Drug repurposing screen identifies lonafarnib as respiratory syncytial virus fusion protein inhibitor Article Swipe
Svenja M. Sake
,
Xiaoyu Zhang
,
Manoj Kumar Rajak
,
Melanie Urbanek‐Quaing
,
Arnaud Carpentier
,
Antonia P. Gunesch
,
Christina Grethe
,
Alina Matthaei
,
Jessica Rückert
,
Marie Galloux
,
Thibaut Larcher
,
Ronan Le Goffic
,
Fortune Hontonnou
,
Arnab K. Chatterjee
,
Kristen Johnson
,
Kaycie Morwood
,
Katharina Rox
,
Walid A. M. Elgaher
,
Jiabin Huang
,
Martin Wetzke
,
Gesine Hansen
,
Nicole Fischer
,
Jean-François Éléouët
,
Marie‐Anne Rameix‐Welti
,
Anna K. H. Hirsch
,
Elisabeth Herold
,
Martin Empting
,
Chris Lauber
,
Thomas F. Schulz
,
Thomas Krey
,
Sibylle Haid
,
Thomas Pietschmann
·
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1038/s41467-024-45241-y
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1038/s41467-024-45241-y
Respiratory syncytial virus (RSV) is a common cause of acute lower respiratory tract infection in infants, older adults and the immunocompromised. Effective directly acting antivirals are not yet available for clinical use. To address this, we screen the ReFRAME drug-repurposing library consisting of 12,000 small molecules against RSV. We identify 21 primary candidates including RSV F and N protein inhibitors, five HSP90 and four IMPDH inhibitors. We select lonafarnib, a licensed farnesyltransferase inhibitor, and phase III candidate for hepatitis delta virus (HDV) therapy, for further follow-up. Dose-response analyses and plaque assays confirm the antiviral activity (IC 50 : 10-118 nM). Passaging of RSV with lonafarnib selects for phenotypic resistance and fixation of mutations in the RSV fusion protein (T335I and T400A). Lentiviral pseudotypes programmed with variant RSV fusion proteins confirm that lonafarnib inhibits RSV cell entry and that these mutations confer lonafarnib resistance. Surface plasmon resonance reveals RSV fusion protein binding of lonafarnib and co-crystallography identifies the lonafarnib binding site within RSV F. Oral administration of lonafarnib dose-dependently reduces RSV virus load in a murine infection model using female mice. Collectively, this work provides an overview of RSV drug repurposing candidates and establishes lonafarnib as a bona fide fusion protein inhibitor.
Related Topics
Concepts
Farnesyltransferase inhibitor
Biology
Virology
Prenylation
Drug repositioning
Fusion protein
Virus
Farnesyltransferase
Drug
Pharmacology
Gene
Recombinant DNA
Genetics
Enzyme
Biochemistry
Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1038/s41467-024-45241-y
- https://www.nature.com/articles/s41467-024-45241-y.pdf
- OA Status
- gold
- Cited By
- 26
- References
- 71
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4391635207
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4391635207Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1038/s41467-024-45241-yDigital Object Identifier
- Title
-
Drug repurposing screen identifies lonafarnib as respiratory syncytial virus fusion protein inhibitorWork title
- Type
-
articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2024Year of publication
- Publication date
-
2024-02-08Full publication date if available
- Authors
-
Svenja M. Sake, Xiaoyu Zhang, Manoj Kumar Rajak, Melanie Urbanek‐Quaing, Arnaud Carpentier, Antonia P. Gunesch, Christina Grethe, Alina Matthaei, Jessica Rückert, Marie Galloux, Thibaut Larcher, Ronan Le Goffic, Fortune Hontonnou, Arnab K. Chatterjee, Kristen Johnson, Kaycie Morwood, Katharina Rox, Walid A. M. Elgaher, Jiabin Huang, Martin Wetzke, Gesine Hansen, Nicole Fischer, Jean-François Éléouët, Marie‐Anne Rameix‐Welti, Anna K. H. Hirsch, Elisabeth Herold, Martin Empting, Chris Lauber, Thomas F. Schulz, Thomas Krey, Sibylle Haid, Thomas PietschmannList of authors in order
- Landing page
-
https://doi.org/10.1038/s41467-024-45241-yPublisher landing page
- PDF URL
-
https://www.nature.com/articles/s41467-024-45241-y.pdfDirect link to full text PDF
- Open access
-
YesWhether a free full text is available
- OA status
-
goldOpen access status per OpenAlex
- OA URL
-
https://www.nature.com/articles/s41467-024-45241-y.pdfDirect OA link when available
- Concepts
-
Farnesyltransferase inhibitor, Biology, Virology, Prenylation, Drug repositioning, Fusion protein, Virus, Farnesyltransferase, Drug, Pharmacology, Gene, Recombinant DNA, Genetics, Enzyme, BiochemistryTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
26Total citation count in OpenAlex
- Citations by year (recent)
-
2025: 17, 2024: 9Per-year citation counts (last 5 years)
- References (count)
-
71Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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