Cited by 385SARS-CoV-2 and COVID-19 Researchvaccines and immunoinformatics approachesAnimal Virus Infections Studies

SARS-CoV-2 spike E484K mutation reduces antibody neutralisation

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Jangra, Sonia, Ye, Chengjin, Rathnasinghe, Raveen, Stadlbauer, Daniel, Alshammary, Hala, Amoako, Angela A., Awawda, Mahmoud H., Beach, Katherine F +22 more·2021·The Lancet Microbe

Abstract

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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Crossref · 10.1016/s2666-5247(21)00068-9

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  • Eta showed reduced neutralization by bamlanivimab and etesevimab monoclonal antibodies and convalescent sera.

    “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]

    In the paper’s main text (page not provided), convalescent sera neutralised a recombinant virus carrying E484K less efficiently than the comparison virus. The study did not test Eta as a variant or report results for bamlanivimab or etesevimab, so those parts of the claim are not supported by this source. (LLM, conf=0.86)

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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
Venue
The Lancet Microbe
Publisher
Elsevier BV
Published
2021-07
Volume
2
Issue
7
Pages
e283-e284
ISSN
2666-5247 (ISSN-L)
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
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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