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SARS-CoV-2 spike E484K mutation reduces antibody neutralisation
Open accessAbstract
It is concerning that emerging variants of SARS-CoV-2 can evade neutralising antibodies induced by previous infection or vaccination through mutations in the spike protein, including the receptor-binding domain (RBD). The asparagine (N) to tyrosine (Y) substitution at position 501 (N501Y), present in variants of concern belonging to the B.1.1.7, B.1.351, and P.1 lineages, does not seem to affect in-vitro neutralisation of human convalescent or post-vaccination sera. However, additional substitutions, such as E484K present in B.1.351 and P.1 lineages, might allow evasion from neutralising antibodies.
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“This variant showed reduced neutralization by bamlanivimab and etesevimab monoclonal antibodies and convalescent sera [43, 44].”
From Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe (2022) · cites this paper as [44]
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Metadata
- Authors
- Jangra, S., Ye, C., Rathnasinghe, R., Stadlbauer, D., Alshammary, H., Amoako, A. A., Awawda, M. H., Beach, K. F., Bermúdez-González, M. C., Chernet, R. L., Eaker, L. Q., Ferreri, E. D., Floda, D. L., Gleason, C. R., Kleiner, G., Jurczyszak, D., Matthews, J. C., Mendez, W. A., Mulder, L. C. F., Russo, K. T., Salimbangon, A.-B. T., Saksena, M., Shin, A. S., Sominsky, L. A., Srivastava, K., Krammer, F., Simon, V., Martinez-Sobrido, L., García-Sastre, A., & Schotsaert, M.
- Affiliations
- Icahn School of Medicine at Mount Sinai (US)
- Texas Biomedical Research Institute (US)
- Tisch Cancer Institute (US)
- Corresponding author
- Schotsaert, Michael
- ORCID
- Jangra, Sonia
- Ye, Chengjin
- Rathnasinghe, Raveen
- Stadlbauer, Daniel
- Alshammary, Hala
- Amoako, Angela A.
- Beach, Katherine F
- Bermúdez-González, Maria C.
- Chernet, Rachel L.
- Ferreri, Emily D.
- Gleason, Charles R.
- Kleiner, Giulio
- Jurczyszak, Denise
- Mulder, Lubbertus C.F.
- Saksena, Miti
- Sominsky, Levy A.
- Krammer, Florian
- Simon, Viviana
- Schotsaert, Michael
- Venue
- The Lancet Microbe
- Publisher
- Elsevier BV
- Published
- 2021-07
- Volume
- 2
- Issue
- 7
- Pages
- e283-e284
- ISSN
- 2666-5247 (ISSN-L)
- PMC
- PMC8026167
- OpenAlex
- W3142966103
- Cited by
- 385
- References
- 8
- Citations by year
- 2026: 7 · 2025: 22 · 2024: 35 · 2023: 55 · 2022: 144 · 2021: 121
- FWCI
- 28.11
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- The Lancet Microbe (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- ImmPort
- Funders
- JPB Foundation (2020\u2013215611)
- U.S. Department of Health and Human Services (HHSN272201400005C)
- NCI (U54CA260560)
- National Institutes of Health
- Pfizer
- NIAID (75N93019C00051, HHSN272201400005C)
- 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
- SARS-CoV-2, spike protein, E484K mutation, antibody neutralization, antibody escape, receptor binding domain, Omicron variant, Beta variant, P.1 lineage, convalescent sera, vaccine-induced antibodies
- MeSH terms
- COVID-19, SARS-CoV-2, Humans, Mutation, Antibodies, Neutralizing, Spike Glycoprotein, Coronavirus
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