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Article Dans Une Revue Proceedings of the National Academy of Sciences of the United States of America Année : 2024

Viruses traverse the human proteome through peptide interfaces that can be biomimetically leveraged for drug discovery

Laurène Meyniel-Schicklin
Jérôme Amaudrut
Laetitia Lines
Farès Halitim
  • Fonction : Auteur
Jean-Laurent Paparin
  • Fonction : Auteur
Peter Machin
  • Fonction : Auteur
Raphaël Darteil
  • Fonction : Auteur
Diane Sampson
  • Fonction : Auteur
Eric C Meldrum
  • Fonction : Auteur
Benoit de Chassey

Résumé

Significance Viruses have designed small protein interfaces to interact with human proteins. These viral peptides are original molecules to modulate the activity of host targets and an inspiration to create original drugs. Here, the wealth of virus-host protein interactions existing in the literature is integrated in an substantial database. A sample peptide library is screened against several pathogens, highlighting peptides modulators of replication. From one of them, a drug discovery program identifies highly potent antiviral molecules interacting with human metabolic targets. These molecules are proven to be active for treatment of mouse model of nonalcoholic steatohepatitis with chronic kidney disease. Our approach validates an original biomimetic framework to address cellular functions for fundamental applications and drug discovery.
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jeudi 23 janvier 2025
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Dates et versions

hal-04411218 , version 1 (23-01-2024)

Identifiants

Citer

Laurène Meyniel-Schicklin, Jérôme Amaudrut, Pierre Mallinjoud, Fabrice Guillier, Philippe E Mangeot, et al.. Viruses traverse the human proteome through peptide interfaces that can be biomimetically leveraged for drug discovery. Proceedings of the National Academy of Sciences of the United States of America, 2024, 121 (5), pp.e2308776121. ⟨10.1073/pnas.2308776121⟩. ⟨hal-04411218⟩
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