Increased resistance of SARS-CoV-2 variant P.1 to antibody neutralization
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Abstract
The emergence of SARS-CoV-2 variants has raised concerns about altered sensitivity to antibody-mediated immunity. The relative resistance of SARS-CoV-2 variants B.1.1.7 and B.1.351 to antibody neutralization has been recently investigated. We report that another emergent variant from Brazil, P.1, is not only refractory to multiple neutralizing monoclonal antibodies but also more resistant to neutralization by convalescent plasma and vaccinee sera. The magnitude of resistance is greater for monoclonal antibodies than vaccinee sera and evident with both pseudovirus and authentic P.1 virus. The cryoelectron microscopy structure of a soluble prefusion-stabilized spike reveals that the P.1 trimer adopts exclusively a conformation in which one of the receptor-binding domains is in the "up" position, which is known to facilitate binding to entry receptor ACE2. The functional impact of P.1 mutations thus appears to arise from local changes instead of global conformational alterations. The P.1 variant threatens current antibody therapies but less so protective vaccine efficacy.
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Neutralizing activity of mRNA vaccines against B.1.351 was lower by a factor of 8.6 for mRNA-1273 and 6.5 for BNT-162b2 than against D614G, with no difference against B.1.1.7-like mutant.
“Neutralizing activity of the two mRNA vaccines against the B.1.351 variant has also been observed to be lower, by a factor of 8.6 (mRNA-1273 vaccine [Moderna]) or 6.5 (BNT-162b2 vaccine [Pfizer]) on pseudovirus neutralization assay, than activity against the D614G virus, whereas no difference was evident against the N510Y.V1 (B.1.1.7)–like mutant.19,28,29”
From Efficacy of the ChAdOx1 nCoV-19 Covid-19 Vaccine against the B.1.351 Variant (2021) · cites this paper as [19]
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Self-citation
- Authors
- Wang, P., Casner, R. G., Nair, M. S., Wang, M., Yu, J., Cerutti, G., Liu, L., Kwong, P. D., Huang, Y., Shapiro, L., & Ho, D. D.
- Affiliations
- Aaron Diamond AIDS Research Center (US)
- Columbia University (US)
- National Institutes of Health (US)
- Corresponding author
- Wang, Pengfei
- Shapiro, Lawrence
- Ho, David D.
- ORCID
- Venue
- Cell Host & Microbe
- Publisher
- Elsevier BV
- Published
- 2021-05
- Volume
- 29
- Issue
- 5
- Pages
- 747-751.e4
- ISSN
- 1931-3128 (ISSN-L)
- PMC
- PMC8053237
- OpenAlex
- W3156291144
- Cited by
- 636
- References
- 5
- Citations by year
- 2026: 8 · 2025: 23 · 2024: 43 · 2023: 77 · 2022: 239 · 2021: 246
- FWCI
- 48.06
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 376 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell Host & Microbe (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- Funders
- JPB Foundation
- Bill & Melinda Gates Foundation
- NIH
- 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, P.1 variant, Alpha variant, Beta variant, neutralizing monoclonal antibodies, convalescent plasma, spike protein, receptor binding domain, ACE2 binding, pseudovirus, vaccine efficacy
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