Discovery of non-retinoid compounds that suppress the pathogenic effects of misfolded rhodopsin in a mouse model of retinitis pigmentosa.

Pathogenic mutations that cause rhodopsin misfolding lead to a spectrum of currently untreatable blinding diseases collectively termed retinitis pigmentosa. Small molecules to correct rhodopsin misfolding are therefore urgently needed. In this study, we utilized virtual screening to search for drug-...

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Main Authors: Joseph T Ortega, Jacklyn M Gallagher, Andrew G McKee, Yidan Tang, Miguel Carmena-Bargueňo, Maria Azam, Zaiddodine Pashandi, Marcin Golczak, Jens Meiler, Horacio Pérez-Sánchez, Jonathan P Schlebach, Beata Jastrzebska
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2025-01-01
Series:PLoS Biology
Online Access:https://doi.org/10.1371/journal.pbio.3002932
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author Joseph T Ortega
Jacklyn M Gallagher
Andrew G McKee
Yidan Tang
Miguel Carmena-Bargueňo
Maria Azam
Zaiddodine Pashandi
Marcin Golczak
Jens Meiler
Horacio Pérez-Sánchez
Jonathan P Schlebach
Beata Jastrzebska
author_facet Joseph T Ortega
Jacklyn M Gallagher
Andrew G McKee
Yidan Tang
Miguel Carmena-Bargueňo
Maria Azam
Zaiddodine Pashandi
Marcin Golczak
Jens Meiler
Horacio Pérez-Sánchez
Jonathan P Schlebach
Beata Jastrzebska
author_sort Joseph T Ortega
collection DOAJ
description Pathogenic mutations that cause rhodopsin misfolding lead to a spectrum of currently untreatable blinding diseases collectively termed retinitis pigmentosa. Small molecules to correct rhodopsin misfolding are therefore urgently needed. In this study, we utilized virtual screening to search for drug-like molecules that bind to the orthosteric site of rod opsin and improve its folding and trafficking. We identified and validated the biological effects of 2 non-retinoid compounds with favorable pharmacological properties that cross the blood-retina barrier. These compounds reversibly bind to unliganded rod opsin, each with a Kd comparable to 9-cis-retinal and improve opsin stability. By improving the internal protein structure network (PSN), these rod opsin ligands also enhanced the plasma membrane expression of total 36 of 123 tested clinical RP variants, including the most prevalent P23H variant. Importantly, these compounds protected retinas against light-induced degeneration in mice vulnerable to bright light injury and prolonged survival of photoreceptors in a retinitis pigmentosa mouse model for rod opsin misfolding.
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spelling doaj-art-70755abceb324a2c8652eecca0be68c22025-08-20T02:28:07ZengPublic Library of Science (PLoS)PLoS Biology1544-91731545-78852025-01-01231e300293210.1371/journal.pbio.3002932Discovery of non-retinoid compounds that suppress the pathogenic effects of misfolded rhodopsin in a mouse model of retinitis pigmentosa.Joseph T OrtegaJacklyn M GallagherAndrew G McKeeYidan TangMiguel Carmena-BargueňoMaria AzamZaiddodine PashandiMarcin GolczakJens MeilerHoracio Pérez-SánchezJonathan P SchlebachBeata JastrzebskaPathogenic mutations that cause rhodopsin misfolding lead to a spectrum of currently untreatable blinding diseases collectively termed retinitis pigmentosa. Small molecules to correct rhodopsin misfolding are therefore urgently needed. In this study, we utilized virtual screening to search for drug-like molecules that bind to the orthosteric site of rod opsin and improve its folding and trafficking. We identified and validated the biological effects of 2 non-retinoid compounds with favorable pharmacological properties that cross the blood-retina barrier. These compounds reversibly bind to unliganded rod opsin, each with a Kd comparable to 9-cis-retinal and improve opsin stability. By improving the internal protein structure network (PSN), these rod opsin ligands also enhanced the plasma membrane expression of total 36 of 123 tested clinical RP variants, including the most prevalent P23H variant. Importantly, these compounds protected retinas against light-induced degeneration in mice vulnerable to bright light injury and prolonged survival of photoreceptors in a retinitis pigmentosa mouse model for rod opsin misfolding.https://doi.org/10.1371/journal.pbio.3002932
spellingShingle Joseph T Ortega
Jacklyn M Gallagher
Andrew G McKee
Yidan Tang
Miguel Carmena-Bargueňo
Maria Azam
Zaiddodine Pashandi
Marcin Golczak
Jens Meiler
Horacio Pérez-Sánchez
Jonathan P Schlebach
Beata Jastrzebska
Discovery of non-retinoid compounds that suppress the pathogenic effects of misfolded rhodopsin in a mouse model of retinitis pigmentosa.
PLoS Biology
title Discovery of non-retinoid compounds that suppress the pathogenic effects of misfolded rhodopsin in a mouse model of retinitis pigmentosa.
title_full Discovery of non-retinoid compounds that suppress the pathogenic effects of misfolded rhodopsin in a mouse model of retinitis pigmentosa.
title_fullStr Discovery of non-retinoid compounds that suppress the pathogenic effects of misfolded rhodopsin in a mouse model of retinitis pigmentosa.
title_full_unstemmed Discovery of non-retinoid compounds that suppress the pathogenic effects of misfolded rhodopsin in a mouse model of retinitis pigmentosa.
title_short Discovery of non-retinoid compounds that suppress the pathogenic effects of misfolded rhodopsin in a mouse model of retinitis pigmentosa.
title_sort discovery of non retinoid compounds that suppress the pathogenic effects of misfolded rhodopsin in a mouse model of retinitis pigmentosa
url https://doi.org/10.1371/journal.pbio.3002932
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