike…”
BackgroundInfluential
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
Tracking Changes in SARS-CoV-2 Spike: Evidence that D614G Increases Infectivity of the COVID-19 Virus
Korber, B., Fischer, W. M., Gnanakaran, S., Yoon, H., Theiler, J., Abfalterer, W., Hengartner, N., Giorgi, E. E., Bhattacharya, T., Foley, B., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.043 · Cited by 4,281 · cited 1×
“, 2020a) and the D614G mutation that is now predominant in human SARS-CoV-2 (Korber et al., 2020).”
Background
Estimated transmissibility and impact of SARS-CoV-2 lineage B.1.1.7 in England
Davies, N. G., Abbott, S., Barnard, R. C., Jarvis, C. I., Kucharski, A. J., Munday, J. D., Pearson, C. A. B., Russell, T. W., Tully, D. C., Washburne, A. D., et al. (2020) · doi:10.1101/2020.12.24.20248822 · Cited by 2,557
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 7×
“The site where mutations tend to have the largest effect on binding and neutralization is E484, which unfortunately is a site where mutations are present in several emerging SARS-CoV-2 lineages (Tegally et al., 2020; Voloch et al., 2020) .”
BackgroundInfluential
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
Self-citation
Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2349-y · Cited by 1,885
Convergent Antibody Responses to SARS-CoV-2 in Convalescent Individuals
Robbiani, D. F., Gaebler, C., Muecksch, F., Lorenzi, J. C. C., Wang, Z., Cho, A., Agudelo, M., Barnes, C. O., Gazumyan, A., Finkin, S., et al. (2020) · Nature · doi:10.1038/s41586-020-2456-9 · Cited by 1,853

Show all 58 references

Sorted by citations

Items 201–300 of 713

From Bench to the Clinic: The Path to Translation of Nanotechnology-Enabled mRNA SARS-CoV-2 Vaccines
Lopez-Cantu, D. O., Wang, X., Carrasco-Magallanes, H., Afewerki, S., Zhang, X., Bonventre, J. V., & Ruiz‐Esparza, G. U. (2022) · Nano-Micro Letters · doi:10.1007/s40820-021-00771-8 · Cited by 49
The Development of SARS-CoV-2 Variants: The Gene Makes the Disease
Pérez-Gómez, R. (2021) · Journal of Developmental Biology · doi:10.3390/jdb9040058 · Cited by 47
Multiplex Biosensing for Simultaneous Detection of Mutations in SARS-CoV-2
Xi, H., Jiang, H., Juhas, M., & Zhang, Y. (2021) · ACS Omega · doi:10.1021/acsomega.1c04024 · Cited by 48
SARS-CoV-2 Delta Variant Pathogenesis and Host Response in Syrian Hamsters
Mohandas, S., Yadav, P. D., Shete, A. M., Nyayanit, D. A., Sapkal, G. N., Lole, K. S., & Gupta, N. (2021) · Viruses · doi:10.3390/v13091773 · Cited by 56
“3 possesses the E484Q mutation which is a known site in RBD which can impact the serum neutralization efficiency [6].”
Background
SARS-CoV-2 Neutralization Resistance Mutations in Patient with HIV/AIDS, California, USA
Hoffman, S. A., Costales, C., Sahoo, M. K., Palanisamy, S., Yamamoto, F. F., Huang, C., Verghese, M., Solis, D., Sibai, M., Subramanian, A. K., et al. (2021) · Emerging infectious diseases · doi:10.3201/eid2710.211461 · Cited by 55
“Viruses harboring E484Q have reduced susceptibility to monoclonal antibodies, convalescent plasma, and vaccinee plasma (7,8).”
Background
Dynamic Profiling of Binding and Allosteric Propensities of the SARS-CoV-2 Spike Protein with Different Classes of Antibodies: Mutational and Perturbation-Based Scanning Reveal Allosteric Duality of Functionally Adaptable Hotspots
Verkhivker, G. M., Agajanian, S., Oztas, D., et al. (2021) · bioRxiv · doi:10.1101/2021.04.13.439743 · Cited by 42
PCR assay to enhance global surveillance for SARS-CoV-2 variants of concernPreprint
Vogels, C. B. F., Breban, M. I., Alpert, T., et al. (2021) · medRxiv · doi:10.1101/2021.01.28.21250486 · Cited by 42
“In particular, B.1.351 and P.1, which were recently discovered in South Africa and Brazil, respectively, may also be more transmissible and contain mutations that could help to evade immune responses 6,7,14 .”
Influential
Distinct Patterns of Emergence of SARS-CoV-2 Spike Variants including N501Y in Clinical Samples in Columbus OhioPreprint
Tu, H., Avenarius, M. R., Kubatko, L. S., Hunt, M., Pan, X., Ru, P., Garee, J. P., Thomas, K., Mohler, P. J., Pancholi, P., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.12.426407 · Cited by 36
Multiple expansions of globally uncommon SARS-CoV-2 lineages in Nigeria
Ozer, E. A., Simons, L. M., Adewumi, M. O., Fowotade, A., Omoruyi, E. C., Adeniji, J. A., Olayinka, O. A., Dean, T. J., Zayas, J. P., Bhimalli, P. P., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28317-5 · Cited by 48
Acquisition of the L452R Mutation in the ACE2-Binding Interface of Spike Protein Triggers Recent Massive Expansion of SARS-CoV-2 Variants
Tchesnokova, V. L., Kulasekara, H. D., Larson, L., Bowers, V., Rechkina, E., Kisiela, D., Sledneva, Y., Choudhury, D., Maslova, I., Deng, K., et al. (2021) · Journal of Clinical Microbiology · doi:10.1128/jcm.00921-21 · Cited by 214
Coronavirus Disease 2019 Vaccine Impact on Rates of Severe Acute Respiratory Syndrome Coronavirus 2 Cases and Postvaccination Strain Sequences Among Health Care Workers at an Urban Academic Medical Center: A Prospective Cohort Study
Bouton, T. C., Lodi, S., Turcinovic, J., Schaeffer, B., Weber, S. E., Quinn, E., Korn, C., Steiner, J., Schechter-Perkins, E. M., Duffy, E., et al. (2021) · Open Forum Infectious Diseases · doi:10.1093/ofid/ofab465 · Cited by 49
“This allowed examination of vaccine effectiveness during a period of higher prevalence and increased SARS-CoV-2 viral diversity than in the initial clinical trials [2, 3].”
Background
Hetero-bivalent nanobodies provide broad-spectrum protection against SARS-CoV-2 variants of concern including Omicron
Ma, H., Zhang, X., Zheng, P., Dube, P. H., Zeng, W., Chen, S., Cheng, Q., Yang, Y., Wu, Y., Zhou, J., et al. (2022) · Cell Research · doi:10.1038/s41422-022-00700-3 · Cited by 42
A review: Antibody-dependent enhancement in COVID-19: The not so friendly side of antibodies
Sánchez‐Zuno, G. A., Matuz-Flores, M. G., González-Estévez, G., Nicoletti, F., Turrubiates‐Hernández, F. J., Mangano, K., & Muñóz-Valle, J. F. (2021) · International Journal of Immunopathology and Pharmacology · doi:10.1177/20587384211050199 · Cited by 48
“Studies have also shown that the presence of this variant directly affects the average binding of convalescent sera (>10 times) reducing the neutralization activity of some individuals.(75) Recently, the BNT162b2 nucleoside modified RNA vaccine encoding the full-length SARS-CoV-2 protein (S) was reported to be effecti…”
Background
COVID-19 pandemic: lessons learned from more than a century of pandemics and current vaccine development for pandemic control
Buchy, P., Buisson, Y., Cintra, O. A. L., Dwyer, D. E., Nissen, M. D., de Lejarazu, R. O., & Petersen, E. (2021) · International Journal of Infectious Diseases · doi:10.1016/j.ijid.2021.09.045 · Cited by 46
An Overview of Vaccines against SARS-CoV-2 in the COVID-19 Pandemic Era
Pascual‐Iglesias, A., Cantón, J., Ortega‐Prieto, A. M., Jiménez-Guardeño, J. M., & Regla-Nava, J. Á. (2021) · Pathogens · doi:10.3390/pathogens10081030 · Cited by 50
Simultaneous evaluation of antibodies that inhibit SARS-CoV-2 variants via multiplex assay
López, E., Haycroft, E. R., Adair, A., Mordant, F. L., O’Neill, M. T., Pymm, P., Redmond, S. J., Lee, W. S., Gherardin, N. A., Wheatley, A. K., et al. (2021) · JCI Insight · doi:10.1172/jci.insight.150012 · Cited by 38
“Of further concern has been the observation that a number of these 394 variants demonstrate escape from antibody neutralization (23-27, 45) with the more 395 recent emergence of new variants with multiple mutations in the RBD (8), also 396 demonstrating resistance to in vitro antibody neutralization (46).”
BackgroundMethodInfluential
On the road to ending the COVID-19 pandemic: Are we there yet?
Case, J. B., Winkler, E. S., Errico, J. M., & Diamond, M. (2021) · Virology · doi:10.1016/j.virol.2021.02.003 · Cited by 47
“J.B. Case et al. Virology 557 (2021) 70–85 previously was identified as a key monoclonal and polyclonal antibody escape mutation in the context of yeast and chimeric vesicular stomatitis virus screening campaigns (Greaney et al., 2021a, 2021b; Starr et al., 2020; Weisblum et al., 2020).”
A point-of-care lateral flow assay for neutralising antibodies against SARS-CoV-2
Fulford, T. S., Văn, H. T., Gherardin, N. A., Zheng, S., Ciula, M., Drummer, H. E., Redmond, S. J., Tan, H., Boo, I., Li, F., et al. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103729 · Cited by 47
“5), choosing variants observed during second wave infections in June 2020 that have been reported to have varying sensitivity to some mAbs [33,34].”
Background
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
Molecular rationale for SARS-CoV-2 spike circulating mutations able to escape bamlanivimab and etesevimab monoclonal antibodies
Laurini, E., Marson, D., Aulić, S., Fermeglia, A., & Pricl, S. (2021) · Scientific Reports · doi:10.1038/s41598-021-99827-3 · Cited by 45
Durability of mRNA-1273-induced antibodies against SARS-CoV-2 variantsPreprint
Pegu, A., O’Connell, S. E., Schmidt, S. D., O'Dell, S. J., Talana, C. A., Lai, L., Albert, J., Anderson, E. J., Bennett, H., Corbett, K. S., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.13.444010 · Cited by 50
Coincident rapid expansion of two SARS-CoV-2 lineages with enhanced infectivity in Nigeria
Ozer, E. A., Simons, L. M., Adewumi, O. M., Fowotade, A. A., Omoruyi, E. C., Adeniji, J. A., Dean, T. J., Zayas, J., Bhimalli, P. P., Ash, M. K., et al. (2021) · doi:10.1101/2021.04.09.21255206 · Cited by 34
“The average age of the patients was 42 years (range [11-84]) and the gender distribution was 50% female and 50% male.”
Evolutionary analysis of Omicron variant BF.7 and BA.5.2 pandemic in China
Sun, Y., Wang, M., Lin, W., Dong, W., & Xu, J. (2023) · Journal of Biosafety and Biosecurity · doi:10.1016/j.jobb.2023.01.002 · Cited by 43
Booster dose of mRNA vaccine augments waning T cell and antibody responses against SARS-CoV-2
Kurt, F. G. Ö., Lepper, A., Gerhards, C., Roemer, M., Lasser, S., Arkhypov, I., Bitsch, R., Bugert, P., Altevogt, P., Gouttefangeas, C., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1012526 · Cited by 48
“Carrying a large number of mutations in its spike protein, this variant has a stronger binding capacity to human ACE2 protein (21) and an increased transmissibility (22) than the original strain.”
Background
The variants of SARS‐CoV‐2 and the challenges of vaccines
Han, X., & Ye, Q. (2021) · Journal of Medical Virology · doi:10.1002/jmv.27513 · Cited by 37
Spread of Mink SARS-CoV-2 Variants in Humans: A Model of Sarbecovirus Interspecies Evolution
Devaux, C. A., Pinault, L., Delerce, J., Raoult, D., Levasseur, A., & Frutos, R. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.675528 · Cited by 44
Key Substitutions in the Spike Protein of SARS-CoV-2 Variants Can Predict Resistance to Monoclonal Antibodies, but Other Substitutions Can Modify the Effects
Lusvarghi, 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
“Adaptive and immune selective pressures are problematic for nAbs selected from convalescent donors in early 2020, as the most potent antibodies were often against immune dominant epitopes involving the 484 position (15, 56, 62, 63).”
Background
Emergence 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
Potentiometric Biosensors Based on Molecular-Imprinted Self-Assembled Monolayer Films for Rapid Detection of Influenza A Virus and SARS-CoV-2 Spike Protein
Lee, W., Subramanian, A., Mueller, S., Levón, K., Nam, C., & Rafailovich, M. H. (2022) · ACS Applied Nano Materials · doi:10.1021/acsanm.2c00068 · Cited by 42
SARS-CoV-2 E484K Mutation Narrative Review: Epidemiology, Immune Escape, Clinical Implications, and Future Considerations
Yang, W.-T., Huang, W.-H., Liao, T.-L., Hsiao, T.-H., Chuang, H.-N., & Liu, P.-Y. (2022) · Infection and Drug Resistance · doi:10.2147/idr.s344099 · Cited by 51
“Greaney et al recognized that E484 plays a crucial role in neutralization by convalescent sera by mutated spike receptor-binding domain yeast library.(7) Assays such as authentic viruses and pseudoviruses with mutated spike protein were applied to evaluate the impacts of mutations on convalescent sera.”
Method
Immune response to SARS-CoV-2 variants: A focus on severity, susceptibility, and preexisting immunity
Alefishat, E. A., Jelinek, H. F., Mousa, M., Tay, G. K., & AlSafar, H. S. (2022) · Journal of Infection and Public Health · doi:10.1016/j.jiph.2022.01.007 · Cited by 39
“Invitro evidence demonstrates that the presence of the E484K mutation reduces the neutralization of multiclonal antibodies in convalescent sera [190].”
Mechanisms of SARS-CoV-2 neutralization by shark variable new antigen receptors elucidated through X-ray crystallography
Ubah, O. C., Lake, E. W., Gunaratne, G. S., Gallant, J. P., Fernie, M., Robertson, A. J., Marchant, J. S., Bold, T. D., Langlois, R. A., Matchett, W. E., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27611-y · Cited by 38
The Impact of Vaccination to Control COVID-19 Burden in the United States: A Simulation Modeling Approach
Alagoz, O., Sethi, A., Patterson, B., et al. (2021) · medRxiv · doi:10.1101/2021.03.22.21254131 · Cited by 36
Comparative Perturbation-Based Modeling of the SARS-CoV-2 Spike Protein Binding with Host Receptor and Neutralizing Antibodies : Structurally Adaptable Allosteric Communication Hotspots Define Spike Sites Targeted by Global Circulating Mutations
Verkhivker, G. M., Agajanian, S., Oztas, D., et al. (2021) · bioRxiv · doi:10.1101/2021.02.21.432165 · Cited by 36
Ferritin nanocages as efficient nanocarriers and promising platforms for COVID-19 and other vaccines development
Reutovich, A. A., Srivastava, A. K., Arosio, P., & Bou‐Abdallah, F. (2022) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2022.130288 · Cited by 41
“529) that evade vaccine-induced immunity (7, 8), posing issues for viral transmission and global vaccination efforts.”
Background
Selection analysis identifies unusual clustered mutational changes in Omicron lineage BA.1 that likely impact Spike functionPreprint
Martin, D. P., Lytras, S., Lucaci, A. G., Maier, W., Grüning, B. A., Shank, S. D., Weaver, S., MacLean, O. A., Orton, R. J., Lemey, P., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.14.476382 · Cited by 40
Self-citation
Prediction and Evolution of the Molecular Fitness of SARS-CoV-2 Variants: Introducing SpikePro
Pucci, F., & Rooman, M. J. (2021) · Viruses · doi:10.3390/v13050935 · Cited by 35
“We used deep mutagenesis scanning data from [53], in which the escape fractions of about 2000 single-site RBD variants were assessed on the neutralizing activity of plasma samples taken from 17 SARS-CoV-2-infected individuals, at different time points after infection.”
BackgroundMethodInfluential
Molecular Evolution of SARS-CoV-2 during the COVID-19 Pandemic
González-Vázquez, L. D., & Arenas, M. (2023) · Genes · doi:10.3390/genes14020407 · Cited by 44
Synthetic virions reveal fatty acid-coupled adaptive immunogenicity of SARS-CoV-2 spike glycoprotein
Staufer, O., Gupta, K., Bücher, J. E. H., Köhler, F., Sigl, C., Singh, G., Vasileiou, K., Relimpio, A. Y., Macher, M., Fabritz, S., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28446-x · Cited by 36
Antibody escape and global spread of SARS-CoV-2 lineage A.27
Kaleta, T., Kern, L., Hong, S. L., Hölzer, M., Kochs, G., Beer, J., Schnepf, D., Schwemmle, M., Bollen, N., Kolb, P., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28766-y · Cited by 33
S19W, T27W, and N330Y mutations in ACE2 enhance SARS-CoV-2 S-RBD binding toward both wild-type and antibody-resistant viruses and its molecular basis
Ye, F., Lin, X., Chen, Z., Yang, F., Lin, S., Yang, J., Chen, H., Sun, H., Wang, L., Wen, A., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00756-4 · Cited by 37
“Of note, the natural virus variant of SARS-CoV-2 bearing the E484K mutation in S-RBD, which is initially identified in South Africa, has drawn more and more attention.(49,50) The variant has been shown to exhibit strong resistance to human convalescent serum antibodies and a series of monoclonal neutralizing antibodie…”
Background
The hindrances to perform the COVID-19 vaccination in Brazil
Boschiero, M. N., Palamim, C. V. C., & Marson, F. A. L. (2021) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2021.1955607 · Cited by 41
Generation of a Sleeping Beauty Transposon-Based Cellular System for Rapid and Sensitive Screening for Compounds and Cellular Factors Limiting SARS-CoV-2 Replication
Widera, M., Wilhelm, A., Toptan, T., Raffel, J. M., Kowarz, E., Roesmann, F., Grözinger, F., Siemund, A. L., Luciano, V., Külp, M., et al. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.701198 · Cited by 41
Development of colorimetric sensors based on gold nanoparticles for SARS-CoV-2 RdRp, E and S genes detection
Rodríguez-Díaz, C., Lafuente‐Gómez, N., Coutinho, C., Pardo, D., Iniesta, H. A., López‐Valls, M., Coloma, R., Milán-Rois, P., Domenech, M., Abreu, M., et al. (2022) · Talanta · doi:10.1016/j.talanta.2022.123393 · Cited by 44
Regional and temporal coordinated mutation patterns in SARS-CoV-2 spike protein revealed by a clustering and network analysis
Negi, S. S., Schein, C. H., & Braun, W. A. (2022) · Scientific Reports · doi:10.1038/s41598-022-04950-4 · Cited by 35
SARS-CoV-2 Delta variant induces enhanced pathology and inflammatory responses in K18-hACE2 mice
Lee, K. S., Wong, T. Y., Russ, B. P., Horspool, A. M., Miller, O. A., Rader, N. A., Givi, J. P., Winters, M. T., Wong, Z. Y., Cyphert, H. A., et al. (2022) · PLoS ONE · doi:10.1371/journal.pone.0273430 · Cited by 42
“1) VOC, occur within the spike protein, which mediates 87 viral attachment and entry into host cells via the ACE2 receptor (25,26).”
Background
Development of an IgG-Fc fusion COVID-19 subunit vaccine, AKS-452
Alleva, D. G., Delpero, A. R., Scully, M. M., Murikipudi, S., Ragupathy, R., Greaves, E. K., Sathiyaseelan, T., Haworth, J. R., Shah, N. J., Rao, V., et al. (2021) · Vaccine · doi:10.1016/j.vaccine.2021.09.077 · Cited by 39
“It is worth noting that a recent study evaluating HCS binding to SP/RBD mutant proteins [45] demonstrated that the vast majority of SP binding was focused to SP/RBD epitopes (70% to 99% attributed to SP/RBD binding).”
Emerging vaccine-breakthrough SARS-CoV-2 variantsPreprint
Wang, R., Chen, J., Hozumi, Y., Yin, C., & Wei, G. (2021) · PubMed · doi:10.48550/arxiv.2109.04509 · Cited by 7
COVID-19 vaccine impact on rates of SARS-CoV-2 cases and post vaccination strain sequences among healthcare workers at an urban academic medical center: a prospective cohort study
(2021) · doi:10.1101/2021.03.30.21254655 · Cited by 49
“This allowed examination of vaccine effectiveness during a period of higher prevalence and increased SARS-CoV-2 viral diversity than in the initial clinical trials [2, 3].”
Background
Spherical neutralizing aptamer suppresses SARS-CoV-2 Omicron escape
Sun, M., Wu, Z., Zhang, J., Chen, M., Lu, Y. W. W., Yang, C. J., & Song, Y. (2022) · Nano Today · doi:10.1016/j.nantod.2022.101499 · Cited by 36
A SARS-CoV-2 Variant with L452R and E484Q Neutralization Resistance Mutations
Verghese, M., Jiang, B., Iwai, N., Mar, M., Sahoo, M. K., Yamamoto, F. F., Mfuh, K. O., Miller, J. A., Wang, H., Zehnder, J. L., et al. (2021) · Journal of Clinical Microbiology · doi:10.1128/jcm.00741-21 · Cited by 40
Leveraging deep learning to improve vaccine design
Hederman, A. P., & Ackerman, M. E. (2023) · Trends in Immunology · doi:10.1016/j.it.2023.03.002 · Cited by 41
Vaccination with S pan , an antigen guided by SARS-CoV-2 S protein evolution, protects against challenge with viral variants in mice
Zhao, Y., Ni, W., Liang, S., Dong, L., Xiang, M., Cai, Z., Niu, D., Zhang, Q., Wang, D., Zheng, Y., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.abo3332 · Cited by 34
“Changes in the E at position 484 to K, Q, or A reduced the neutralizing activity of antibodies by more than 10-fold (40, 41).”
Background
Genomic surveillance reveals the detection of SARS‐CoV‐2 delta, beta, and gamma VOCs during the third wave in Pakistan
Umair, M., Ikram, A., Salman, M., Haider, S. A., Badar, N., Rehman, Z., Ammar, M., Rana, M. S., & Ali, Q. (2021) · Journal of Medical Virology · doi:10.1002/jmv.27429 · Cited by 44
“It has been recently identified that these variants are capable of evading monoclonal and serum antibody responses.(9,10) The K417N/T, E484K, and N501Y mutations significantly decreased the neutralizing activity of convalescent and messenger RNA vaccine‐induced serum.”
Background
A Simple Reverse Transcriptase PCR Melting-Temperature Assay To Rapidly Screen for Widely Circulating SARS-CoV-2 Variants
Banada, P. P., Green, R., Banik, S., Chopoorian, A., Streck, D. L., Jones, R., Chakravorty, S., & Alland, D. (2021) · Journal of Clinical Microbiology · doi:10.1128/jcm.00845-21 · Cited by 61
The COVID-19 vaccine development: A pandemic paradigm
Carneiro, D. D. C., Sousa, J. D. O., & Monteiro-Cunha, J. P. (2021) · Virus Research · doi:10.1016/j.virusres.2021.198454 · Cited by 37
Three SARS-CoV-2 reinfection cases by the new Variant of Concern (VOC) P.1/501Y.V3Preprint
Naveca, F. G., da Costa, C. F., do Nascimento, V. A., de Souza, V. C., Corado, A. D. L. G., Nascimento, F., Costa, Á., Duarte, D., Silva, G., Mejía, M., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-318392/v1 · Cited by 83
A Simple RT-PCR Melting temperature Assay to Rapidly Screen for Widely Circulating SARS-CoV-2 Variants.
Banada, P., Green, R., Banik, S., et al. (2021) · medRxiv · doi:10.1101/2021.03.05.21252709 · Cited by 31
“7 caused a decrease in vaccine efficacy (5-8).”
Background
Impact of the B.1.1.7 variant on neutralizing monoclonal antibodies recognizing diverse epitopes on SARS-CoV-2 Spike
Graham, 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
Antigenic 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
Waning and boosting of antibody Fc-effector functions upon SARS-CoV-2 vaccination
Tong, X., McNamara, R. P., Avendaño, M. J., Serrano, E. F., García‐Salum, T., Pardo‐Roa, C., Bertera, H. L., Chicz, T. M., Lévican, J., Poblete, E., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39189-8 · Cited by 38
Dominant CD8+ T Cell Nucleocapsid Targeting in SARS-CoV-2 Infection and Broad Spike Targeting From Vaccination
Taus, E., Hofmann, C., Ibarrondo, F. J., Hausner, M. A., Fulcher, J. A., Krogstad, P. A., Ferbas, K. G., Tobin, N. H., Rimoin, A. W., Aldrovandi, G. M., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.835830 · Cited by 31
Evolution of the SARS-CoV-2 genome and emergence of variants of concern
Safari, I., & Elahi, E. (2021) · Archives of Virology · doi:10.1007/s00705-021-05295-5 · Cited by 41
SARS CoV-2 Delta variant exhibits enhanced infectivity and a minor decrease in neutralization sensitivity to convalescent or post-vaccination sera
Kuzmina, A., Wattad, S., Khalaila, Y., Ottolenghi, A., Rosental, B., Engel, S., Rosenberg, E., & Taube, R. (2021) · iScience · doi:10.1016/j.isci.2021.103467 · Cited by 33
“Among these, E484K and K417N are key for antibody escape and reduced sensitivity to administrated vaccines (Greaney et al., 2021; Kuzmina et al., 2021; Starr et al., 2020; Xie et al., 2021) (Baum et al., 2020; Ku et al., 2021; Weisblum et al., 2020; Wibmer et al., 2021) (Andreano et al., 2021; Xie…”
Background
Role of SARS-CoV-2 and ACE2 variations in COVID-19
Antony, P., & Vijayan, R. (2021) · Biomedical Journal · doi:10.1016/j.bj.2021.04.006 · Cited by 32
“The E484K mutation has been identiﬁed as a neutralizing antibody escape mutation, which suggest a change in antigenicity [85].”
Antibodies to the SARS-CoV-2 receptor-binding domain that maximize breadth and resistance to viral escapePreprint
Starr, T. N., Czudnochowski, N., Zatta, F., Park, Y., Liu, Z., Addetia, A., Pinto, D., Beltramello, M., Hernandez, P., Greaney, A. J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.06.438709 · Cited by 24
Self-citation
Characterisation of B.1.1.7 and Pangolin coronavirus spike provides insights on the evolutionary trajectory of SARS-CoV-2Preprint
Dicken, S. J., Murray, M. J., Thorne, L., Reuschl, A., Forrest, C., Ganeshalingham, M., Muir, L., Kalemera, M. D., Palor, M., McCoy, L. E., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.22.436468 · Cited by 30
Artificial Cell Membrane Polymersome-Based Intranasal Beta Spike Formulation as a Second Generation Covid-19 Vaccine
Lam, J. H., Shivhare, D., Chia, T. W., Chew, S. L., Sinsinbar, G., Aw, T. Y., Wong, S., Venkataraman, S., Lim, F. W. I., Vandepapelière, P., et al. (2022) · ACS Nano · doi:10.1021/acsnano.2c06350 · Cited by 33
COVID-19: vaccines, efficacy and effects on variants
Rudan, I., Adeloye, D., & Sheikh, A. (2022) · Current Opinion in Pulmonary Medicine · doi:10.1097/mcp.0000000000000868 · Cited by 34
Identifying SARS-CoV-2 antiviral compounds by screening for small molecule inhibitors of Nsp5 main protease
Milligan, J. C., Zeisner, T. U., Papageorgiou, G., Joshi, D., Soudy, C., Ulferts, R., Wu, M., Lim, C. T., Tan, K. W., Weissmann, F., et al. (2021) · Biochemical Journal · doi:10.1042/bcj20210197 · Cited by 66
How will emerging SARS-CoV-2 variants impact herd immunity?
Lippi, G., & Henry, B. M. (2021) · Annals of Translational Medicine · doi:10.21037/atm-21-893 · Cited by 33
“Beside the previously mentioned enhanced transmissibility of viral variants containing the N501Y mutations, additional concern has been raised that the E484K mutation within the receptor biding domain (RBD) of the spike protein may enable the virus to partially escape recognition by the host immune system, as attested…”
Background
Human immunoglobulin from transchromosomic bovines hyperimmunized with SARS-CoV-2 spike antigen efficiently neutralizes viral variants
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
Improving family access to dying patients during the COVID-19 pandemic
Downar, J., & Kekewich, M. (2021) · The Lancet Respiratory Medicine · doi:10.1016/s2213-2600(21)00025-4 · Cited by 35
Neutralizing Antibody Responses to SARS-CoV-2 in Recovered COVID-19 Patients Are Variable and Correlate With Disease Severity and Receptor-Binding Domain Recognition
Macioła, A. K., Raja, M. L., Pacenti, M., Salata, C., Silvestro, G. D., Rosato, A., & Pasqual, G. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.830710 · Cited by 31
The Variation of SARS-CoV-2 and Advanced Research on Current Vaccines
Jiang, Y., Wu, Q. Y., Song, P., & You, C. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2021.806641 · Cited by 34
“It is worth noting that the nucleotide substitution of G23012A in the Beta variant participated in the E484Kmutation, considered to involve in altering viral antigenicity and in turn causing low efficacy of vaccines (44, 47, 48).”
Background
Molecular docking and pharmacokinetic studies of phytocompounds from Nigerian Medicinal Plants as promising inhibitory agents against SARS-CoV-2 methyltransferase (nsp16)
Saliu, T. P., Umar, H. I., Ogunsile, O. J., Okpara, M. O., Yanaka, N., & Elekofehinti, O. O. (2021) · Journal of Genetic Engineering and Biotechnology · doi:10.1186/s43141-021-00273-5 · Cited by 32
“1; and the other emerging variants are complicating the global burden of COVID19 [4, 5].”
BackgroundInfluential
Shooting at a Moving Target—Effectiveness and Emerging Challenges for SARS-CoV-2 Vaccine Development
Günl, F., Mecate-Zambrano, A., Rehländer, S., Hinse, S., Ludwig, S., & Brunotte, L. (2021) · Vaccines · doi:10.3390/vaccines9101052 · Cited by 27
Characterization of a Novel ACE2-Based Therapeutic with Enhanced Rather than Reduced Activity against SARS-CoV-2 Variants
Ferrari, M., Mekkaoui, L., Ilca, F. T., Akbar, Z., Bughda, R., Lamb, K., Ward, K., Parekh, F., Karattil, R., Allen, C. G., et al. (2021) · Journal of Virology · doi:10.1128/jvi.00685-21 · Cited by 37
Comprehensive Comparison of Seven SARS-CoV-2-Specific Surrogate Virus Neutralization and Anti-Spike IgG Antibody Assays Using a Live-Virus Neutralization Assay as a Reference
Graninger, M., Jani, C. M., Reuberger, E., Prüger, K., Gaspar, P., Springer, D. N., Borsodi, C., Weidner, L., Rabady, S., Puchhammer‐Stöckl, E., et al. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.02314-22 · Cited by 29
Variable loss of antibody potency against SARS-CoV-2 B.1.1.529 (Omicron)Preprint
Sheward, D. J., Kim, C., Ehling, R. A., Pankow, A. P., Dopico, X. C., Martin, D. P., Reddy, S. T., Dillner, J., Hedestam, G. B. K., Albert, J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.19.473354 · Cited by 17
Deepening of In Silico Evaluation of SARS-CoV-2 Detection RT-qPCR Assays in the Context of New Variants
Gand, M., Vanneste, K., Thomas, I., Gucht, S. V., Capron, A., Herman, P., Roosens, N. H. C., & Keersmaecker, S. C. J. D. (2021) · Genes · doi:10.3390/genes12040565 · Cited by 29
Probabilistic Approach to COVID-19 Data Analysis and Forecasting Future Outbreaks Using a Multi-Layer Perceptron Neural Network
Khan, R. U., Almakdi, S., Alshehri, M. S., Kumar, R., Ali, I., Hussain, S. M., Haq, A. U., Khan, I. U., Ullah, A., & Uddin, M. I. (2022) · Diagnostics · doi:10.3390/diagnostics12102539 · Cited by 29
Interpreting the B-cell receptor repertoire with single-cell gene expression using Benisse
Zhang, Z., Chang, W. Y., Wang, K., Yang, Y., Wang, X., Yao, C., Wu, T., Wang, L. L., & Wang, T. (2022) · Nature Machine Intelligence · doi:10.1038/s42256-022-00492-6 · Cited by 25
Ready-to-use public infrastructure for global SARS-CoV-2 monitoring
Maier, W., Bray, S. A., van den Beek, M., Bouvier, D., Coraor, N., Miladi, M., Singh, B., Rambla, J., Baker, D., Roach, N. P., et al. (2021) · Nature Biotechnology · doi:10.1038/s41587-021-01069-1 · Cited by 25
Applications of laboratory findings in the prevention, diagnosis, treatment, and monitoring of COVID-19
Meng, Z., Guo, S., Zhou, Y., Li, M., Wang, M., & Ying, B. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00731-z · Cited by 35
A Possible Role of Remdesivir and Plasma Therapy in the Selective Sweep and Emergence of New SARS-CoV-2 Variants
Colson, P., Devaux, C. A., Lagier, J., Gautret, P., & Raoult, D. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10153276 · Cited by 22
“Furthermore, these mutations can lead to immune escape, as shown in several in vitro studies [35,43,44].”
Background
Comprehensive Deep Mutational Scanning Reveals the Immune-Escaping Hotspots of SARS-CoV-2 Receptor-Binding Domain Targeting Neutralizing Antibodies
Tsai, K., Lee, Y.-C., & Tseng, T.-S. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.698365 · Cited by 32
TMPRSS2 and RNA-Dependent RNA Polymerase Are Effective Targets of Therapeutic Intervention for Treatment of COVID-19 Caused by SARS-CoV-2 Variants (B.1.1.7 and B.1.351)
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).”
Background
Titers of antibodies against ancestral SARS-CoV-2 correlate with levels of neutralizing antibodies to multiple variants
Tran, T. T., Vaage, E. B., Mehta, A., Chopra, A., Tietze, L., Kolderup, A., Anthi, A. K., König, M. S. S., Nygaard, G. O., Lind, A., et al. (2022) · npj Vaccines · doi:10.1038/s41541-022-00586-7 · Cited by 47
Plant-produced SARS-CoV-2 receptor binding domain (RBD) variants showed differential binding efficiency with anti-spike specific monoclonal antibodies
Rattanapisit, K., Bulaon, C. J. I., Khorattanakulchai, N., Shanmugaraj, B., Wangkanont, K., & Phoolcharoen, W. (2021) · PLoS ONE · doi:10.1371/journal.pone.0253574 · Cited by 26
“In contrast, the E484K (Beta) mutation is of great concern, since it enhances binding affinity with ACE2 and reduces the binding interactions with neutralizing antibodies [37] and polyclonal serum antibodies [38] compromising the neutralization.”
Background
The Genetic Variant of SARS-CoV-2: Would it matter for Controlling the Devastating Pandemic?
Guo, S., Liu, K., & Zheng, J. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.59137 · Cited by 46
“Indeed, a single mutation in reside 484 was previously shown to significantly reduce the neutralization by several monoclonal antibodies and sera [73, 79].”
Background
Unsuppressed HIV infection impairs T cell responses to SARS-CoV-2 infection and abrogates T cell cross-recognition
Nkosi, T., Chasara, C., Mbatha, A., Nsimbi, M., Papadopoulos, A. O., Nguni, T. L., Karim, F., Moosa, M. Y. S., Gazy, I., Jambo, K., et al. (2022) · eLife · doi:10.7554/elife.78374 · Cited by 31
“These mutations have been shown to directly affect ACE2 receptor binding affinity, infectivity, viral load, and transmissibility (40-42).”
Background
A tale of three SARS-CoV-2 variants with independently acquired P681H mutations in New York StatePreprint
Lasek‐Nesselquist, E., Pata, J. D., Schneider, E., & George, K. S. (2021) · medRxiv · doi:10.1101/2021.03.10.21253285 · Cited by 22
Mutations in the SARS-CoV-2 spike protein modulate the virus affinity to the human ACE2 receptor, an in silico analysis
Ortega, J. T., Pujol, F. H., Jastrzębska, B., & Rangel, H. R. (2021) · EXCLI journal · doi:10.17179/excli2021-3471 · Cited by 26
A combination of cross-neutralizing antibodies synergizes to prevent SARS-CoV-2 and SARS-CoV pseudovirus infection
Liu, H., Yuan, M., Huang, D.-L., Bangaru, S., Lee, C. D., Peng, L., Zhu, X.-Y., Nemazee, D., van Gils, M. V., Sanders, R., et al. (2021) · bioRxiv · doi:10.1101/2021.02.11.430866 · Cited by 24
“The RBS is also prone to naturally occurring mutations, similar to the N-terminal domain (NTD), where insertions and deletions have also been found (Greaney et al., 2021b; Kemp et al., 2021; Liu et al., 2021; McCarthy et al., 2020; Starr et al., 2020; Tegally et al., 2020; Van Egeren et al., 2020;…”
BackgroundInfluential
Immunoinformatics Study: Multi-Epitope Based Vaccine Design from SARS-CoV-2 Spike Glycoprotein
Umitaibatin, R., Harisna, A. H., Jauhar, M. M., Syaifie, P. H., Arda, A. G., Nugroho, D., Ramadhan, D., Mardliyati, E., Shalannanda, W., & Anshori, I. (2023) · Vaccines · doi:10.3390/vaccines11020399 · Cited by 26
“Several studies reported that these mutations can evade monoclonal antibodies [56,61] and influence polyclonal antibody recognition [62,63].”
Background
Sertraline 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
Impact of SARS-CoV-2 Variants on the Analytical Sensitivity of rRT-PCR Assays
Chen, Y., Han, Y., Yang, J., Ma, Y., Li, J., & Zhang, R. (2022) · Journal of Clinical Microbiology · doi:10.1128/jcm.02374-21 · Cited by 24
“The E484K mutation presented in the Beta and Gamma variants can facilitate evasion from the host immune system (8), thereby reducing the neutralization activity of the vaccine against the variants (9).”
Background
Coronavirus Genomes and Unique Mutations in Structural and Non-Structural Proteins in Pakistani SARS-CoV-2 Delta Variants during the Fourth Wave of the Pandemic
Anwar, M. Z., Lodhi, M. S., Khan, M. T., Khan, M. I., & Sharif, S. (2022) · Genes · doi:10.3390/genes13030552 · Cited by 21
Functional Effects of Receptor-Binding Domain Mutations of SARS-CoV-2 B.1.351 and P.1 Variants
Bayarri‐Olmos, R., Jarlhelt, I., Johnsen, L. B., Hansen, C. B., Helgstrand, C., Bjelke, J. R., Matthiesen, F., Nielsen, S. D., Iversen, K. K., Ostrowski, S. R., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.757197 · Cited by 25

Authors: Greaney, A. J., Loes, A. N., Crawford, K. H. D., Starr, T. N., Malone, K. D., Chu, H. Y., & Bloom, J. D.
Affiliations: University of Washington (US)
Howard Hughes Medical Institute (US)
Fred Hutch Cancer Center (US)
Corresponding author: Bloom, Jesse D.
ORCID: Greaney, Allison J.
Loes, Andrea N.
Crawford, Katharine H.D.
Starr, Tyler N.
Chu, Helen Y.
Bloom, Jesse D.
Venue: Cell Host & Microbe
Publisher: openRxiv
Published: 2021-01-04
Volume: 29
Issue: 3
Pages: 463-476.e6
ISSN: 1931-3128 (ISSN-L)
DOI: 10.1101/2020.12.31.425021
PMC: PMC7869748
OpenAlex: W3127852352
Cited by: 1,178
References: 58
Citations by year: 2026: 43 · 2025: 64 · 2024: 79 · 2023: 158 · 2022: 361 · 2021: 459
FWCI: 83.77
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Cell Host & Microbe (publishedVersion)
bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Howard Hughes Medical Institute
Bill and Melinda Gates Foundation (INV-004949)
Damon Runyon Cancer Research Foundation (DRG-2381-19)
Washington Research Foundation
Vanderbilt University
University of Washington
National Institutes of Health (1s10od028685-01)
National Institute of Allergy and Infectious Diseases (R01AI127893, T32AI083203, F30AI149928, R01AI140891, R01AI141707)
Office of Research Infrastructure Programs, National Institutes of Health (S10OD028685)
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
Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 detection and testing
Keywords: SARS-CoV-2, spike protein receptor-binding domain, antibody escape mutations, neutralizing antibodies, E484K mutation, antibody epitopes, convalescent plasma, humoral immunity
MeSH terms: Protein Domains, COVID-19, SARS-CoV-2, Adult, Aged, Antibodies, Monoclonal, Antibodies, Viral, Binding Sites, Cell Line, Female, Humans, Male, Middle Aged, Mutation, Prospective Studies, Protein Binding, Receptors, Virus, Young Adult, Antibodies, Neutralizing, 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

Comprehensive mapping of mutations to the SARS-CoV-2 receptor-binding domain that affect recognition by polyclonal human serum antibodies

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks