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  Antibody accessibility determines location of spike surface mutations in SARS-CoV-2 variants

von Bülow, S., Sikora, M., Blanc, F. E. C., Covino, R., & Hummer, G. (2023). Antibody accessibility determines location of spike surface mutations in SARS-CoV-2 variants. PLoS Computational Biology, 19(1): e1010822. doi:10.1371/journal.pcbi.1010822.

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 Creators:
von Bülow, Sören1, Author                 
Sikora, Mateusz1, 2, Author                 
Blanc, Florian E. C.1, Author                 
Covino, Roberto3, Author
Hummer, Gerhard1, 4, Author                 
Affiliations:
1Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
2Malopolska Centre of Biotechnology, Jagiellonian University, Kraków, Poland, ou_persistent22              
3Frankfurt Institute for Advanced Studies, Frankfurt am Main, Germany, ou_persistent22              
4Institute of Biophysics, Goethe University Frankfurt, Frankfurt am Main, Germany, ou_persistent22              

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Free keywords: Antibodies, Biochemical simulations, Glycosylation, Immune response, Molecular dynamics, Protein structure, SARS CoV 2, Vaccination and immunization
 Abstract: The steady emergence of SARS-CoV-2 variants gives us a real-time view of the interplay between viral evolution and the host immune defense. The spike protein of SARS-CoV-2 is the primary target of antibodies. Here, we show that steric accessibility to antibodies provides a strong predictor of mutation activity in the spike protein of SARS-CoV-2 variants, including Omicron. We introduce an antibody accessibility score (AAS) that accounts for the steric shielding effect of glycans at the surface of spike. We find that high values of the AAS correlate strongly with the sites of mutations in the spike proteins of newly emerging SARS-CoV-2 variants. We use the AAS to assess the escapability of variant spike proteins, i.e., their ability to escape antibody-based immune responses. The high calculated escapability of the Omicron variant BA.5 with respect to both wild-type (WT) vaccination and BA.1 infection is consistent with its rapid spread despite high rates of vaccination and prior infection with earlier variants. We calculated the AAS from structural and molecular dynamics simulation data that were available early in the pandemic, in the spring of 2020. The AAS thus allows us to prospectively assess the ability of variant spike proteins to escape antibody-based immune responses and to pinpoint regions of expected mutation activity in future variants.

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Language(s): eng - English
 Dates: 2022-04-072022-12-172023-01-24
 Publication Status: Published online
 Pages: 15
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1371/journal.pcbi.1010822
BibTex Citekey: bulow_antibody_2023
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Title: PLoS Computational Biology
Source Genre: Journal
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Publ. Info: San Francisco, CA : Public Library of Science
Pages: - Volume / Issue: 19 (1) Sequence Number: e1010822 Start / End Page: - Identifier: ISSN: 1553-734X
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000017180_1