Cited by 518SARS-CoV-2 and COVID-19 ResearchAnimal Virus Infections Studiesvaccines and immunoinformatics approaches

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Neutralization of SARS-CoV-2 lineage B.1.1.7 pseudovirus by BNT162b2 vaccine–elicited human sera

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Muik, Alexander, Wallisch, Ann-Kathrin, Sänger, Bianca, Swanson, Kena A., Mühl, Julia, Chen, Wei, Cai, Hui, Maurus, Daniel, Sarkar, Ritu, Türeci, Özlem, Dormitzer, Philip R., Şahin, Uğur·2021·Science

DOI 10.1126/science.abg6105PMC PMC7971771

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Abstract

Vaccine protects against B1.1.7 variant: The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) B1.1.7 (VOC 202012/01) variant that emerged in late 2020 in the United Kingdom has many changes in the spike protein gene. Three of these are associated with enhanced infectivity and transmissibility, and there are concerns that B.1.1.7 might compromise the effectiveness of the vaccine. Muik et al. compared the neutralization efficacy of sera from 40 subjects immunized with the BioNTech-Pfizer mRNA vaccine BNT162b2 against a pseudovirus bearing the Wuhan reference strain or the lineage B.1.1.7 spike protein (see the Perspective by Altmann et al. ). Serum was derived from 40 subjects in two age groups 21 days after the booster shot. The vaccine remained effective against B.1.1.7 with a slight but significant decrease in neutralization that was more apparent in participants under 55 years of age. Thus, the vaccine provides a significant “cushion” of protection against this variant. Science , this issue p. 1152 ; see also p. 1103

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Background
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Highly potent dual-targeting angiotensin-converting enzyme 2 (ACE2) and Neuropilin-1 (NRP1) peptides: A promising broad-spectrum therapeutic strategy against SARS-CoV-2 infection
Mei, S., Zou, Y., Jiang, S., Lü, X., Wang, Y., Han, J. D. J., Yang, P., Niu, M., Li, J., Yuan, K., et al. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115908 · Cited by 10
Self-Assembly of Single-Virus SERS Hotspots for Highly Sensitive In Situ Detection of SARS-CoV-2 on Solid Surfaces
Song, K., Xue, W., Li, X., Chang, Y., & Liu, M. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.4c01607 · Cited by 9
In vivo characterization of emerging SARS-CoV-2 variant infectivity and human antibody escape potential
Lam, B. K., Kung, Y. J., Lin, J. W., Tseng, S.-H., Tsai, Y. C., He, L., Castiglione, G. M., Egbert, E. R., Duh, E. J., Bloch, E. M., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109838 · Cited by 9
SARS-CoV-2 booster vaccination rescues attenuated IgG1 memory B cell response in primary antibody deficiency patients
Lin, F. J., Doss, A. M. A., Davis-Adams, H. G., Adams, L. J., Hanson, C. H., VanBlargan, L. A., Liang, C.-Y., Chen, R. E., Monroy, J. M., Wedner, H. J., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1033770 · Cited by 9
From a genome-wide screen of RNAi molecules against SARS-CoV-2 to a validated broad-spectrum and potent prophylaxis
Yogev, O., Weissbrod, O., Battistoni, G., Bressan, D., Naamati, A., Falciatori, I., Berkyurek, A. C., Rasnic, R., Izuagbe, R., Hosmillo, M. D. T., et al. (2023) · Communications Biology · doi:10.1038/s42003-023-04589-5 · Cited by 14
Dynamic Management of Lung Cancer Care During Surging COVID-19
Wang, A. R., Chang, S. H., Kim, E. J., Bessich, J. L., Sabari, J. K., Cooper, B. T., Geraci, T. C., & Cerfolio, R. J. (2021) · Frontiers in Surgery · doi:10.3389/fsurg.2021.663364 · Cited by 9
Phylogenicity of B.1.1.7 surface glycoprotein, novel distance function and first report of V90T missense mutation in SARS-CoV-2 surface glycoprotein
Stojanov, D. (2021) · Meta Gene · doi:10.1016/j.mgene.2021.100967 · Cited by 10
Vaccine development and technology for SARS‐CoV‐2: Current insight
Cattel, L., Giordano, S., Traina, S., Lupia, T., Corcione, S., Angelone, L., Valle, G. L., Rosa, F. G. D., & Cattel, F. (2021) · Journal of Medical Virology · doi:10.1002/jmv.27425 · Cited by 7
“The efficacy of the Pfizer/BioNTech vaccine against the SARS‐ CoV‐2 alpha variant was compared to its efficacy against the Wuhan reference strain in a preliminary study.(62) The data showed a slightly reduced neutralization susceptibility of the BNT162b2 vaccine.”
Method
mRNA Vaccines as an Efficient Approach for the Rapid and Robust Induction of Host Immunity Against SARS-CoV-2
Noor, R. (2022) · SN Comprehensive Clinical Medicine · doi:10.1007/s42399-022-01168-3 · Cited by 9
19n01, a broadly neutralizing antibody against omicron BA.1, BA.2, BA.4/5, and other SARS-CoV-2 variants of concern
García‐Vega, M., Melgoza-González, E. A., Hernández‐Valenzuela, S., Hinojosa‐Trujillo, D., Reséndiz‐Sandoval, M., Llamas-Covarrubias, M. A., Loza-López, M., Valenzuela, O., Soto‐Gaxiola, A., Hernández‐Oñate, M. Á., et al. (2023) · iScience · doi:10.1016/j.isci.2023.106562 · Cited by 9
“Most vaccines elicit antibody responses with decreased neutralizing activity against Omicron and other variants, and two or three boosters are needed to increase the neutralizing response.(9,10) Monoclonal antibodies (mAbs) represent an important therapeutic option that provides clinical benefit in mild to moderate CO…”
Provisional recommendations for SARS-CoV-2 vaccination in patients with cryoglobulinaemic vasculitis
Scarpato, S., Sebastiani, M., Quartuccio, L., Marson, P., Fraticelli, P., Castelnovo, L., Visentini, M., Candela, M., Mazzaro, C., Saccardo, F., et al. (2021) · Clinical and Experimental Rheumatology · doi:10.55563/clinexprheumatol/2v6v5j · Cited by 8
“7 lineage will escape to the Comirnaty-mediated protection (22).”
Background
Elicitation of Broadly Neutralizing Antibodies against B.1.1.7, B.1.351, and B.1.617.1 SARS-CoV-2 Variants by Three Prototype Strain-Derived Recombinant Protein Vaccines
Yang, Y. P., Zang, J., Xu, S., Zhang, X., Yuan, S., Wang, H., Lavillette, D., Zhang, C., & Huang, Z. W. (2021) · Viruses · doi:10.3390/v13081421 · Cited by 8
Malaria vaccine approaches leveraging technologies optimized in the COVID-19 era
Kanoi, B. N., Maina, M., Likhovole, C., Kobia, F., & Gitaka, J. (2022) · Frontiers in Tropical Diseases · doi:10.3389/fitd.2022.988665 · Cited by 11
A comprehensive review on immunogen and immune-response proteins of SARS-CoV-2 and their applications in prevention, diagnosis, and treatment of COVID-19
Zhang, D., Kukkar, D., Kim, K., & Bhatt, P. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.129284 · Cited by 6
Immunity against conserved epitopes dominates after two consecutive exposures to SARS-CoV-2 Omicron BA.1
Muik, A., Quandt, J., Lui, B. G., Bacher, M., Lutz, S., Grünenthal, M., Toker, A., Grosser, J., Ozhelvaci, O., Blokhina, O., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114567 · Cited by 10
Self-citation
A Recombinant Subunit Vaccine Induces a Potent, Broadly Neutralizing, and Durable Antibody Response in Macaques against the SARS-CoV-2 P.1 (Gamma) Variant
To, A., Wong, T. A. S., Lieberman, M. M., Thompson, K. S., Ball, A. H., Pessaint, L., Greenhouse, J. J., Daham, N., Cook, A., Narvaez, B., et al. (2022) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.1c00600 · Cited by 8
Neutralizing Antibodies Response against SARS-CoV-2 Variants of Concern Elicited by Prior Infection or mRNA BNT162b2 Vaccination
Bonura, F., Genovese, D., Amodio, E., Calamusa, G., Sanfilippo, G. L., Cacioppo, F., Giammanco, A., Grazia, S. D., & Ferraro, D. (2022) · Vaccines · doi:10.3390/vaccines10060874 · Cited by 8
“[41] on a group of two-dose vaccinees, evidenced slight but statistically significantly reduced NtAb titers against the Alpha variant compared with the B.”
Result
The impact of CoronaVac on the neutralization breadth and magnitude of the antibody response to SARS-CoV-2 viruses
Zhang, L., Chen, H., Yang, S. L., Zhao, Y., Shen, X. Y., He, X., Ye, H., Wang, D., Lou, J., Wang, Y., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.990071 · Cited by 8
Cross-reaction of current available SARS-CoV-2 MAbs against the pangolin-origin coronavirus GX/P2V/2017
Jia, Y., Niu, S., Hu, Y., Chai, Y., Zheng, A., Su, C., Wu, L., Han, P., Han, P., Lu, D., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111831 · Cited by 8
In Silico Prediction of Hub Genes Involved in Diabetic Kidney and COVID-19 Related Disease by Differential Gene Expression and Interactome Analysis
Osuna‐Martínez, U., Aviña‐Padilla, K., Olimón-Andalón, V., Angulo‐Rojo, C., Guadrón‐Llanos, A. M., Rivas-Ferreira, J. C., Urrea, F., & Calderón-Zamora, L. (2022) · Genes · doi:10.3390/genes13122412 · Cited by 8
“Even with the development of vaccines and their worldwide distribution, it is noteworthy that we must consider the constant interaction with new and possibly more infectious variants [14,16,17].”
Changes within the P681 residue of spike dictate cell fusion and syncytia formation of Delta and Omicron variants of SARS-CoV-2 with no effects on neutralization or infectivity
Kuzmina, A., Korovin, D., Cohen-Lass, I., Atari, N., Ottolenghi, A., Hu, P., Mandelboim, M., Rosental, B., Rosenberg, E., Diaz‐Griffero, F., et al. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e16750 · Cited by 8
Exploring the Interaction between E484K and N501Y Substitutions of SARS-CoV-2 in Shaping the Transmission Advantage of COVID-19 in Brazil: A Modeling Study
Zhao, S., Ran, J., & Han, L. (2021) · American Journal of Tropical Medicine and Hygiene · doi:10.4269/ajtmh.21-0412 · Cited by 7
Sharp Reductions in COVID-19 Case Fatalities and Excess Deaths in Peru in Close Time Conjunction, State-By-State, with Ivermectin TreatmentsPreprint
Chamie-Quintero, J. J., Hibberd, J. A., & Scheim, D. E. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3765018 · Cited by 8
Naturally-acquired immunity in Syrian Golden Hamsters provides protection from re-exposure to emerging heterosubtypic SARS-CoV-2 variants B.1.1.7 and B.1.351Preprint
Clark, J. J., Sharma, P., Bentley, E. G., Harding, A. C., Kipar, A., Neary, M., Box, H., Hughes, G. L., Patterson, E. I., Sharp, J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.10.434447 · Cited by 7
Bioinformatics analysis of SARS-CoV-2 RBD mutant variants and insights into antibody and ACE2 receptor bindingPreprint
Ranjan, P., Neha, N., Devi, C., & Das, P. K. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.03.438113 · Cited by 8
Cycle Threshold Probability Score for Immediate and Sensitive Detection of B.1.351 SARS-CoV-2 Lineage
Smet, D. D., Vanhee, M., Maes, B., Swaerts, K., Jaeger, P. D., Maelegheer, K., Hoecke, F. V., & Martens, G. A. (2021) · American Journal of Clinical Pathology · doi:10.1093/ajcp/aqab186 · Cited by 6
A review of epidemiology, clinical features and disease course, transmission dynamics, and neutralization efficacy of SARS-CoV-2 variants
Deb, P., Molla, M. M. A., Saif‐Ur‐Rahman, K., Das, M. C., & Das, D. (2021) · Egyptian Journal of Bronchology · doi:10.1186/s43168-021-00090-x · Cited by 7
Bottom-up Assembled Synthetic SARS-CoV-2 Miniviruses Reveal Lipid Membrane Affinity of Omicron Variant Spike Glycoprotein
Relimpio, A. Y., Fink, A., Bui, D. T., et al. (2023) · ACS Nano · doi:10.1021/acsnano.3c08323 · Cited by 7
Genome sequencing of SARS-CoV-2 reveals the prevalence of variant B 1.1.7 in Egypt
Seadawy, M. G., Gad, A. F., Abo-Elmaaty, S. A., & Hassan, M. G. (2021) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2021.105191 · Cited by 7
Nucleic Acid-Based COVID-19 Therapy Targeting Cytokine Storms: Strategies to Quell the Storm
Abusalah, M. A. H., Khalifa, M., Al-Hatamleh, M. A. I., Jarrar, M., Mohamud, R., & Yean, C. Y. (2022) · Journal of Personalized Medicine · doi:10.3390/jpm12030386 · Cited by 6
Neutralization Heterogeneity of Circulating SARS-CoV-2 Variants to Sera Elicited by a Vaccinee or Convalescent
Zhang, M., Gong, Y., & Jiao, S. (2022) · Future Virology · doi:10.2217/fvl-2021-0100 · Cited by 7
The Influence of New SARS-CoV-2 Variant Omicron (B.1.1.529) on Vaccine Efficacy, its Correlation to Delta Variants: A Computational Approach
Ranjan, P., Neha, N., Devi, C., Devar, K. A., & Das, P. K. (2022) · Microbial Pathogenesis · doi:10.1016/j.micpath.2022.105619 · Cited by 6
“The UK variant of B.1.1.7 lineage has 8 mutations in S protein that seems to be remaining susceptible for RNA-based COVID-19 vaccine BNT162b2 [39].”
BackgroundInfluential
Superrepellent Doubly Reentrant Geometry Promotes Antibiofouling and Prevention of Coronavirus Contamination
Lee, M., Chien, Y., Teng, P., et al. (2022) · Advanced Materials Technologies · doi:10.1002/admt.202200387 · Cited by 7
Structural basis and analysis of hamster ACE2 binding to different SARS-CoV-2 spike RBDs
Niu, S., Zhao, Z., Liu, Z., Rong, X., Chai, Y., Bai, B., Han, P., Shang, G., Ren, J., Wang, Y., et al. (2024) · Journal of Virology · doi:10.1128/jvi.01157-23 · Cited by 7
Evolutionary and Phenotypic Characterization of Two Spike Mutations in European Lineage 20E of SARS-CoV-2
Ruiz-Rodríguez, P., Francés-Gómez, C., Chiner‐Oms, Á., López, M. G., Jiménez-Serrano, S., Cancino‐Muñoz, I., Ruiz-Hueso, P., Torres‐Puente, M., Bracho, M. A., D’Auria, G., et al. (2021) · mBio · doi:10.1128/mbio.02315-21 · Cited by 8
Predicted Epitope Abundance Supports Vaccine-Induced Cytotoxic Protection Against SARS-CoV-2 Variants of Concern
Martín-Galiano, A. J., Díez‐Fuertes, F., McConnell, M. J., & López, D. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.732693 · Cited by 7
“It has been shown that humoral protection is retained by distinct vaccines against emerging viral lineages (3) (4) (5).”
Background
The Trade-off Between Prioritization and Vaccination Speed Depends on Mitigation Measures
Agarwal, N., Komo, A., Patel, C., Pathak, P. A., & Ünver, M. U. (2021) · National Bureau of Economic Research · doi:10.3386/w28519 · Cited by 7
Updated vaccine protects from infection with SARS-CoV-2 variants, prevents transmission and is immunogenic against Omicron in hamstersPreprint
Sharma, S., Vercruysse, T., Sánchez-Felipe, L., Kerstens, W., Rasulova, M., Abdelnabi, R., Foo, C. S.-Y., Lemmens, V., Looveren, D. V., Maes, P., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.11.12.468374 · Cited by 7
“Subsequent emergence of E484K within this lineage 74 hampers the activity of nAb suggestive for immune escape (7-9).”
Background
Molecular basis of broad neutralization against SARS-CoV-2 variants including Omicron by a human antibodyPreprint
Ju, B., Zheng, Q., Guo, H., Fan, Q., Li, T., Song, S., Sun, H., Shen, S., Zhou, X., Cheng, L., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.19.476892 · Cited by 7
T cell epitope mapping reveals immunodominance of evolutionarily conserved regions within SARS-CoV-2 proteome
Bozkus, C. C., Brown, M., Velazquez, L. G., Thomas, M., Wilson, E. A., O’Donnell, T. J., Kaminska, A., Ruchnewitz, D., Geertz, D., Bykov, Y., et al. (2025) · iScience · doi:10.1016/j.isci.2025.113044 · Cited by 9
“Antibody recognition of ancestral and Alpha (B.1.1.7) strain RBD was comparable across all time points tested, while there was a reduction in the recognition of Beta (B.1.351) and Gamma (P.1) RBD (Figure 2A), consistent with other studies showing limited antigenic change with Alpha 36 and reduced viral neutralization…”
Influential
A Barcoded Flow Cytometric Assay to Explore the Antibody Responses Against SARS-CoV-2 Spike and Its Variants
Vesper, N., Ortiz, Y. M., Bartels-Burgahn, F., Yang, J., de la Rosa, K., Tenbusch, M., Schulz, S. R., Finzel, S., Jäck, H., Eibel, H., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.730766 · Cited by 6
“This is in line with a study showing that the protective antibody respose of mRNA vaccinated person is sufficient but lower in the case of the alpha mutant (29).”
Result
Early clinical trial data and real‐world assessment of COVID‐19 vaccines: Insights from the Society of Infectious Diseases Pharmacists
Patel, N., Bouchard, J. L., Oliver, M. B., Badowski, M. E., Carreno, J. J., & the Society of Infectious Diseases Pharmacists (2021) · Pharmacotherapy The Journal of Human Pharmacology and Drug Therapy · doi:10.1002/phar.2622 · Cited by 5
COVID-19 Vaccination: The Mainspring of Challenges and the Seed of Remonstrance
Najjar, H., Al-Jighefee, H. T., Qush, A., Ahmed, M. N., Awwad, S., & Kamareddine, L. (2021) · Vaccines · doi:10.3390/vaccines9121474 · Cited by 6
Epidemiological and genomic findings of the first documented Italian outbreak of SARS-CoV-2 Alpha variant of concern
Amato, L., Candeloro, L., Girolamo, A. D., Savini, L., Puglia, I., Marcacci, M., Caporale, M., Mangone, I., Cammà, C., Conte, A., et al. (2022) · Epidemics · doi:10.1016/j.epidem.2022.100578 · Cited by 6
“Nevertheless, immunity from previous infections was overall secured towards Alpha VOC, as secured was the protection against the disease provided by the vaccination (Muik et al., 2021; World Health Organization WHO, 2021b).”
Prioritizing COVID-19 vaccination. Part 2: Real-time comparison between single-dose and double-dose in Japan
Kobayashi, T., & Nishiura, H. (2022) · Mathematical Biosciences & Engineering · doi:10.3934/mbe.2022350 · Cited by 6
Third booster vaccination and stopping the Omicron, a new variant of concern
Ghazvini, K., Karbalaei, M., & Keikha, M. (2022) · Vacunas · doi:10.1016/j.vacun.2022.05.005 · Cited by 6
Will Peptides Help to Stop COVID-19?
Krut’, V. G., Chuvpilo, S. A., Astrakhantseva, I. V., Kozlovskaya, L. I., Efimov, G. A., Kruglov, A., Drutskaya, M. S., & Nedospasov, S. A. (2022) · Biochemistry (Moscow) · doi:10.1134/s0006297922070021 · Cited by 7
Structure-based design of oligomeric receptor-binding domain (RBD) recombinant proteins as potent vaccine candidates against SARS-CoV-2
Zhang, T., Zheng, N., Wang, Z., & Xu, X. (2023) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2023.2174755 · Cited by 6
“However, during the epidemic period, the virus has undergone multiple mutations, resulting in a decline in the effectiveness of the vaccines initially developed.(1,2) It is expected that new waves of transmission may still occur in the future as new variants of SARS-CoV-2 continuously emerge.”
BackgroundMethod
Assessment of automated high-throughput serological assays for prediction of high-titer SARS-CoV-2 neutralizing antibody
Moscato, G. A., Mazzetti, P., Lucenteforte, E., Rosellini, A., Cara, A., Quaranta, P., Mainardi, V., Villa, P., Focosi, D., Lanza, M., et al. (2021) · Journal of Clinical Virology Plus · doi:10.1016/j.jcvp.2021.100016 · Cited by 6
Zoonotic and anthropozoonotic potential of COVID-19 and its implications for public health
El-Sayed, A., Abdel‐Daim, M. M., & Kamel, M. S. (2021) · Environmental Science and Pollution Research · doi:10.1007/s11356-021-16415-8 · Cited by 6
“In addition, this mutation is characterized by its higher spread rate and ability to escape from vaccinal protection (Iacobucci 2021, Muik et al. 2021, Supasa et al. 2021).”
Background
Neutralization of European, South African, and United States SARS-CoV-2 mutants by a human antibody and antibody domainsPreprint
Sun, Z., Kim, A., Sobolewski, M. D., Enick, N., Chen, C., Adams, C., Jacobs, J. L., McCormick, K. D., Mellors, J. W., Dimitrov, D. S., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.22.436481 · Cited by 6
Vaccination shapes evolutionary trajectories of SARS-CoV-2Preprint
Meijers, M., Ruchnewitz, D., Łuksza, M., & Lässig, M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.07.19.500637 · Cited by 6

Authors: Muik, A., Wallisch, A.-K., Sänger, B., Swanson, K. A., Mühl, J., Chen, W., Cai, H., Maurus, D., Sarkar, R., Türeci, Ö., Dormitzer, P. R., & Şahin, U.
Affiliations: BioNTech (Germany) (DE)
Pfizer (United States) (US)
Johannes Gutenberg University Mainz (DE)
Corresponding author: Şahin, Uğur
ORCID: Muik, Alexander
Wallisch, Ann-Kathrin
Sänger, Bianca
Swanson, Kena A.
Mühl, Julia
Chen, Wei
Cai, Hui
Maurus, Daniel
Türeci, Özlem
Dormitzer, Philip R.
Şahin, Uğur
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2021-03-12
Volume: 371
Issue: 6534
Pages: 1152-1153
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.abg6105
PMC: PMC7971771
OpenAlex: W3123108673
Semantic Scholar: a28b6633cf65c49f1251702b8e3e3c1b85e19236
Cited by: 515
References: 12
Citations by year: 2026: 4 · 2025: 8 · 2024: 17 · 2023: 34 · 2022: 152 · 2021: 298
FWCI: 39.63
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Science (publishedVersion, cc-by)
bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: Pfizer
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, B.1.1.7 lineage, BNT162b2, mRNA vaccines, neutralizing antibodies, spike protein mutations, vaccine escape, pseudovirus neutralization
MeSH terms: COVID-19, SARS-CoV-2, COVID-19 Vaccines, BNT162 Vaccine, Adult, Aged, Antibodies, Viral, China, Female, United Kingdom, Humans, Male, Middle Aged, Neutralization Tests, Young Adult, Antibodies, Neutralizing, Spike Glycoprotein, Coronavirus

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Neutralization of SARS-CoV-2 lineage B.1.1.7 pseudovirus by BNT162b2 vaccine–elicited human sera

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