Antisense oligonucleotide splicing modulation as a novel Cystic Fibrosis therapeutic approach for the W1282X nonsense mutation.


Journal

Journal of cystic fibrosis : official journal of the European Cystic Fibrosis Society
ISSN: 1873-5010
Titre abrégé: J Cyst Fibros
Pays: Netherlands
ID NLM: 101128966

Informations de publication

Date de publication:
07 2022
Historique:
received: 23 08 2021
revised: 14 12 2021
accepted: 14 12 2021
pubmed: 2 1 2022
medline: 28 7 2022
entrez: 1 1 2022
Statut: ppublish

Résumé

Antisense oligonucleotide- based drugs for splicing modulation were recently approved for various genetic diseases with unmet need. Here we aimed to generate skipping over exon 23 of the CFTR transcript, to eliminate the W1282X nonsense mutation and avoid RNA degradation induced by the nonsense mediated mRNA decay mechanism, allowing production of partially active CFTR proteins lacking exon 23. ∼80 ASOs were screened in 16HBEge W1282X cells. ASO candidates showing significant exon skipping were assessed for their W1282X allele selectivity and the increase of CFTR protein maturation and function. The effect of a highly potent ASO candidates was further analyzed in well differentiated primary human nasal epithelial cells, derived from a W1282X homozygous patient. ASO screening led to identification of several ASOs that significantly decrease the level of CFTR transcripts including exon 23. These ASOs resulted in significant levels of mature CFTR protein and together with modulators restore the channel function following free uptake into these cells. Importantly, a highly potent lead ASOs, efficiently delivered by free uptake, was able to increase the level of transcripts lacking exon 23 and restore the CFTR function in cells from a W1282X homozygote patient. The highly efficient exon 23 skipping induced by free uptake of the lead ASO and the resulting levels of mature CFTR protein exhibiting channel function in the presence of modulators, demonstrate the ASO therapeutic potential benefit for CF patients carrying the W1282X mutation with the objective to advance the lead candidate SPL23-2 to proof-of-concept clinical study.

Sections du résumé

BACKGROUND
Antisense oligonucleotide- based drugs for splicing modulation were recently approved for various genetic diseases with unmet need. Here we aimed to generate skipping over exon 23 of the CFTR transcript, to eliminate the W1282X nonsense mutation and avoid RNA degradation induced by the nonsense mediated mRNA decay mechanism, allowing production of partially active CFTR proteins lacking exon 23.
METHODS
∼80 ASOs were screened in 16HBEge W1282X cells. ASO candidates showing significant exon skipping were assessed for their W1282X allele selectivity and the increase of CFTR protein maturation and function. The effect of a highly potent ASO candidates was further analyzed in well differentiated primary human nasal epithelial cells, derived from a W1282X homozygous patient.
RESULTS
ASO screening led to identification of several ASOs that significantly decrease the level of CFTR transcripts including exon 23. These ASOs resulted in significant levels of mature CFTR protein and together with modulators restore the channel function following free uptake into these cells. Importantly, a highly potent lead ASOs, efficiently delivered by free uptake, was able to increase the level of transcripts lacking exon 23 and restore the CFTR function in cells from a W1282X homozygote patient.
CONCLUSION
The highly efficient exon 23 skipping induced by free uptake of the lead ASO and the resulting levels of mature CFTR protein exhibiting channel function in the presence of modulators, demonstrate the ASO therapeutic potential benefit for CF patients carrying the W1282X mutation with the objective to advance the lead candidate SPL23-2 to proof-of-concept clinical study.

Identifiants

pubmed: 34972649
pii: S1569-1993(21)02172-X
doi: 10.1016/j.jcf.2021.12.012
pii:
doi:

Substances chimiques

Codon, Nonsense 0
Oligonucleotides, Antisense 0
Cystic Fibrosis Transmembrane Conductance Regulator 126880-72-6

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

630-636

Informations de copyright

Copyright © 2021 The Author(s). Published by Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest Batsheva Kerem has equity in SpliSense and is paid for consultancy. All other authors have no financial conflict of interest.

Auteurs

Yifat S Oren (YS)

SpliSense Biohouse Labs, Hadassah Ein Kerem, Jerusalem, Israel.

Ofra Avizur-Barchad (O)

SpliSense Biohouse Labs, Hadassah Ein Kerem, Jerusalem, Israel.

Efrat Ozeri-Galai (E)

SpliSense Biohouse Labs, Hadassah Ein Kerem, Jerusalem, Israel.

Renana Elgrabli (R)

SpliSense Biohouse Labs, Hadassah Ein Kerem, Jerusalem, Israel.

Meital R Schirelman (MR)

SpliSense Biohouse Labs, Hadassah Ein Kerem, Jerusalem, Israel.

Tehilla Blinder (T)

SpliSense Biohouse Labs, Hadassah Ein Kerem, Jerusalem, Israel.

Chava D Stampfer (CD)

SpliSense Biohouse Labs, Hadassah Ein Kerem, Jerusalem, Israel.

Merav Ordan (M)

SpliSense Biohouse Labs, Hadassah Ein Kerem, Jerusalem, Israel.

Onofrio Laselva (O)

Department of Medical and Surgical Sciences, University of Foggia, Foggia, Italy; Division of Molecular Medicine, Research Institute, Hospital for Sick Children, Toronto, ON M5G 0A4, Canada.

Malena Cohen-Cymberknoh (M)

Pediatric Pulmonology Unit and CF Center, Hadassah Medical Center and Faculty of Medicine, Hebrew University of Jerusalem, Israel.

Eitan Kerem (E)

CF Center, Hadassah Hebrew University Medical Center, Jerusalem, Israel.

Christine E Bear (CE)

Division of Molecular Medicine, Research Institute, Hospital for Sick Children, Toronto, ON M5G 0A4, Canada.

Batsheva Kerem (B)

SpliSense Biohouse Labs, Hadassah Ein Kerem, Jerusalem, Israel; Department of Genetics, The Hebrew University, Jerusalem, Israel. Electronic address: batshevak@savion.huji.ac.il.

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Classifications MeSH