Neutralization of viruses with European, South African, and United States SARS-CoV-2 variant spike proteins by convalescent sera and BNT162b2 mRNA vaccine-elicited antibodies
Open accessAbstract
The increasing prevalence of SARS-CoV-2 variants with mutations in the spike protein has raised concerns that recovered individuals may not be protected from reinfection and that current vaccines will become less effective. The B.1.1.7 isolate identified in the United Kingdom and B.1.351 isolate identified in the Republic of South Africa encode spike proteins with multiple mutations in the S1 and S2 subunits. In addition, variants have been identified in Columbus, Ohio (COH.20G/677H), Europe (20A.EU2) and in domesticated minks. Analysis by antibody neutralization of pseudotyped viruses showed that convalescent sera from patients infected prior to the emergence of the variant viruses neutralized viruses with the B.1.1.7, B.1.351, COH.20G/677H Columbus Ohio, 20A.EU2 Europe and mink cluster 5 spike proteins with only a minor decrease in titer compared to that of the earlier D614G spike protein. Serum specimens from individuals vaccinated with the BNT162b2 mRNA vaccine neutralized D614G virus with titers that were on average 7-fold greater than convalescent sera. Vaccine elicited antibodies neutralized virus with the B.1.1.7 spike protein with titers similar to D614G virus and neutralized virus with the B.1.351 spike with, on average, a 3-fold reduction in titer (1:500), a titer that was still higher than the average titer with which convalescent sera neutralized D614G (1:139). The reduction in titer was attributable to the E484K mutation in the RBD. The B.1.1.7 and B.1.351 viruses were not more infectious than D614G on ACE2.293T cells in vitro but N501Y, an ACE2 contacting residue present in the B.1.1.7, B.1.351 and COH.20G/677H spike proteins caused higher affinity binding to ACE2, likely contributing to their increased transmissibility. These findings suggest that antibodies elicited by primary infection and by the BNT162b2 mRNA vaccine are likely to maintain protective efficacy against B.1.1.7 and most other variants but that the partial resistance of virus with the B.1.351 spike protein could render some individuals less well protected, supporting a rationale for the development of modified vaccines containing E484K.
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The 10.3-12.4-fold loss of activity against B.1.351 is larger than reported results using mutant pseudoviruses.
“On the other hand, the loss in activity by 10.3-12.4-foldagainst B.1.351 is larger than results that were reported using mutant pseudoviruses 34,42,43 .”
From Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 (2021) · cites this paper as [43]
The E484K mutation appears to result in a lower neutralising ability of mRNA vaccine sera.
“The E484K mutation appears to result in a lower neutralising ability of mRNA vaccine sera.48”
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“Xie et al. engineered 3 SARS-CoV-2 viruses containing key spike mutations from the United Kingdom and South African variants: N501Y; 69/70-deletion + N501Y + D614G; and E484K + N501Y + D614G.”
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“293T cells relative to that 144 of virus with the D614G mutation, an assay that we have used previously to analyze 145 variant spike protein affinity [11].”
Self-citationZhou, H., Dcosta, B. M., Samanovic, M. I., Mulligan, M. J., Landau, N. R., & Tada, T. (2021) · mBio · doi:10.1128/mbio.01386-21 · Cited by 68 · see citing works
“351 variant spike protein has been found to reduce the level of protection provided by vaccination in populations in which the variant has become prevalent (17, 20).”
BackgroundSelf-citationValdés-Balbín, Y., Santana-Mederos, D., Paquet, F., Fernández-Castillo, S., Climent, Y., Chiodo, F., Rodríguez, L., Ramírez, B. S., León, K., Hernández, T., et al. (2021) · ACS Central Science · doi:10.1021/acscentsci.1c00216 · Cited by 53 · see citing works
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“529 isolates with R346K mutations may be 172 warranted if the substitution becomes more prevalent; (4) Our data is derived from experiments 173”
MethodmRNA-1273 protects against SARS-CoV-2 beta infection in nonhuman primates
Corbett, K. S., Werner, A. P., Connell, S. O., Gagné, M., Lai, L., Moliva, J. I., Flynn, B. J., Choi, A., Koch, M., Foulds, K. E., et al. (2021) · Nature Immunology · doi:10.1038/s41590-021-01021-0 · Cited by 53 · see citing works
Tada, T., Zhou, H., Dcosta, B. M., Samanovic, M. I., Mulligan, M. J., & Landau, N. R. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.02.450959 · Cited by 51 · see citing works
Self-citationThe ins and outs of SARS-CoV-2 variants of concern (VOCs)
Salehi-Vaziri, ., Fazlalipour, M., Khorrami, S. M. S., Azadmanesh, K., Pouriayevali, M. H., Jalali, T., Shoja, Z., & Maleki, A. (2022) · Archives of Virology · doi:10.1007/s00705-022-05365-2 · Cited by 58 · see citing works
“A deletion at positions 69 and 70 of the spike protein (Δ69–70), which is associated with diagnostic realtime PCR failure (S gene target failure: SGTF), has been reported to be a marker for the Alpha variant, which was given the name VOC 202012/01 by Public Health England (PHE) [23, 24].”
BackgroundPreclinical evaluation of a SARS-CoV-2 mRNA vaccine PTX-COVID19-B
Liu, J., Budylowski, P., Samson, R., Griffin, B. D., Babuadze, G., Rathod, B., Colwill, K., Abioye, J. A., Schwartz, J. A., Law, R., et al. (2022) · Science Advances · doi:10.1126/sciadv.abj9815 · Cited by 56 · see citing works
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The evolutionary dynamics of endemic human coronaviruses
Jo, W. K., Drosten, C., & Drexler, J. F. (2021) · Virus Evolution · doi:10.1093/ve/veab020 · Cited by 57 · see citing works
Development and preclinical evaluation of virus‐like particle vaccine against COVID‐19 infection
Yilmaz, I. C., İpekoğlu, E. M., Bulbul, A., Turay, N., Yıldırım, M., Evcili, İ., Yilmaz, N. S., Guvencli, N., Aydin, Y., Gungor, B., et al. (2021) · Allergy · doi:10.1111/all.15091 · Cited by 59 · see citing works
Preclinical evaluation of a SARS-CoV-2 mRNA vaccine PTX-COVID19-B
Liu, J., Budylowski, P., Samson, R., Griffin, B., Babuadze, G., Rathod, B., Colwill, K., Abioye, J., Schwartz, J., Law, R., et al. (2021) · bioRxiv · doi:10.1101/2021.05.11.443286 · Cited by 51 · see citing works
Abebe, E. C., & Dejenie, T. A. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1055457 · Cited by 56 · see citing works
SARS-CoV-2 variants and effectiveness of vaccines: a review of current evidence
Tatsi, E., Filippatos, F., & Michos, A. G. (2021) · Epidemiology and Infection · doi:10.1017/s0950268821002430 · Cited by 63 · see citing works
“351 compared to those with wild-type virus, but still more enhanced than titres in convalescent individuals infected by wild-type virus [78].”
ResultProtective activity of mRNA vaccines against ancestral and variant SARS-CoV-2 strains
Ying, B.-L., Whitener, B. M., VanBlargan, L., et al. (2021) · bioRxiv · doi:10.1101/2021.08.25.457693 · Cited by 45 · see citing works
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Protective activity of mRNA vaccines against ancestral and variant SARS-CoV-2 strains
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“Mink cluster 5 was neutralized by plasma samples from convalescent patients at the same level as prototypic SARS-CoV-2, as reported previously (Tada et al., 2021; Wu et al., 2021).”
Tauzin, A., Nayrac, M., Benlarbi, M., Gong, S. Y., Gasser, R., Beaudoin-Bussières, G., Brassard, N., Laumaea, A., Vézina, D., Prévost, J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.18.435972 · Cited by 41 · see citing works
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“351 which also bears the mutation [24-28, 32-34].”
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Epitope-specific antibody responses differentiate COVID-19 outcomes and variants of concern
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“While it has been shown that mutations result in more fit, and likely more contagious, viruses (15, 16, 40), the serological consequences of the mutations found in VOCs are unclear (40).”
InfluentialDetection of SARS-CoV-2 variants by Abbott molecular, antigen, and serological tests
Rodgers, M. A., Batra, R., Snell, L., et al. (2021) · medRxiv · doi:10.1101/2021.04.24.21256045 · Cited by 36
“1 lineages that have been 136 linked to increased transmissibility and immune escape [1-7].”
Chen, R. E., Gorman, M. J., Zhu, D. Y., Carreño, J. M., Yuan, D., VanBlargan, L. A., Burdess, S., Lauffenburger, D. A., Kim, W., Turner, J. S., et al. (2021) · Med · doi:10.1016/j.medj.2021.11.004 · Cited by 36 · see citing works
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“However, we used a limited panel of antibodies and we note that many other reports demonstrate that B.1.1.7 does not escape neutralisation by the majority of COVID-19 patient serum or human mAbs (2, 11, 22, 44–46).”
BackgroundMethodInfluentialThe Emergence and Spread of Novel SARS-CoV-2 Variants
Yi, H., Wang, J., Wang, J., Lu, Y., Zhang, Y., Peng, R., Lu, J., & Chen, Z. (2021) · Frontiers in Public Health · doi:10.3389/fpubh.2021.696664 · Cited by 28 · see citing works
“Three mutations in S gene of these mutations have potential biological effects: First, mutation N501Y is located in the receptor-binding motif (RBM), one of the six key contact residues within the receptor-binding domain (RBD), and has been identified to enhance the affinity of the virus to ACE2 (20, 21).”
BackgroundInfluentialShowers, W. M., Leach, S. M., Kechris, K., & Strong, M. (2021) · Infection, Genetics and Evolution · doi:10.1016/j.meegid.2021.105153 · Cited by 26 · see citing works
Evolution of Antiviral Drug Resistance in SARS-CoV-2
Dinata, R., Baindara, P., & Mandal, S. M. (2025) · Viruses · doi:10.3390/v17050722 · Cited by 29 · see citing works
“It has been observed that activity loss of convalescent sera and vaccine-elicited antibodies against B.1.351 is higher than the results reported using mutant pseudoviruses [70,71].”
InfluentialMorris, C. P., Luo, C. H., Amadi, A., Schwartz, M. C., Gallagher, N., Ray, S. C., Pekosz, A. S., & Mostafa, H. H. (2021) · Clinical Infectious Diseases · doi:10.1093/cid/ciab636 · Cited by 23 · see citing works
Roth, N., Schön, J., Hoffmann, D., Thran, M., Thess, A., Mueller, S. O., Petsch, B., & Rauch, S. (2021) · doi:10.1101/2021.05.13.443734 · Cited by 18 · see citing works
The Antigenicity of Epidemic SARS-CoV-2 Variants in the United Kingdom
Wu, J., Zhang, L., Zhang, Y., Wang, H., Ding, R., Nie, J., Li, Q., Liu, S., Yu, Y., Yang, X., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.687869 · Cited by 22 · see citing works
The challenge of emerging SARS-CoV-2 mutants to vaccine development
Li, R., Liu, J., & Zhang, H. (2021) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2021.03.001 · Cited by 24 · see citing works
Molecular variants of SARS-CoV-2: antigenic properties and current vaccine efficacy
Damavandi, A. R., Dowran, R., Sharif, S. A., Kashanchi, F., & Jafari, R. (2022) · Medical Microbiology and Immunology · doi:10.1007/s00430-022-00729-6 · Cited by 21 · see citing works
Chadha, J., Khullar, L., & Mittal, N. (2021) · Environmental Microbiology · doi:10.1111/1462-2920.15687 · Cited by 32 · see citing works
“In a similar context, the E484K mutation in B.1.351 variant (VOC) has been shown to lower the protective efficacy of the BNT162b2 mRNA vaccine (Pfizer) in populations with a prevalence of B.1.351 variant (Tada et al., 2021).”
BackgroundInfluentialChen, X., Chen, Z., Azman, A. S., Sun, R., Lu, W., Zheng, N., Zhou, J., Wu, Q., Deng, X., Zhao, Z., et al. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3858816 · Cited by 11 · see citing works
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 24 · see citing works
“7) or the older dominant strains, including studies in vaccinees [5,8,11,13,26,27].”
BackgroundEfficacy and Safety of COVID-19 Vaccines—An Update
Sharma, E., Revinipati, S., Bhandari, S., Thakur, S., Goyal, S., Ghose, A., Bajpai, S., Muhammad, W., & Boussios, S. (2022) · Diseases · doi:10.3390/diseases10040112 · Cited by 15 · see citing works
“Serum samples of vaccinated individuals neutralized D164G strain with seven-fold raised antibody titer than convalescent serum [33].”
Evaluation of mRNA-1273 against SARS-CoV-2 B.1.351 Infection in Nonhuman PrimatesPreprint
Corbett, K. S., Werner, A. P., Connell, S. O., Gagné, M., Lai, L., Moliva, J. I., Flynn, B. J., Choi, A., Koch, M. J., Foulds, K. E., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.21.445189 · Cited by 11 · see citing works
da Silva, E. S., Kohnen, M., Gilson, G., Staub, T., Arendt, V., Hilger, C., Servais, J.-Y., Charpentier, É., Domingues, O., Snoeck, C. J., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147675 · Cited by 12 · see citing works
Deep dissection of the antiviral immune profile of patients with COVID-19
Atanackovic, D., Avila, S. V., Lutfi, F. U., de Miguel‐Pérez, D., Fan, X., Sanchez‐Petitto, G., Mause, E. R. V., Siglin, J., Baddley, J. W., Mannuel, H. D., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02852-1 · Cited by 10 · see citing works
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Trombetta, C. M., Marchi, S., Viviani, S., Manenti, A., Benincasa, L., Ruello, A., Bombardieri, E., Vicenti, I., Zazzi, M., & Montomoli, E. (2021) · Viruses · doi:10.3390/v13071347 · Cited by 14 · see citing works
“The immunoevasion could lead to reinfection of subjects who recovered from a previous infection [16] and could reduce the protection induced by vaccination and/or natural infection [27].”
BackgroundResultLennerstrand, J., & Palanisamy, N. (2021) · Viruses · doi:10.3390/v13101974 · Cited by 12 · see citing works
Impact of Ribosome Activity on SARS-CoV-2 LNP – Based mRNA Vaccines
Tsiambas, E., Chrysovergis, A., PAPANIKOLAOU, V. S., MASTRONIKOLIS, N. S., Ragos, V., Batistatou, A. K., Peschos, D., Kavantzas, N., Lazaris, A. C., & Kyrodimos, E. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.654866 · Cited by 11 · see citing works
“In contrast to British variant, other recently isolated spike protein mutant patterns (South African and Brazilian) seem to influence partially the effectiveness of the first generation v-mRNA vaccines in sub-groups of individuals that demonstrate a level or resistance (Tada et al., 2021).”
ResultSmyth, D. S., Trujillo, M., Cheung, K., Gao, A., Hoxie, I., Kannoly, S., Kubota, N., Markman, M., San, K. M., Sompanya, G., et al. (2021) · medRxiv · doi:10.1101/2021.03.21.21253978 · Cited by 10 · see citing works
“Even more concerning are reports of decreased antibody59 mediated neutralization of these variants (7-9).”
BackgroundCarter, C., Airas, J., & Parish, C. A. (2022) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2022.108360 · Cited by 10 · see citing works
A bispecific monomeric nanobody induces spike trimer dimers and neutralizes SARS-CoV-2 in vivoPreprint
Hanke, L., Das, H., Sheward, D. J., Vidakovics, L. P., Urgard, E., Moliner-Morro, A., Kim, C., Karl, V., Pankow, A. P., Smith, N. L., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.20.436243 · Cited by 5 · see citing works
Stanojevic, M., Geiger, A. E., Ostermeier, B., Sohai, D. K., Lazarski, C. A., Lang, H., Jensen-Wachspress, M. A., Webber, K., Burbelo, P. D., Cohen, J. I., et al. (2021) · Cytotherapy · doi:10.1016/j.jcyt.2021.07.006 · Cited by 9 · see citing works
SARS-CoV-2 Portrayed against HIV: Contrary Viral Strategies in Similar Disguise
Duerr, R., Crosse, K. M., Valero-Jimenez, A. M., & Dittmann, M. (2021) · Microorganisms · doi:10.3390/microorganisms9071389 · Cited by 12 · see citing works
“Some of these second-wave Spike mutations seem to confer partial neutralization resistance, as measured in in vitro assays with convalescent or vaccine sera [292-297].”
BackgroundTaha, A. E., Alduraywish, A. A., Almaeen, A. H., El‐Metwally, T. H., Alayyaf, M., Mallick, A., & Abouelkheir, M. M. (2022) · Vaccines · doi:10.3390/vaccines11010026 · Cited by 6 · see citing works
Zhang, M., Gong, Y., & Jiao, S. (2022) · Future Virology · doi:10.2217/fvl-2021-0100 · Cited by 7 · see citing works
“Beta is more worrisome when compared with Alpha in that it is not only refractory to neutralization by most NTD antibodies and multiple RBD antibodies [20,48] but also exhibits varying degrees of resistance to convalescent serum and vaccine-elicited antibodies [20,31,65,66,70,72,73].”
BackgroundSong, Y., Ge, Z., Cui, S., Tian, D., Wan, G., Zhu, S., Wang, X., Wang, Y., Zhao, X., Xiang, P., et al. (2021) · Microbiology Spectrum · doi:10.1128/spectrum.00273-21 · Cited by 12 · see citing works
In vivo monoclonal antibody efficacy against SARS-CoV-2 variant strains
Diamond, M. S., Chen, R. E., Winkler, E. S., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-448370/v1 · Cited by 6
Passive Immunity Should and Will Work for COVID-19 for Some Patients
Cimolai, N. (2021) · Clinical Hematology International · doi:10.2991/chi.k.210328.001 · Cited by 6 · see citing works
Chen, R. E., Gorman, M., Zhu, D. Y., et al. (2021) · medRxiv · doi:10.1101/2021.09.28.21264250 · Cited by 5
“; https://doi.org/10.1101/2021.09.28.21264250doi: medRxiv preprint 13 L452, E484, and elsewhere (Chen et al., 2021b; McCallum et al., 2021; Tada et al., 2021; Wang 256 et al., 2021a; Wang et al., 2021b; Wibmer et al., 2021).”
InfluentialMaiti, A. K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25126306 · Cited by 3 · see citing works
Xu, X., Hong, Y., Chen, E., Wang, Y., Ma, B., Li, J., Su, W., Zhou, Y., & Zhang, M. (2022) · Vaccines · doi:10.3390/vaccines10122110 · Cited by 4 · see citing works
Song, Y., Ge, Z.-R., Cui, S., et al. (2021) · medRxiv · doi:10.1101/2021.05.04.21256655 · Cited by 4
“7 variant cases with non-variant cases, (1) there were more patients 315 with body temperature over 38°C; (2) the laboratory tests of the level of CRP, SAA, CK 316 and DD was significantly higher; (3) the abnormal proportion of CD4T was 317 significantly higher; (4) the patients that had ground glass opacity in the lu…”
ResultVoss, C., Esmail, S., Liu, X., et al. (2021) · medRxiv · doi:10.1101/2021.03.16.21253716 · Cited by 4
“This may explain why recent studies have shown the Pfizer and Moderna mRNA vaccines are effective in protecting from infection by the variant (37-39).”
ResultDetection of SARS-CoV-2 variants by Abbott molecular, antigen, and serological tests
Rodgers, M. A., Olivo, A., Harris, B. J., Lark, C., Luo, X., Berg, M. G., Meyer, T. V., Mohaimani, A., Orf, G. S., Goldstein, D. Y., et al. (2022) · Journal of Clinical Virology · doi:10.1016/j.jcv.2022.105080 · Cited by 43 · see citing works
Multifactorial Traits of SARS-CoV-2 Cell Entry Related to Diverse Host Proteases and Proteins
You, J., Seok, J. H., Joo, M., Bae, J., Kim, J. I., Park, M., & Kim, K. (2021) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2021.048 · Cited by 3 · see citing works
“An amino acid residue “R” is constantly exposed at the C-terminus of the S1/ S2 cleavage site by the host protease furin, commonly known as the C-end rule (CendR) (Teesalu et al., 2009).”
Sziemel, A. M., Hwa, S.-H., Sigal, A., Tyson, G. B., Logan, N. A., Willett, B. J., & Durcan, P. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.11.439360 · Cited by 2 · see citing works
Brentville, V. A., Vankemmelbeke, M., Metheringham, R. L., Symonds, P., Cook, K., Urbanowicz, R. A., Tsoleridis, T., Coleman, C., Chang, K.-C., Skinner, A., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.18.448932 · Cited by 5 · see citing works
“Data have suggested that although the approved vaccines induce responses that can provide some cross-reactivity with the Alpha variant, they are less effective against the Beta, Delta and Gamma variants [27,32-34].”
BackgroundMathematical artificial intelligence design of mutation-proof COVID-19 monoclonal antibodies
Chen, J.-H., & Wei, G.-S. (2022) · arXiv.org · doi:10.48550/arxiv.2204.09471 · Cited by 2
Impffortschritt in Deutschland und der Welt: Chancen und Risiken
Grimm, V., Lembcke, F. K., & Schwarz, M. (2021) · Wirtschaftsdienst · doi:10.1007/s10273-021-2894-5 · Cited by 5 · see citing works
Long, S., Olsen, R., Christensen, P., et al. (2021) · medRxiv · doi:10.1101/2021.02.26.21252227 · Cited by 2 · see citing works
“20 These variants also are of concern because they contain a mutation 88 (E484K) in the spike protein that decreases efficacy of some therapeutic mAbs, decreases in 89 vitro virus neutralization, and may result in potential escape from immunity induced by natural 90 infection or vaccination.(29-37) All three variants…”
da Silva, E. E. S., Kohnen, M., Gilson, G., et al. (2022) · medRxiv · doi:10.1101/2022.06.21.22276659 · Cited by 1
“in neutralizing activity is modest (2-3-fold) [48, 72-77], while it reaches ~10-fold to full escape for Beta and Gamma [48, 72-79].”
BackgroundResultOrtloff, A., & Harsch, I. (2021) · GMS Hygiene and Infection Control · doi:10.3205/dgkh000387 · Cited by 1
High-Potency Polypeptide-based Inhibition of Enveloped-virus GlycoproteinsPreprint
Ma, J., Acevedo, A. C., & Wang, Q. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.05.438537 · Cited by 3 · see citing works
Ettorre, L., Williams, T., Houy, C., Zhu, S., Kishko, M., Azizi, A., James, D. A., Gajewska, B., & Szeto, J. (2025) · Vaccines · doi:10.3390/vaccines13080794
“These mutations imparted conformational changes to the ACE2 binding region and decreased susceptibility to sero-neutralization [14].”
'Geno-to-pheno' SARS-CoV-2 genome-COVID-19 association studies
Tang, J. W.-T. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103333
“However, there is still some protection offered by these vaccines against severe disease and death [4,5].”
- Authors
- Tada, T., Dcosta, B. M., Samanovic-Golden, M., Herati, R. S., Cornelius, A., Mulligan, M. J., & Landau, N. R.
- Affiliations
- New York University (US)
- Corresponding author
- Landau, Nathaniel R.
- Venue
- mBio
- Publisher
- openRxiv
- Published
- 2021-02-07
- Volume
- 12
- Issue
- 3
- Pages
- e0069621-e0069621
- ISSN
- 2150-7511 (ISSN-L)
- PMC
- PMC7872356
- OpenAlex
- W3164611210
- Cited by
- 153
- References
- 35
- Citations by year
- 2025: 4 · 2024: 5 · 2023: 11 · 2022: 45 · 2021: 88
- FWCI
- 11.88
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- mBio (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institutes of Health (AI122390)
- National Institute on Drug Abuse (DP1DA046100)
- National Institute of Allergy and Infectious Diseases (K08AI120898, R21AI122390, U01AI047996, R33AI122390, UM1AI148574)
- Common Fund (AI122390, AI120898, DA046100, UM1AI148574)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- SARS-CoV-2 variants, neutralizing antibodies, convalescent sera, vaccine-elicited antibodies, B.1.351 variant, anti-spike antibodies, antibody escape, combination therapy, vaccine effectiveness, variant surveillance
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 ›
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