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

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

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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

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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.

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“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).”
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“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…”
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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×
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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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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

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Why are some coronavirus variants more infectious?
Mukherjee, R., & Satardekar, R. (2021) · Journal of Biosciences · doi:10.1007/s12038-021-00221-y · Cited by 23
“The escape maps identified few major epitopes or hot spots in the RBD, which often acquire mutations to evade neutralization by antibodies targeting a wide surface, with the E484 residue showing the maximum impact on binding (Greaney et al. 2021a).”
Background
Developing Cytokine Storm-Sensitive Therapeutic Strategy in COVID-19 Using 8P9R Chimeric Peptide and Soluble ACE2
Nazerian, Y., Vakili, K. G., Ebrahimi, A., & Niknejad, H. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.717587 · Cited by 22
Previous Infection Combined with Vaccination Produces Neutralizing Antibodies with Potency against SARS-CoV-2 Variants
Ibarrondo, F. J., Hofmann, C., Ali, A., Ayoub, P., Kohn, D. B., & Yang, O. O. (2021) · mBio · doi:10.1128/mbio.02656-21 · Cited by 17
Emerging concerns regarding COVID‐19; second wave and new variant
Hafeez, S., Din, M., Zia, F., Ali, M., & Shinwari, Z. K. (2021) · Journal of Medical Virology · doi:10.1002/jmv.26979 · Cited by 27
“protein of coronavirus, if a mutation modifies one of the antibody target regions, it could decrease that specific antibody's binding activity.(19)”
Background
A rapid, cost efficient and simple method to identify current SARS-CoV-2 variants of concern by Sanger sequencing part of the spike protein genePreprint
Jørgensen, T. S., Blin, K., Kuntke, F., Salling, H. K., Michaelsen, T. Y., Albertsen, M., & Larsen, H. (2021) · medRxiv · doi:10.1101/2021.03.27.21252266 · Cited by 16
Mechanisms of Hepatitis C Virus Escape from Vaccine-Relevant Neutralizing Antibodies
Velázquez‐Moctezuma, R., Augestad, E. H., Castelli, M., Olesen, C. H., Clementi, N., Clementi, M., Mancini, N., & Prentoe, J. C. (2021) · Vaccines · doi:10.3390/vaccines9030291 · Cited by 18
“Further, many of the escape mutations identified in vitro have already been observed in circulating human isolates [126,127].”
Background
Memory B Cells and Memory T Cells Induced by SARS-CoV-2 Booster Vaccination or Infection Show Different Dynamics and Responsiveness to the Omicron Variant
Mise‐Omata, S., Ikeda, M., Takeshita, M., Uwamino, Y., Wakui, M., Arai, T., Yoshifuji, A., Murano, K., Siomi, H., Nakagawara, K., et al. (2022) · The Journal of Immunology · doi:10.4049/jimmunol.2200525 · Cited by 20
Identification of SARS-CoV-2 Variants of Concern Using Amplicon Next-Generation Sequencing
Nasereddin, A., Golan-Berman, H., Wolf, D. G., Oiknine‐Djian, E., & Adar, S. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.00736-22 · Cited by 21
Deep mutational engineering of broadly-neutralizing nanobodies accommodating SARS-CoV-1 and 2 antigenic drift
Laroche, A., Delgado, M. L. O., Chalopin, B., Cuniasse, P., DuBois, S. G., Sierocki, R., Gallais, F., Debroas, S., Bellanger, L., Simon, S., et al. (2022) · mAbs · doi:10.1080/19420862.2022.2076775 · Cited by 21
“standing of the interaction modalities, as recently shown for the RBD/ACE2 and RBD/antibodies interactions.(12,13,39,40) In this work, we used these systematic mutagenesis data to engineer new nanobodies with improved affinity and tailored selectivity.”
Method
Research progress on vaccine efficacy against SARS-CoV-2 variants of concern
Bian, L., Liu, J., Gao, F., Gao, Q., He, Q., Mao, Q., Wu, X., Xu, M., & Liang, Z. (2022) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2022.2057161 · Cited by 30
“Greaney et al.(34) found that E484K reduces the neutralizing potency of convalescent sera from some donors by 10-fold.”
Background
Computer Simulations and Network-Based Profiling of Binding and Allosteric Interactions of SARS-CoV-2 Spike Variant Complexes and the Host Receptor: Dissecting the Mechanistic Effects of the Delta and Omicron Mutations
Verkhivker, G. M., Agajanian, S., Kassab, R., & Krishnan, K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23084376 · Cited by 18
COVID-19 Genetic Variants and Their Potential Impact in Vaccine Development
Giau, V. V., Bagyinszky, E., & An, S. S. A. (2022) · Microorganisms · doi:10.3390/microorganisms10030598 · Cited by 21
RBD Double Mutations of SARS-CoV-2 Strains Increase Transmissibility through Enhanced Interaction between RBD and ACE2 Receptor
Sinha, S., Tam, B., & Wang, S. M. (2021) · Viruses · doi:10.3390/v14010001 · Cited by 22
SARS-CoV-2 Delta variant pathogenesis and host response in Syrian hamsters
Sreelekshmy, M., Dhruv, Y. P., Anita, S., et al. (2021) · bioRxiv · doi:10.1101/2021.07.24.453631 · Cited by 17
“3 possesses the E484Q mutation which is a known site in RBD which can impact the serum neutralization efficiency [6].”
Background
SARS-CoV-2 variants: A double-edged sword?
Jogalekar, M. P., Veerabathini, A., & Gangadaran, P. (2021) · Experimental Biology and Medicine · doi:10.1177/15353702211014146 · Cited by 24
“351 via evasion of antibody neutralization by convalescent plasma and vaccines,(19) and monoclonal antibodies,(7) although there is a lot of inter- and intra-person heterogeneity in terms of the effect of E484K on antibody binding.(20) In some cases, the potency of plasma was even reduced by 10-fold.”
Background
Pharmaceutical Aspects and Clinical Evaluation of COVID-19 Vaccines
Hofman, K., Shenoy, G. N., Chak, V., & Balu‐Iyer, S. V. (2021) · Immunological Investigations · doi:10.1080/08820139.2021.1904977 · Cited by 20
“1 (Brazil) (Greaney et al. 2021; Vasques Nonaka et al. 2021; Weisblum et al. 2020), raising legitimate concerns about the cross-protective ability of the vaccines being developed.”
BackgroundInfluential
Elicitation of broadly protective sarbecovirus immunity by receptor-binding domain nanoparticle vaccines
Walls, A., Miranda, M. C., Pham, M. N., Schäfer, A., Greaney, A. J., Arunachalam, P. S., Navarro, M., Tortorici, M. A., Rogers, K. A., O'Connor, M. A., et al. (2021) · bioRxiv · doi:10.1101/2021.03.15.435528 · Cited by 19
“Note that these filtering criteria are slightly more stringent than those used in 38 but are identical to those used in 14,84 .”
BackgroundMethodInfluentialSelf-citation
Deep mutagenesis scanning using whole trimeric SARS-CoV-2 spike highlights the importance of NTD-RBD interactions in determining spike phenotype
Kugathasan, R., Sukhova, K., Moshe, M., Kellam, P., & Barclay, W. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011545 · Cited by 16
“RBD-directed antibodies account for ~90% of the neutralising antibody response of convalescent [7] and vaccine sera [8], while neutralising NTD antibodies contribute a minority [18].”
BackgroundInfluential
Identification of broad, potent antibodies to functionally constrained regions of SARS-CoV-2 spike following a breakthrough infection
Guenthoer, J., Lilly, M., Starr, T. N., Dadonaite, B., Lovendahl, K. N., Croft, J. T., Stoddard, C. I., Chohan, V., Ding, S.-L., Ruiz, F., et al. (2022) · bioRxiv · doi:10.1101/2022.12.15.520606 · Cited by 17
“1) had 15 mutations in the RBD that collectively altered binding across all of the RBD mAb classes (33), resulting in reduced activity of the majority of RBD-targeting mAbs (29, 32, 34-36).”
BackgroundResultSelf-citation
A novel plant‐made monoclonal antibody enhances the synergetic potency of an antibody cocktail against the SARS‐CoV ‐2 Omicron variant
Jugler, C., Sun, H., Nguyen, K., Palt, R., Felder, M., Steinkellner, H., & Chen, Q. (2022) · Plant Biotechnology Journal · doi:10.1111/pbi.13970 · Cited by 16
“This will potentially reduce neutralizing potency of host antibody response against the new variants (Greaney et al., 2021; Hoffmann et al., 2021) and, in some cases, abolish the utility of previously potent therapeutic mAbs (Chen et al.”
BackgroundInfluential
Long-term SARS-CoV-2 Asymptomatic Carriage in an Immunocompromised Host: Clinical, Immunological, and Virological Implications
Spinicci, M., Mazzoni, A., Coppi, M., Antonelli, A., Salvati, L., Maggi, L., Basile, G., Graziani, L., Lauria, N. D., Pilato, V. D., et al. (2022) · Journal of Clinical Immunology · doi:10.1007/s10875-022-01313-6 · Cited by 19
“001%) according to GISAID (last accessed on April 29, 2022); (iii) G446V, which was located in the receptor-binding domain (RBD) and was related with in vitro decreased sensitivity to convalescent sera [17] and monoclonal antibody REGN10987 [18]; and (iv) N679K, which was described both in the South African C.”
Immune transcriptome analysis of COVID-19 patients infected with SARS-CoV-2 variants carrying the E484K escape mutation identifies a distinct gene module
Lee, H., Knabl, L., Knabl, L., Wieser, M., Mur, A., Zabernigg, A., Schumacher, J., Kapferer, S., Kaiser, N., Furth, P. A., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-06752-0 · Cited by 15
Emergence and spread of a sub-lineage of SARS-CoV-2 Alpha variant B.1.1.7 in Europe, and with further evolution of spike mutation accumulations shared with the Beta and Gamma variants
Stadtmüller, M., Laubner, A., Rost, F., Winkler, S., Patrasová, E., Šimůnková, L., Reinhardt, S., Beil, J., Dalpke, A. H., & Yi, B. (2022) · Virus Evolution · doi:10.1093/ve/veac010 · Cited by 24
Pseudotyped Bat Coronavirus RaTG13 is efficiently neutralised by convalescent sera from SARS-CoV-2 infected patients
Cantoni, D. M., Neto, M. M., Thakur, N., Elrefaey, A. M. E., Newman, J., Vishwanath, S., Nadesalingam, A., Chan, A., Smith, P., Castillo‐Olivares, J., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03325-9 · Cited by 17
Genomic reconstruction of the SARS-CoV-2 epidemic in EnglandPreprint
Vöhringer, H. S., Sanderson, T., Sinnott, M., et al. (2021) · medRxiv · doi:10.1101/2021.05.22.21257633 · Cited by 29
The SARS-CoV-2 mRNA-1273 vaccine elicits more RBD-focused neutralization, but with broader antibody binding within the RBDPreprint
Greaney, A. J., Loes, A. N., Gentles, L. E., et al. (2021) · bioRxiv · doi:10.1101/2021.04.14.439844 · Cited by 16
“FACS sorting of yeast libraries to select mutants with reduced binding by polyclonal post-vaccination sera Serum mapping experiments were performed in biological duplicate using the independent mutant RBD libraries, similarly to as previously described for monoclonal antibodies (22) and exactly as previously described…”
MethodSelf-citation
SARS CoV-2 escape variants exhibit differential infectivity and neutralization sensitivity to convalescent or post-vaccination sera
Kuzmina, A., Khalaila, Y., Voloshin, O., Keren-Naus, A., Bohehm, L., Raviv, Y., Shemer-Avni, Y., Rosenberg, E., & Taube, R. (2021) · medRxiv · doi:10.1101/2021.02.22.21252002 · Cited by 17
“…mutation N501Y in the B.1.1.7 strain does not compromise post vaccine serum neutralization (Shi et al., 2021), E484K partly impairs neutralization (Greaney et al., 2021), potentially compromising effectiveness of neutralizing sera and currently available vaccines (Baum et al., 2020; Ku et al.,…”
Influential
Neutralizing and enhancing antibodies against SARS-CoV-2
Liu, Y., & Arase, H. (2022) · Inflammation and Regeneration · doi:10.1186/s41232-022-00233-7 · Cited by 13
Two Years of Genomic Surveillance in Belgium during the SARS-CoV-2 Pandemic to Attain Country-Wide Coverage and Monitor the Introduction and Spread of Emerging Variants
Cuypers, L., Dellicour, S., Hong, S. L., Potter, B. I., Verhasselt, B., Vereecke, N., Lambrechts, L., Durkin, K., Bours, V., Klamer, S., et al. (2022) · Viruses · doi:10.3390/v14102301 · Cited by 17
The role of single-domain antibodies (or nanobodies) in SARS-CoV-2 neutralization
Zebardast, A., Hosseini, P., Hasanzadeh, A., & Latifi, T. (2021) · Molecular Biology Reports · doi:10.1007/s11033-021-06819-7 · Cited by 19
A Comprehensive Molecular Epidemiological Analysis of SARS-CoV-2 Infection in Cyprus from April 2020 to January 2021: Evidence of a Highly Polyphyletic and Evolving Epidemic
Chrysostomou, A. C., Vrancken, B., Koumbaris, G., Themistokleous, G., Aristokleous, A., Masia, C., Eleftheriou, C., Iοannou, C., Stylianou, D. C., Ioannides, M., et al. (2021) · Viruses · doi:10.3390/v13061098 · Cited by 15
“Namely, the uncommon G446V mutation has been reported to reduce serum binding and neutralization [68].”
Background
Kinetics of Neutralizing Antibodies of COVID-19 Patients Tested Using Clinical D614G, B.1.1.7, and B 1.351 Isolates in Microneutralization Assays
Virtanen, J. M. E., Uusitalo, R., Korhonen, E. M., Aaltonen, K., Smura, T., Kuivanen, S. H., Pakkanen, S. H., Mero, S., Patjas, A., Riekkinen, M., et al. (2021) · Viruses · doi:10.3390/v13060996 · Cited by 25
“7) or the older dominant strains, including studies in vaccinees [5,8,11,13,26,27].”
BackgroundResult
The Role of Host Cell Glycans on Virus Infectivity: The SARS‐CoV‐2 Case
Acosta-Gutiérrez, S., Buckley, J., & Battaglia, G. (2021) · bioRxiv · doi:10.1101/2021.05.08.443212 · Cited by 15
Limited Neutralization of Authentic Severe Acute Respiratory Syndrome Coronavirus 2 Variants Carrying E484K In Vitro
Widera, M., Wilhelm, A., Hoehl, S., Pallas, C., Kohmer, N., Wolf, T., Rabenau, H. F., Corman, V. M., Drosten, C., Vehreschild, M. J. G. T., et al. (2021) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiab355 · Cited by 88
“Further studies have shown that of E484K represents an immunodominant site on the RBD since E484K reduced naturalization capacity of human convalescent sera by >100-fold [1-4].”
Background
The End or a New Era of Development of SARS-CoV-2 Virus: Genetic Variants Responsible for Severe COVID-19 and Clinical Efficacy of the Most Commonly Used Vaccines in Clinical Practice
Miteva, D., Kitanova, M., Batselova, H., Lazova, S., Chervenkov, L., Peshevska-Sekulovska, M., Sekulovski, M., Gulinac, M., Vasilev, G., Tomov, L., et al. (2023) · Vaccines · doi:10.3390/vaccines11071181 · Cited by 16
SARS-CoV-2 Variants, Current Vaccines and Therapeutic Implications for COVID-19
Liang, H., Wu, Y., Yau, V., Yin, H.-X., Lowe, S., Bentley, R., Ahmed, M. A., Zhao, W., & Sun, C. (2022) · Vaccines · doi:10.3390/vaccines10091538 · Cited by 16
“Unlike most other RBD mutations, T478K retains sensitivity to all but a few mAbs, and to most convalescent and post-vaccination plasma samples [27,30,48,49].”
Background
A Complementary Union of SARS-CoV2 Natural and Vaccine Induced Immune Responses
Torresi, J., Edeling, M. A., Nolan, T. M., & Godfrey, D. I. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.914167 · Cited by 15
Structural and Computational Studies of the SARS-CoV-2 Spike Protein Binding Mechanisms with Nanobodies: From Structure and Dynamics to Avidity-Driven Nanobody Engineering
Verkhivker, G. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23062928 · Cited by 17
Phylogenetic and full-length genome mutation analysis of SARS-CoV-2 in Indonesia prior to COVID-19 vaccination program in 2021
Nidom, R. V., Indrasari, S., Normalina, I., Nidom, A. N., Afifah, B., Dewi, L., Putra, A. K., Ansori, A. N. M., Kusala, M. K. J., Alamudi, M. Y., et al. (2021) · Bulletin of the National Research Centre/Bulletin of the National Research Center · doi:10.1186/s42269-021-00657-0 · Cited by 28
Structural and energetic profiling of SARS-CoV-2 receptor binding domain antibody recognition and the impact of circulating variants
Yin, R. M., Guest, J. D., Taherzadeh, G., Gowthaman, R., Mittra, I., Quackenbush, J., & Pierce, B. G. (2021) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1009380 · Cited by 18
“Several recent studies have used in vitro experimental approaches to test human sera [8,10] and sets of monoclonal antibodies [5,8,11,12] to profile SARS-CoV-2 antibody resistance.”
Background
Immunogenic amino acid motifs and linear epitopes of COVID-19 mRNA vaccines
Wisnewski, A. V., Redlich, C. A., Kamath, K., Abad, Q.-A., Smith, R., Fazen, L. E., Santiago, R., Liu, J., Luna, J. C., Martinez, B., et al. (2021) · PLoS ONE · doi:10.1371/journal.pone.0252849 · Cited by 16
A new SARS-CoV-2 variant poorly detected by RT-PCR on nasopharyngeal samples, with high lethality
Fillâtre, P., Dufour, M.-J., Behillil, S., et al. (2021) · medRxiv · doi:10.1101/2021.05.05.21256690 · Cited by 14
Practical guidance for clinical laboratories for SARS-CoV-2 serology testing
Charlton, C. L., Kanji, J. N., Tran, V., Kus, J. V., Gubbay, J. B., Osiowy, C., Robinson, J. L., Sekirov, I., DREBOT, M. A., Hatchette, T. F., et al. (2021) · Canada Communicable Disease Report · doi:10.14745/ccdr.v47i04a01 · Cited by 14
Surveillance of SARS-CoV-2 in Frankfurt am Main from October to December 2020 Reveals High Viral Diversity Including Spike Mutation N501Y in B.1.1.70 and B.1.1.7
Widera, M., Mühlemann, B., Corman, V. M., Toptan, T., Beheim-Schwarzbach, J., Kohmer, N., Schneider, J. A., Berger, A., Veith, T., Pallas, C., et al. (2021) · Microorganisms · doi:10.3390/microorganisms9040748 · Cited by 13
“, E484K, K417N) [2], or increased binding to the ACE-2 receptor (e.”
Background
SARS-CoV-2 variant B.1.1.7 caused HLA-A2+ CD8+ T cell epitope mutations for impaired cellular immune response
Xiao, C., Mao, L., Wang, Z., Gao, L., Zhu, G., Su, J., Chen, X., Yuan, J., Hu, Y., Yin, Z., et al. (2022) · iScience · doi:10.1016/j.isci.2022.103934 · Cited by 21
“…that specific CD8+ epitopes to SARS-CoV-2 are mainly located in ORF1ab, N protein, S protein, ORF 3, M protein and ORF 8(Ferretti et al., 2020; Grifoni et al., 2020), and the identification of these epitopes will provide the basis for next-generation vaccine development and better…”
BackgroundInfluential
How unequal vaccine distribution promotes the evolution of vaccine escapePreprint
Gerrish, P. J., Saldaña, F., Galeota-Sprung, B., Colato, A., Rodríguez‐Torres, E. E., & Velasco‐Hernández, J. X. (2021) · medRxiv · doi:10.1101/2021.03.27.21254453 · Cited by 8
Molecular strategies for antibody binding and escape of SARS-CoV-2 and its mutations
Hendy, M. A., Kaufman, S., & Ponga, M. R. (2021) · Scientific Reports · doi:10.1038/s41598-021-01081-0 · Cited by 17
ESC - a comprehensive resource for SARS-CoV-2 immune escape variants
Rophina, M., Pandhare, K., Shamnath, A., et al. (2021) · bioRxiv · doi:10.1101/2021.02.18.431922 · Cited by 14
Broad strategies for neutralizing SARS-CoV-2 and other human coronaviruses with monoclonal antibodies
Ling, Z., Yi, C., Sun, X., Yang, Z., & Sun, B. (2022) · Science China Life Sciences · doi:10.1007/s11427-022-2215-6 · Cited by 16
“…of SARS-CoV-2 escape variants under the pressure of NAbs and deep mutational scanning (DMS) experiments with yeast cells expressing all possible amino acid substitutions in the RBD have been performed to understand the escape mechanism of SARS-CoV-2 (Greaney et al., 2021; Liu et al., 2021).”
Method
Detection of SARS-CoV-2 Variants of Concern with Tiling Amplicon Sequencing from Wastewater
Wang, Y., Ni, G., Tian, W., Yang, L., Hosegood, I., Newell, R., Woodcroft, B. J., Yang, B., Hu, S., & Guo, J. (2022) · ACS ES&T Water · doi:10.1021/acsestwater.2c00083 · Cited by 9

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

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

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