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Discovery of potent SARS-CoV-2 nsp3 macrodomain inhibitors uncovers lack of translation to cellular antiviral response.
Lee, Alpha A; Amick, Isabelle; Aschenbrenner, Jasmin C; Barr, Haim M; Benjamin, Jared; Brandis, Alexander; Cohen, Galit; Diaz-Tapia, Randy; Duberstein, Shirly; Dixon, Jessica; Cousins, David; Fairhead, Michael; Fearon, Daren; Frick, James; Gayvert, James; Godoy, Andre S; Griffin, Ed J; Huber, Kilian; Koekemoer, Lizbé; Lahav, Noa; Marples, Peter G; McGovern, Briana L; Mehlman, Tevie; Robinson, Matthew C; Singh, Usha; Szommer, Tamas; Tomlinson, Charles W E; Vargo, Thomas; von Delft, Frank; Wang, SiYi; White, Kris; Williams, Eleanor; Winokan, Max.
Afiliación
  • Lee AA; ASAP Discovery Consortium.
  • Amick I; PostEra Inc, 1 Broadway, Cambridge MA 02142.
  • Aschenbrenner JC; ASAP Discovery Consortium.
  • Barr HM; PostEra Inc, 1 Broadway, Cambridge MA 02142.
  • Benjamin J; ASAP Discovery Consortium.
  • Brandis A; Diamond Light Source Ltd, Harwell Science and Innovation Campus, Didcot OX11 0QX, UK.
  • Cohen G; Research Centre at Harwell, Harwell Science and Innovation Campus, Didcot OX11 0QX, UK.
  • Diaz-Tapia R; ASAP Discovery Consortium.
  • Duberstein S; The Wohl Drug Discovery Institute of the Nancy and Stephen Grand Israel National Center for Personalized Medicine, Weizmann Institute of Science, Rehovot 7610001, Israel.
  • Dixon J; ASAP Discovery Consortium.
  • Cousins D; Icahn School of Medicine, Mount Sinai, New York, New York, United States of America.
  • Fairhead M; ASAP Discovery Consortium.
  • Fearon D; Life Sciences Core Facilities, The Weizmann Institute of Science Rehovot 7610001, Israel.
  • Frick J; The Wohl Drug Discovery Institute of the Nancy and Stephen Grand Israel National Center for Personalized Medicine, Weizmann Institute of Science, Rehovot 7610001, Israel.
  • Gayvert J; ASAP Discovery Consortium.
  • Godoy AS; Icahn School of Medicine, Mount Sinai, New York, New York, United States of America.
  • Griffin EJ; ASAP Discovery Consortium.
  • Huber K; The Wohl Drug Discovery Institute of the Nancy and Stephen Grand Israel National Center for Personalized Medicine, Weizmann Institute of Science, Rehovot 7610001, Israel.
  • Koekemoer L; ASAP Discovery Consortium.
  • Lahav N; Centre for Medicines Discovery, University of Oxford, Oxford OX3 7FZ, UK.
  • Marples PG; ASAP Discovery Consortium.
  • McGovern BL; MedChemica Consultancy Ltd, Macclesfield, Cheshire, SK11 6DU, UK.
  • Mehlman T; ASAP Discovery Consortium.
  • Robinson MC; Centre for Medicines Discovery, University of Oxford, Oxford OX3 7FZ, UK.
  • Singh U; ASAP Discovery Consortium.
  • Szommer T; Diamond Light Source Ltd, Harwell Science and Innovation Campus, Didcot OX11 0QX, UK.
  • Tomlinson CWE; Research Centre at Harwell, Harwell Science and Innovation Campus, Didcot OX11 0QX, UK.
  • Vargo T; ASAP Discovery Consortium.
  • von Delft F; PostEra Inc, 1 Broadway, Cambridge MA 02142.
  • Wang S; ASAP Discovery Consortium.
  • White K; PostEra Inc, 1 Broadway, Cambridge MA 02142.
  • Williams E; ASAP Discovery Consortium.
  • Winokan M; São Carlos Institute of Physics, University of São Paulo, Av. Joao Dagnone, 1100 - Jardim Santa Angelina, Sao Carlos, 13563-120, Brazil.
bioRxiv ; 2024 Aug 21.
Article en En | MEDLINE | ID: mdl-39229055
ABSTRACT
A strategy for pandemic preparedness is the development of antivirals against a wide set of viral targets with complementary mechanisms of action. SARS-CoV-2 nsp3-mac1 is a viral macrodomain with ADP-ribosylhydrolase activity, which counteracts host immune response. Targeting the virus' immunomodulatory functionality offers a differentiated strategy to inhibit SARS-CoV-2 compared to approved therapeutics, which target viral replication directly. Here we report a fragment-based lead generation campaign guided by computational approaches. We discover tool compounds which inhibit nsp3-mac1 activity at low nanomolar concentrations, and with responsive structure-activity relationships, high selectivity, and drug-like properties. Using our inhibitors, we show that inhibition of nsp3-mac1 increases ADP-ribosylation, but surprisingly does not translate to demonstrable antiviral activity in cell culture and iPSC-derived pneumocyte models. Further, no synergistic activity is observed in combination with interferon gamma, a main protease inhibitor, nor a papain-like protease inhibitor. Our results question the extent to which targeting modulation of innate immunity-driven ADP-ribosylation can influence SARS-CoV-2 replication. Moreover, these findings suggest that nsp3-mac1 might not be a suitable target for antiviral therapeutics development.

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: BioRxiv Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: BioRxiv Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos