Functional differences among the spike glycoproteins of multiple emerging severe acute respiratory syndrome coronavirus 2 variants of concern
Open accessAbstract
We compared the functional properties of spike (S) glycoproteins from the original SARS-CoV-2 strain (D614) (Wuhan, China), the globally dominant D614G strain, and emerging geographic variants: B.1.1.7 (United Kingdom), B.1.351 (South Africa), P.1 (Brazil), and B.1.1.248 (Brazil/Japan). Compared with D614G, the emerging variants exhibited an increased affinity for the receptor, ACE2, and increased ability to infect cells with low ACE2 levels. All variants lost infectivity similarly at room temperature and 37°C; however, in the cold, B.1.1.7 was more stable, and P.1 and B.1.1.248 were less stable. Shedding of the S1 glycoprotein from the S contributed to virus inactivation in the cold. B.1.351, P.1, and B.1.1.248 were neutralized by convalescent and vaccinee sera less efficiently than the other variants. S glycoprotein properties such as requirements for ACE2 levels on the target cell, functional stability in the cold, and resistance to host neutralizing antibodies potentially contribute to the outgrowth of emerging SARS-CoV-2 variants.
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Some amino acid changes shared with Alpha, Beta, Gamma, or Delta VOCs lead to increased transmissibility and partial escape from vaccine-induced humoral immunity.
“Some amino acid changes [Δ69/70, T95I, G142D, Δ145, K417N, T478K, N501Y, and P681H (T, Thr; I, Ile; G, Gly; D, Asp; K, Lys; N, Asn; Y, Tyr; P, Pro; H, His)] are shared mutations also found in the Alpha, Beta (B.1.351), Gamma (P.1), or Delta VOCs and were described to lead to increased transmissibility, as well as to a typically mild partial escape from vaccine-induced humoral immunity (7–10).”
From Neutralization of SARS-CoV-2 Omicron by BNT162b2 mRNA vaccine–elicited human sera (2022) · cites this paper as [9]
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- Authors
- Wang, Q., Nair, M. S., Anang, S., Zhang, S., Nguyen, H., Huang, Y., Liu, L., Ho, D. D., & Sodroski, J. G.
- Affiliations
- Harvard University (US)
- Aaron Diamond AIDS Research Center (US)
- Corresponding author
- Sodroski, Joseph G.
- ORCID
- Venue
- iScience
- Publisher
- Elsevier BV
- Published
- 2021-11
- Volume
- 24
- Issue
- 11
- Pages
- 103393
- ISSN
- 2589-0042 (ISSN-L)
- PMC
- PMC8559451
- OpenAlex
- W3208906316
- Cited by
- 15
- References
- 54
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 5 · 2022: 7
- FWCI
- 1.11
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- iScience (publishedVersion, cc-by-nc-nd)
- 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
- 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
- Health Sciences › Medicine › Infectious Diseases › COVID-19 Clinical Research Studies
- Keywords
- SARS-CoV-2, spike protein, SARS-CoV-2 variants of concern, D614G mutation, Alpha variant, Beta variant, P.1 variant, neutralizing antibodies, vaccine escape, viral infectivity
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