Charge Matters: Mutations in Omicron Variant Favor Binding to Cells.


Journal

Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
Titre abrégé: Chembiochem
Pays: Germany
ID NLM: 100937360

Informations de publication

Date de publication:
18 03 2022
Historique:
revised: 11 01 2022
received: 14 12 2021
pubmed: 13 1 2022
medline: 29 3 2022
entrez: 12 1 2022
Statut: ppublish

Résumé

Evidence is strengthening to suggest that the novel SARS-CoV-2 mutant Omicron, with its more than 60 mutations, will spread and dominate worldwide. Although the mutations in the spike protein are known, the molecular basis for why the additional mutations in the spike protein that have not previously occurred account for Omicron's higher infection potential, is not understood. We propose, based on chemical rational and molecular dynamics simulations, that the elevated occurrence of positively charged amino acids in certain domains of the spike protein (Delta: +4; Omicron: +5 vs. wild type) increases binding to cellular polyanionic receptors, such as heparan sulfate due to multivalent charge-charge interactions. This observation is a starting point for targeted drug development.

Identifiants

pubmed: 35020256
doi: 10.1002/cbic.202100681
pmc: PMC9015620
doi:

Substances chimiques

Spike Glycoprotein, Coronavirus 0
spike protein, SARS-CoV-2 0

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

e202100681

Subventions

Organisme : EXIST
Organisme : Berlin University Alliance G2 Global Health
Organisme : IRTG 2662

Informations de copyright

© 2022 The Authors. ChemBioChem published by Wiley-VCH GmbH.

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Auteurs

Chuanxiong Nie (C)

Institut für Chemie und Biochemie, Freie Universität Berlin, Takustrasse 3, 14195, Berlin, Germany.

Anil Kumar Sahoo (AK)

Fachbereich Physik, Freie Universität Berlin, 14195, Berlin, Germany.
Max Planck Institute of Colloids and Interfaces, 14476, Potsdam, Germany.

Roland R Netz (RR)

Fachbereich Physik, Freie Universität Berlin, 14195, Berlin, Germany.

Andreas Herrmann (A)

Institut für Chemie und Biochemie, Freie Universität Berlin, Takustrasse 3, 14195, Berlin, Germany.

Matthias Ballauff (M)

Institut für Chemie und Biochemie, Freie Universität Berlin, Takustrasse 3, 14195, Berlin, Germany.

Rainer Haag (R)

Institut für Chemie und Biochemie, Freie Universität Berlin, Takustrasse 3, 14195, Berlin, Germany.

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Classifications MeSH