Structural insight into the cGAS active site explains differences between therapeutically relevant species

Abstract Cyclic GMP-AMP synthase (cGAS) is an intracellular sensor of double-stranded DNA that triggers a pro-inflammatory response upon binding. The interest in cGAS as a drug discovery target has increased substantially over the past decade due to growing evidence linking its activation to numerou...

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Main Authors: Alexander M. Skeldon, Li Wang, Nicolas Sgarioto, Ramsay E. Beveridge, Silas Chan, Stephane Dorich, Valerie Dumais, Nadine Fradet, Samuel Gaudreault, Philippe LeGros, Daniel McKay, Ria Seliniotakis, Daniel V. Sietsema, Lingling Zhang, Marc-Olivier Boily, Jason D. Burch, Alex Caron, Lee D. Fader, Lodoe Lama, Wei Xie, Dinshaw J. Patel, Thomas Tuschl, Michael A. Crackower, Kelly A. Pike
Format: Article
Language:English
Published: Nature Portfolio 2025-03-01
Series:Communications Chemistry
Online Access:https://doi.org/10.1038/s42004-025-01481-7
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author Alexander M. Skeldon
Li Wang
Nicolas Sgarioto
Ramsay E. Beveridge
Silas Chan
Stephane Dorich
Valerie Dumais
Nadine Fradet
Samuel Gaudreault
Philippe LeGros
Daniel McKay
Ria Seliniotakis
Daniel V. Sietsema
Lingling Zhang
Marc-Olivier Boily
Jason D. Burch
Alex Caron
Lee D. Fader
Lodoe Lama
Wei Xie
Dinshaw J. Patel
Thomas Tuschl
Michael A. Crackower
Kelly A. Pike
author_facet Alexander M. Skeldon
Li Wang
Nicolas Sgarioto
Ramsay E. Beveridge
Silas Chan
Stephane Dorich
Valerie Dumais
Nadine Fradet
Samuel Gaudreault
Philippe LeGros
Daniel McKay
Ria Seliniotakis
Daniel V. Sietsema
Lingling Zhang
Marc-Olivier Boily
Jason D. Burch
Alex Caron
Lee D. Fader
Lodoe Lama
Wei Xie
Dinshaw J. Patel
Thomas Tuschl
Michael A. Crackower
Kelly A. Pike
author_sort Alexander M. Skeldon
collection DOAJ
description Abstract Cyclic GMP-AMP synthase (cGAS) is an intracellular sensor of double-stranded DNA that triggers a pro-inflammatory response upon binding. The interest in cGAS as a drug discovery target has increased substantially over the past decade due to growing evidence linking its activation to numerous peripheral and neurological diseases. Here, we report the binding mode of previously described cGAS inhibitors while also uncovering the structural basis for the interspecies potency shifts within this chemotype. A single threonine to isoleucine substitution between human and mouse cGAS drives compound activity, as demonstrated by biochemical, cellular, and in vivo studies. Finally, we utilize a structurally enabled design approach to engineer a novel chemical inhibitor with excellent potency for both human and mouse enzymes by targeting key interactions within the enzyme active site. Overall, this work provides the framework for rational optimization of cGAS inhibitors and potential preclinical translational strategies.
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spelling doaj-art-b503103e367541b0b22097529d58ce012025-08-20T03:41:46ZengNature PortfolioCommunications Chemistry2399-36692025-03-018111510.1038/s42004-025-01481-7Structural insight into the cGAS active site explains differences between therapeutically relevant speciesAlexander M. Skeldon0Li Wang1Nicolas Sgarioto2Ramsay E. Beveridge3Silas Chan4Stephane Dorich5Valerie Dumais6Nadine Fradet7Samuel Gaudreault8Philippe LeGros9Daniel McKay10Ria Seliniotakis11Daniel V. Sietsema12Lingling Zhang13Marc-Olivier Boily14Jason D. Burch15Alex Caron16Lee D. Fader17Lodoe Lama18Wei Xie19Dinshaw J. Patel20Thomas Tuschl21Michael A. Crackower22Kelly A. Pike23Ventus TherapeuticsVentus TherapeuticsVentus TherapeuticsVentus TherapeuticsVentus TherapeuticsVentus TherapeuticsVentus TherapeuticsVentus TherapeuticsVentus TherapeuticsVentus TherapeuticsVentus TherapeuticsVentus TherapeuticsVentus TherapeuticsVentus TherapeuticsVentus TherapeuticsVentus TherapeuticsVentus TherapeuticsVentus TherapeuticsLaboratory for RNA Molecular Biology, The Rockefeller UniversityStructural Biology Program, Memorial Sloan-Kettering Cancer CenterStructural Biology Program, Memorial Sloan-Kettering Cancer CenterLaboratory for RNA Molecular Biology, The Rockefeller UniversityVentus TherapeuticsVentus TherapeuticsAbstract Cyclic GMP-AMP synthase (cGAS) is an intracellular sensor of double-stranded DNA that triggers a pro-inflammatory response upon binding. The interest in cGAS as a drug discovery target has increased substantially over the past decade due to growing evidence linking its activation to numerous peripheral and neurological diseases. Here, we report the binding mode of previously described cGAS inhibitors while also uncovering the structural basis for the interspecies potency shifts within this chemotype. A single threonine to isoleucine substitution between human and mouse cGAS drives compound activity, as demonstrated by biochemical, cellular, and in vivo studies. Finally, we utilize a structurally enabled design approach to engineer a novel chemical inhibitor with excellent potency for both human and mouse enzymes by targeting key interactions within the enzyme active site. Overall, this work provides the framework for rational optimization of cGAS inhibitors and potential preclinical translational strategies.https://doi.org/10.1038/s42004-025-01481-7
spellingShingle Alexander M. Skeldon
Li Wang
Nicolas Sgarioto
Ramsay E. Beveridge
Silas Chan
Stephane Dorich
Valerie Dumais
Nadine Fradet
Samuel Gaudreault
Philippe LeGros
Daniel McKay
Ria Seliniotakis
Daniel V. Sietsema
Lingling Zhang
Marc-Olivier Boily
Jason D. Burch
Alex Caron
Lee D. Fader
Lodoe Lama
Wei Xie
Dinshaw J. Patel
Thomas Tuschl
Michael A. Crackower
Kelly A. Pike
Structural insight into the cGAS active site explains differences between therapeutically relevant species
Communications Chemistry
title Structural insight into the cGAS active site explains differences between therapeutically relevant species
title_full Structural insight into the cGAS active site explains differences between therapeutically relevant species
title_fullStr Structural insight into the cGAS active site explains differences between therapeutically relevant species
title_full_unstemmed Structural insight into the cGAS active site explains differences between therapeutically relevant species
title_short Structural insight into the cGAS active site explains differences between therapeutically relevant species
title_sort structural insight into the cgas active site explains differences between therapeutically relevant species
url https://doi.org/10.1038/s42004-025-01481-7
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