Scholars@Duke publication: Structural diversity of the SARS-CoV-2 Omicron spike.

Structural diversity of the SARS-CoV-2 Omicron spike.

Publication , Journal Article

Gobeil, SM-C; Henderson, R; Stalls, V; Janowska, K; Huang, X; May, A; Speakman, M; Beaudoin, E; Manne, K; Li, D; Parks, R; Barr, M; Deyton, M ...

Published in: Mol Cell

June 2, 2022

Published version (DOI) Link to item

Aided by extensive spike protein mutation, the SARS-CoV-2 Omicron variant overtook the previously dominant Delta variant. Spike conformation plays an essential role in SARS-CoV-2 evolution via changes in receptor-binding domain (RBD) and neutralizing antibody epitope presentation, affecting virus transmissibility and immune evasion. Here, we determine cryo-EM structures of the Omicron and Delta spikes to understand the conformational impacts of mutations in each. The Omicron spike structure revealed an unusually tightly packed RBD organization with long range impacts that were not observed in the Delta spike. Binding and crystallography revealed increased flexibility at the functionally critical fusion peptide site in the Omicron spike. These results reveal a highly evolved Omicron spike architecture with possible impacts on its high levels of immune evasion and transmissibility.

Duke Scholars

Author Rory Henderson Duke Human Vaccine Institute

Author David Charles Montefiori Surgery, Surgical Sciences

Author Kevin O'Neil Saunders Surgery, Surgical Sciences

Author Kevin J Wiehe Medicine, Duke Human Vaccine Institute

Author Wilton Bryan Williams Surgery, Surgical Sciences

Author Barton Ford Haynes Medicine, Duke Human Vaccine Institute

Author Priyamvada Acharya Surgery, Surgical Sciences

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Published In

Mol Cell

DOI

10.1016/j.molcel.2022.03.028

EISSN

1097-4164

Publication Date

June 2, 2022

Volume

Issue

Start / End Page

2050 / 2068.e6

Location

United States

Related Subject Headings

Spike Glycoprotein, Coronavirus
SARS-CoV-2
Mutation
Humans
Developmental Biology
COVID-19
Angiotensin-Converting Enzyme 2
42 Health sciences
32 Biomedical and clinical sciences
31 Biological sciences

Citation

APA

Chicago

ICMJE

MLA

NLM

Gobeil, S.-C., Henderson, R., Stalls, V., Janowska, K., Huang, X., May, A., … Acharya, P. (2022). Structural diversity of the SARS-CoV-2 Omicron spike. Mol Cell, 82(11), 2050-2068.e6. https://doi.org/10.1016/j.molcel.2022.03.028

Gobeil, Sophie M-C, Rory Henderson, Victoria Stalls, Katarzyna Janowska, Xiao Huang, Aaron May, Micah Speakman, et al. “Structural diversity of the SARS-CoV-2 Omicron spike.” Mol Cell 82, no. 11 (June 2, 2022): 2050-2068.e6. https://doi.org/10.1016/j.molcel.2022.03.028.

Gobeil SM-C, Henderson R, Stalls V, Janowska K, Huang X, May A, et al. Structural diversity of the SARS-CoV-2 Omicron spike. Mol Cell. 2022 Jun 2;82(11):2050-2068.e6.

Gobeil, Sophie M. C., et al. “Structural diversity of the SARS-CoV-2 Omicron spike.” Mol Cell, vol. 82, no. 11, June 2022, pp. 2050-2068.e6. Pubmed, doi:10.1016/j.molcel.2022.03.028.

Gobeil SM-C, Henderson R, Stalls V, Janowska K, Huang X, May A, Speakman M, Beaudoin E, Manne K, Li D, Parks R, Barr M, Deyton M, Martin M, Mansouri K, Edwards RJ, Eaton A, Montefiori DC, Sempowski GD, Saunders KO, Wiehe K, Williams W, Korber B, Haynes BF, Acharya P. Structural diversity of the SARS-CoV-2 Omicron spike. Mol Cell. 2022 Jun 2;82(11):2050-2068.e6.

Published In

Mol Cell

DOI

10.1016/j.molcel.2022.03.028

EISSN

1097-4164

Publication Date

June 2, 2022

Volume

Issue

Start / End Page

2050 / 2068.e6

Location

United States

Related Subject Headings

Spike Glycoprotein, Coronavirus
SARS-CoV-2
Mutation
Humans
Developmental Biology
COVID-19
Angiotensin-Converting Enzyme 2
42 Health sciences
32 Biomedical and clinical sciences
31 Biological sciences