Targeting the Spike: Repurposing Mithramycin and Dihydroergotamine to Block SARS-CoV-2 Infection.


Journal

ACS omega
ISSN: 2470-1343
Titre abrégé: ACS Omega
Pays: United States
ID NLM: 101691658

Informations de publication

Date de publication:
21 Nov 2023
Historique:
received: 28 04 2023
accepted: 15 09 2023
medline: 29 11 2023
pubmed: 29 11 2023
entrez: 29 11 2023
Statut: epublish

Résumé

The urgency to find complementary therapies to current SARS-CoV-2 vaccines, whose effectiveness is preserved over time and not compromised by the emergence of new and emerging variants, has become a critical health challenge. We investigate the possibility of jamming the opening of the Receptor Binding Domain (RBD) of the spike protein of SARS-CoV-2 with small compounds. Through in silico screening, we identified two potential candidates that would lock the Receptor Binding Domain (RBD) in a closed configuration, preventing the virus from infecting the host cells. We show that two drugs already approved by the FDA, mithramycin and dihydroergotamine, can block infection using concentrations in the μM range in cell-based assays. Further STD-NMR experiments support dihydroergotamine's direct interaction with the spike protein. Overall, our results indicate that repurposing of these compounds might lead to potential clinical drug candidates for the treatment of SARS-CoV-2 infection.

Identifiants

pubmed: 38027314
doi: 10.1021/acsomega.3c02921
pmc: PMC10666140
doi:

Types de publication

Journal Article

Langues

eng

Pagination

43490-43499

Informations de copyright

© 2023 The Authors. Published by American Chemical Society.

Déclaration de conflit d'intérêts

The authors declare no competing financial interest.

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Auteurs

Soledad Stagnoli (S)

Structure and Cell Biology of Viruses Lab, Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), 48160 Derio, Spain.

Gabriele Macari (G)

Department of Sciences, University of Rome Tre, 00154 Rome, Italy.

Pietro Corsi (P)

Department of Sciences, University of Rome Tre, 00154 Rome, Italy.

Barbara Capone (B)

Department of Sciences, University of Rome Tre, 00154 Rome, Italy.

Ander Vidaurrazaga (A)

Structure and Cell Biology of Viruses Lab, Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), 48160 Derio, Spain.

June Ereño-Orbea (J)

Chemical Glycobiology Laboratory, CIC bioGUNE, BRTA, 48160 Derio, Spain.
IKERBASQUE, Basque Foundation for Science, 48009 Bilbao, Spain.

Ana Ardá (A)

Chemical Glycobiology Laboratory, CIC bioGUNE, BRTA, 48160 Derio, Spain.

Fabio Polticelli (F)

Department of Sciences, University of Rome Tre, 00154 Rome, Italy.
National Institute of Nuclear Physics, Roma Tre Section, 00154 Rome, Italy.

Jesús Jiménez-Barbero (J)

Chemical Glycobiology Laboratory, CIC bioGUNE, BRTA, 48160 Derio, Spain.
IKERBASQUE, Basque Foundation for Science, 48009 Bilbao, Spain.
Centro de Investigación Biomédica En Red de Enfermedades Respiratorias. (CIBERES), Instituto de Salud Carlos III, 28029 Madrid, Spain.
Department of Organic & Inorganic Chemistry, Faculty of Science and Technology University of the Basque Country, EHU-UPV, 48940 Leioa, Spain.

Nicola Ga Abrescia (NG)

Structure and Cell Biology of Viruses Lab, Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), 48160 Derio, Spain.
IKERBASQUE, Basque Foundation for Science, 48009 Bilbao, Spain.
Centro de Investigación Biomédica en Red de Enfermedades Hepáticas y Digestivas (CIBERehd), Instituto de Salud Carlos III, 28029 Madrid, Spain.

Ivan Coluzza (I)

IKERBASQUE, Basque Foundation for Science, 48009 Bilbao, Spain.
Computational Soft Matter and Biophysics Lab, Basque Center for Materials, Applications and Nanostructures (BCMaterials), Buil. Martina Casiano, Pl. 3 Parque Científico UPV/EHU Barrio Sarriena, 48940 Leioa, Spain.

Classifications MeSH