Partial resistance of SARS-CoV-2 Delta variants to vaccine-elicited antibodies and convalescent sera
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Abstract
Highly transmissible SARS-CoV-2 variants identified in India and designated B.1.617, Kappa (B.1.617.1), Delta (B.1.617.2), B.1.618, and B.1.36.29 contain spike mutations L452R, T478K, E484K, E484Q, and N440K located within the spike receptor-binding domain and thus could contribute to increased transmissibility and potentially allow re-infection or cause resistance to vaccine-elicited antibody. To address these issues, we used lentiviruses pseudotyped by variant spikes to measure their neutralization by convalescent sera, vaccine-elicited and Regeneron therapeutic antibodies, and ACE2 affinity. Convalescent sera and vaccine-elicited antibodies neutralized viruses with Delta spike with 2- to 5-fold decrease in titer in different donors. Regeneron antibody cocktail neutralized virus with the Delta spike with a 2.6-fold decrease in titer. Neutralization resistance to serum antibodies and monoclonal antibodies was mediated by L452R mutation. These relatively modest decreases in antibody neutralization titer for viruses with variant spike proteins suggest that current vaccines will remain protective against the family of Delta variants.
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Previous experience with the delta variant in the United Kingdom suggested that protection against hospitalization after two doses of vaccine was well maintained.
“Previous experience with the delta variant in the United Kingdom suggested that protection against hospitalization after two doses of vaccine was well maintained.”
From Effectiveness of COVID-19 vaccines against the Omicron (B.1.1.529) variant of concern (2021) · cites this paper as [19]
Vaccine effectiveness against severe disease caused by the omicron variant is likely to be substantially higher than the estimates against symptomatic disease.
“on the basis of experience with other variants and early estimates of hospitalization rates, vaccine effectiveness against severe disease is likely to be substantially higher than the estimates against symptomatic disease”
From Effectiveness of COVID-19 vaccines against the Omicron (B.1.1.529) variant of concern (2021) · cites this paper as [19]
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Cites
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The rapid adaptation of SARS-CoV-2–rise of the variants: transmission and resistance
Soh, S. M., Kim, Y., Kim, C., Jang, U. S., & Lee, H.-R. (2021) · The Journal of Microbiology · doi:10.1007/s12275-021-1348-5 · Cited by 37 · see citing works
Focosi, D., Tuccori, M., Baj, A., & Maggi, F. (2021) · Viruses · doi:10.3390/v13071211 · Cited by 37 · see citing works
Structural insights of a highly potent pan-neutralizing SARS-CoV-2 human monoclonal antibody
Torres, J. L., Ozorowski, G., Andreano, E., Liu, H., Copps, J., Piccini, G., Donnici, L., Conti, M., Planchais, C., Planas, D., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2120976119 · Cited by 33 · see citing works
Neerukonda, S. N., Vassell, R. A., Lusvarghi, S., Wang, R., Echegaray, F., Bentley, L., Eakin, A. E., Erlandson, K. J., Katzelnick, L. C., Weiss, C. D., et al. (2021) · Viruses · doi:10.3390/v13122485 · Cited by 30 · see citing works
“A prior study showed that convalescent sera and vaccine-elicited antibody neutralization titers against pseudoviruses bearing spikes containing L452R-E484QP681R substitutions displayed 2–5-fold reduction, compared to the neutralization titers against WT (D614G) pseudoviruses [25].”
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“As noted in prior publications, which use these PVPs, S protein incorporation into PVPs is consistent across variant S proteins (14, 46).”
Self-citationResearch 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 29 · see citing works
S glycoprotein diversity of the Omicron variantPreprint
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A potent and broad neutralization of SARS-CoV-2 variants of concern by DARPins
Chonira, V., Kwon, Y. D., Gorman, J., Case, J. B., Ku, Z., Simeon, R. L., Casner, R. G., Harris, D. R., Olia, A. S., Stephens, T., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01193-2 · Cited by 22 · see citing works
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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
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Somogyi, E., Csiszovszki, Z., Molnár, L., Lőrincz, O., Tóth, J., Pattijn, S., Schockaert, J., Mazy, A., Miklós, I., Pántya, K., et al. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.684152 · Cited by 18 · see citing works
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Baj, A., Novazzi, F., Ferrante, F. D., Genoni, A. P., Tettamanzi, E., Catanoso, G., Gasperina, D. D., Dentali, F., Focosi, D., & Maggi, F. (2021) · Emerging Microbes & Infections · doi:10.1080/22221751.2021.1994356 · Cited by 18 · see citing works
In vitro and in silico evaluation of antiretrovirals against SARS-CoV-2: A drug repurposing approach
Zapata-Cardona, M. I., Flórez‐Álvarez, L., Guerra-Sandoval, A. L., Chvatal‐Medina, M., Almonacid, C. M. G., Hincapié-García, J. A., Hernández, J. C., Rugeles, M. T., & Zapata, W. (2023) · AIMS Microbiology · doi:10.3934/microbiol.2023002 · Cited by 18 · see citing works
“…the world, the appearance of variants with several degrees of resistance to the vaccine and naturally acquired antibodies [2], along with the restricted specific therapy available for this disease, underline the need for continuing with the evaluation of molecules with antiviral properties [3,4].”
Delta-Omicron recombinant escapes therapeutic antibody neutralization
Duerr, R., Zhou, H., Tada, T., Dimartino, D., Marier, C., Zappile, P., Wang, G., Plitnick, J., Griesemer, S. B., Girardin, R. C., et al. (2023) · iScience · doi:10.1016/j.isci.2023.106075 · Cited by 18 · see citing works
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Ahammad, I., Hossain, M. U., Rahman, A., Chowdhury, Z. M., Bhattacharjee, A., Das, K. C., Keya, C. A., & Salimullah, M. (2021) · PLoS ONE · doi:10.1371/journal.pone.0258019 · Cited by 17 · see citing works
Focosi, D., Franchini, M., Joyner, M. J., & Casadevall, A. (2022) · Vox Sanguinis · doi:10.1111/vox.13239 · Cited by 15 · see citing works
van der Straten, K., van Gils, M. J., de Taeye, S. W., & de Bree, G. J. (2022) · Frontiers in Medical Technology · doi:10.3389/fmedt.2022.867982 · Cited by 16 · see citing works
Kumar, A., Asghar, A., Dwivedi, P., Kumar, G., Narayan, R. K., Jha, R. K., Parashar, R., Sahni, C., & Pandey, S. N. (2022) · JMIR Bioinformatics and Biotechnology · doi:10.2196/36860 · Cited by 17 · see citing works
Delshad, M., Sanaei, M., Pourbagheri‐Sigaroodi, A., & Bashash, D. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109128 · Cited by 16 · see citing works
Mahmood, T. B., Hossan, M. I., Mahmud, S., Shimu, M. S. S., Alam, M. J., Bhuyan, M. M. R., & Emran, T. B. (2022) · Immunity Inflammation and Disease · doi:10.1002/iid3.683 · Cited by 16 · see citing works
“Tada et al.56 depicts that L452R mutation contributed to the reduction in neutralizing potential of 14 out of 35 RBD specific monoclonal antibodies (mAbs) and in another study conducted by McCallum et al.57 showed that L452R mutations promotes viral replication hence infectivity of the virus by facilitating immune eva…”
ResultChest CT features of children infected by B.1.617.2 (Delta) variant of COVID-19
Cheng, Q.-R., Fan, M.-X., Hao, J., Hu, X., Ge, X., Hu, Z., & Li, Z. (2021) · World Journal of Pediatrics · doi:10.1007/s12519-021-00484-3 · Cited by 15 · see citing works
Dissecting Naturally Arising Amino Acid Substitutions at Position L452 of SARS-CoV-2 Spike
Tan, T. S., Toyoda, M., Ode, H., Barabona, G., Hamana, H., Kitamatsu, M., Kishi, H., Motozono, C., Iwatani, Y., & Ueno, T. (2022) · Journal of Virology · doi:10.1128/jvi.01162-22 · Cited by 14 · see citing works
Efficacy and limitations of repurposed drugs and vaccines for COVID-19
Murmu, N., Sarkar, M., Dey, S., Manna, R., Roy, S., Mondal, T., Halder, S., Bhattacharjee, N., Dash, S. K., & Giri, B. (2023) · Journal of Medicine Surgery and Public Health · doi:10.1016/j.glmedi.2023.100041 · Cited by 13 · see citing works
Lennerstrand, J., & Palanisamy, N. (2021) · Viruses · doi:10.3390/v13101974 · Cited by 12 · see citing works
Tada, T., Dcosta, B. M., Zhou, H., & Landau, N. R. (2023) · iScience · doi:10.1016/j.isci.2023.106092 · Cited by 9 · see citing works
Self-citationSARS-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
Valdovinos-Navarro, B. J., Dueñas, S., Flores-Acosta, G. I., Gasperin-Bulbarela, J., Bernáldez-Sarabia, J., Cabanillas-Bernal, O., Cervantes-Luévano, K., & Licea-Navarro, A. F. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012267 · Cited by 11 · see citing works
“It has previously been reported that the Delta variant may show slight resistance to convalescent and vaccine-generated sera from BNT 162b2 (Pfizer/BioNTech) and ChAdOx (Oxford/AstraZeneca) [11,12].”
BackgroundBiosensors for Point Mutation Detection
Jiang, H., Xi, H., Juhas, M., & Zhang, Y. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.797831 · Cited by 11 · see citing works
“However, the level by which the resistance to neutralizing antibodies increases in SARSCoV-2 point mutants will require further investigation as another study demonstrated that SARS-CoV-2 with variant S protein showed only low decrease in antibody neutralization (Tada et al., 2021).”
ResultMeurisse, M., Oyen, H. J. V., Blot, K. Y., Catteau, L., Serrien, B., Klamer, S., Cauët, É., Robert, A. R., & Goethem, N. V. (2022) · BMC Infectious Diseases · doi:10.1186/s12879-022-07777-6 · Cited by 11 · see citing works
Chen, 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
SARS-CoV-2 pathophysiology and post-vaccination severity: a systematic review
Rustagi, V., Gupta, S. R. R., Talwar, C., Singh, A., Xiao, Z.-Z., Jamwal, R., Bala, K., Bhaskar, A. K., Nagar, S., & Singh, I. K. (2024) · Immunologic Research · doi:10.1007/s12026-024-09553-x · Cited by 12 · see citing works
“Waning of protection from omicron has been observed after vaccination as it leads to evading natural and vaccine-induced immunity [100].”
HaploCoV: unsupervised classification and rapid detection of novel emerging variants of SARS-CoV-2
Chiara, M., Horner, D. S., Ferrandi, E., Gissi, C., & Pesole, G. (2023) · Communications Biology · doi:10.1038/s42003-023-04784-4 · Cited by 10 · see citing works
Wang, S., Zou, X., Li, Z., Fu, J., Fan, H., Yu, H., Dèng, F., Huang, H., Peng, J., Zhao, K., et al. (2021) · Frontiers in Public Health · doi:10.3389/fpubh.2021.791600 · Cited by 8 · see citing works
Egger, A., Sahanic, S., Gleiß, A., Ratzinger, F., Holzer, B., Irsara, C., Binder, N. B., Winkler, C., Binder, C. J., Posch, W., et al. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.00597-22 · Cited by 9 · see citing works
“For example, the Delta and Omicron variants of SARS-CoV-2 were found to partly escape the effect of neutralizing antibodies, and the reactivity of the sera tested here might not be sufficient to neutralize these and other emerging SARS-CoV-2 variants (38, 39).”
BackgroundGenetic Path of the Emergence of SARS-CoV-2
Nasrin, T., & Ali, S. (2021) · Gene Cell and Tissue · doi:10.5812/gct.118302 · Cited by 8 · see citing works
Ren, W., Ju, X., Gong, M., Lan, J., Yu, Y., Long, Q., Zhang, Y. L., Zhong, J., Zhong, G., Wang, X., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.09.03.458829 · Cited by 7 · see citing works
Engineered multivalent self-assembled binder protein against SARS-CoV-2 RBD
Britton, D., Punia, K., Mahmoudinobar, F., Tada, T., Jiang, X., Renfrew, P. D., Bonneau, R., Landau, N. R., Kong, X., & Montclare, J. K. (2022) · Biochemical Engineering Journal · doi:10.1016/j.bej.2022.108596 · Cited by 6 · see citing works
“Neutralization assay ACE-MAP, ACE2, and ACEBINDER were tested against SARS-CoV-2 using the previously established pseudotyped lentiviral neutralization assay [62] which is employed with ACE 0.”
Self-citationVeleanu, A., Kelch, M. A., Ye, C.-J., Flohr, M., Wilhelm, A., Widera, M., Martínez-Sobrido, L., Ciesek, S., & Toptan, T. (2022) · Viruses · doi:10.3390/v14092017 · Cited by 5 · see citing works
Su, Y. C. F., Zeller, M. A., Ou, T. P., Ma, J., Pum, L., Zhang, R., Rath, S., Heang, V., Kol, S., Lim, R., et al. (2024) · Communications Medicine · doi:10.1038/s43856-024-00685-7 · Cited by 6 · see citing works
“The L452R mutation in the RBD was demonstrated to reduce antibody recognition and virus neutralization 14,59 .”
Neutralization assays for SARS-CoV-2
Mukhopadhyay, L., Gupta, N., Yadav, P. D., & Aggarwal, N. (2022) · The Indian Journal of Medical Research · doi:10.4103/ijmr.ijmr_2544_21 · Cited by 4 · see citing works
Ert, H. A. V., Bohan, D., Rogers, K. J., Fili, M., Chávez, R. A. R., Qing, E., Han, C., Dempewolf, S., Hu, G., Schwery, N., et al. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.02676-21 · Cited by 3 · see citing works
Mutation Analysis of SARS-CoV-2 Variants Isolated from Symptomatic Cases from Andhra Pradesh, India
Mudhigeti, N., Sireesha, K., Srikar, A., Katari, S. K., Mohan, A., Vengamma, B., Tirumala, C., Verma, A., & Kalawat, U. (2023) · Viruses · doi:10.3390/v15081656 · Cited by 3 · see citing works
SARS-CoV-2 Variants: Impact of Spike Mutations on Vaccine and Therapeutic Strategies
Raman, R., Patel, K. J., & Ranjan, K. (2022) · Springer eBooks · doi:10.1007/978-3-031-08045-6_7 · Cited by 4 · see citing works
Hilti, D., Wehrli, F., Roditscheff, A., Risch, M., Risch, L., Egli, A., Bodmer, T., & Wohlwend, N. (2023) · Pathogens · doi:10.3390/pathogens12121383 · Cited by 2 · see citing works
Dual coiled-coil protein domain mimic and drug delivery vehicle for SARS-CoV-2
Britton, D., Liu, C., Jia, S., Paul, D., Legocki, J., Xiao, Y., Jiang, X., Kong, X., & Montclare, J. K. (2024) · Biochemical Engineering Journal · doi:10.1016/j.bej.2024.109261 · Cited by 2 · see citing works
A Review on Variant of Concern (Delta Variant of COVID 19)
Jangam, K. K., Vikhe, D. N., Jadhav, R. S., & Shinde, G. S. (2022) · Asian Journal of Research in Pharmaceutical Sciences · doi:10.52711/2231-5659.2022.00025 · Cited by 2 · see citing works
COVID‐19: Laboratory/Serologic Diagnostics
Chin, D., Eibschutz, L. S., Sobczyk, J., Azami, M., Repajic, M., & Dubé, M. P. (2022) · Wiley eBooks · doi:10.1002/9781119789741.ch3 · Cited by 2 · see citing works
Chen, R.-M. (2021) · Mathematical Biosciences & Engineering · doi:10.3934/mbe.2021311 · Cited by 1 · see citing works
Breakthrough infections in MPN-COVID vaccinated patients
Barbui, T., Carobbio, A., Ghirardi, A., Iurlo, A., Stefano, V. D., Sobas, M., Rumi, E., Elli, E. M., Lunghi, F., Kabat, M. G., et al. (2022) · Blood Cancer Journal · doi:10.1038/s41408-022-00749-8 · Cited by 1 · see citing works
“Therefore, a statistically significant benefit of vaccination in individuals with prior COVID-19 was not apparent; however, these findings were based on a small number of reinfections and need confirmation by prolonging the follow-up in longitudinal studies to assess the durability of the protection in comparable grou…”
BackgroundResultOmics approaches in COVID-19: An overview
Maiti, A. K. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-91794-0.00009-3 · Cited by 1 · see citing works
Vlase, C.-M., Stuparu-Crețu, M., Vasile, M.-C., Popovici, G.-C., & Arbune, M. (2024) · Infectious Disease Reports · doi:10.3390/idr16050060 · Cited by 1 · see citing works
“The initial variant of SARS-CoV-2 was named Alpha, but within a few months, variants of concern (VOC) emerged and spread rapidly: Delta (2020–2021), Omicron BA.1, BA.2, BA.3, and BA.5 (2021), Omicron BA.5 (2022) [13–15].”
BackgroundSsenyange, G., Kerfoot, M., Zhao, M., Farhadian, S., Chen, S.-D., Peng, L., Ren, P., Cruz, C. D., Gupta, S., & Sutton, R. E. (2022) · Cell Reports Methods · doi:10.1016/j.crmeth.2022.100252 · Cited by 1 · see citing works
“Variant B.1.617.2 was initially isolated in India, its spike protein has L452R and T478K mutations in the RBD in addition to D614G and a P681R mutation near the proteolytic processing site (Tada et al., 2021b).”
InfluentialKurniawati, E. M., Putri, I. S., Widiatmaja, D. M., Praba, V. M., Visuddho, V., Prameswari, F. U., Zahrani, M., Putra, F. N., Nugraha, D., & Widiastara, A. A. (2022) · Anaesthesia Pain & Intensive Care · doi:10.35975/apic.v26i4.1962 · Cited by 1 · see citing works
Vaccine-induced neutralizing antibodies against SARS-CoV-2 Omicron variant isolated in Osaka, Japan
Hiroi, S., Morikawa, S., Motomura, K., & Mori, H. (2023) · Access Microbiology · doi:10.1099/acmi.0.000465.v3
Systems immune profiling of variant-specific vaccination against SARS-CoV-2Preprint
Peng, L., Park, J. J.-Y., Fang, Z., Zhou, X., Dong, M. B., Xiong, Q., Lin, C., & Chen, S. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.02.471028 · Cited by 1 · see citing works
Mäkelä, A. R., Uğurlu, H., Hannula, L., Kant, R., Salminen, P., Fagerlund, R., Mäki, S., Haveri, A., Strandin, T. M., Kareinen, L., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.28.474326
Ramakrishnan, J., Chinnamadhu, A., Suresh, S., & Kumaradhas, P. (2023) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30432
Yasugi, M., Nakagama, Y., Kaku, N., Nitahara, Y., Hatanaka, N., Yamasaki, S., & Kido, Y. (2023) · Vaccine · doi:10.1016/j.vaccine.2023.08.076
Nguyen, Q., Mai, T. T., Tuong, L.-T., Nguyen, T.-T.-N., Vo, T.-P., Nguyen, D.-N., Phan-Van, C.-T., Trinh, D.-T. T., Tran, V.-T., & Thai, K. (2025) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2024.2446659
“However, the combination of REGN10933 and REGN10987 antibodies has been shown to neutralize these variants (Tada et al., 2021; Takashita et al., 2022).”
Vakhrusheva, A., Frolova, M. E., & Isaev, A. A. (2025) · Vaccines · doi:10.3390/vaccines13121187
- Authors
- Tada, T., Zhou, H., Dcosta, B. M., Samanovic, M. I., Mulligan, M. J., & Landau, N. R.
- Affiliations
- New York University (US)
- Corresponding author
- Landau, Nathaniel R.
- ORCID
- Venue
- iScience
- Publisher
- Elsevier BV
- Published
- 2021-11
- Volume
- 24
- Issue
- 11
- Pages
- 103341
- ISSN
- 2589-0042 (ISSN-L)
- PMC
- PMC8541826
- OpenAlex
- W3208693108
- Cited by
- 101
- References
- 36
- Citations by year
- 2025: 3 · 2024: 4 · 2023: 16 · 2022: 42 · 2021: 36
- FWCI
- 7.75
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- iScience (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institutes of Health (AI120898, AI122390, DA046100, UM1AI148574)
- Eli Lilly and Company
- Pfizer
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Keywords
- Delta variant, spike protein mutations, L452R, E484K, receptor binding domain, antibody neutralization, vaccine-elicited antibodies, convalescent sera, monoclonal antibodies, vaccine protection, COVID-19 pandemic
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