ZFN-mediated in vivo gene editing in hepatocytes leads to supraphysiologic α-Gal A activity and effective substrate reduction in Fabry mice.

Silvere Pagant, Marshall W Huston, Luciana Moreira, Lin Gan, Susan St Martin, Scott Sproul, Michael C Holmes, Kathleen Meyer, Thomas Wechsler, Robert J Desnick, Makiko Yasuda
{"title":"ZFN-mediated in vivo gene editing in hepatocytes leads to supraphysiologic α-Gal A activity and effective substrate reduction in Fabry mice.","authors":"Silvere Pagant,&nbsp;Marshall W Huston,&nbsp;Luciana Moreira,&nbsp;Lin Gan,&nbsp;Susan St Martin,&nbsp;Scott Sproul,&nbsp;Michael C Holmes,&nbsp;Kathleen Meyer,&nbsp;Thomas Wechsler,&nbsp;Robert J Desnick,&nbsp;Makiko Yasuda","doi":"10.1016/j.ymthe.2021.03.018","DOIUrl":null,"url":null,"abstract":"<p><p>Fabry disease, a lysosomal storage disorder resulting from the deficient activity of α-galactosidase A (α-Gal A), is characterized by cardiac, renal, and/or cerebrovascular disease due to progressive accumulation of the enzyme's substrates, globotriaosylceramide (Gb3) and globotriaosylsphingosine (Lyso-Gb3). We report here the preclinical evaluation of liver-targeted in vivo genome editing using zinc-finger nuclease (ZFN) technology to insert the human α-galactosidase A (hGLA) cDNA into the albumin \"safe harbor\" locus of Fabry mice, thereby generating an albumin-α-Gal A fusion protein. The mature α-Gal A protein is secreted into the circulation for subsequent mannose-6-phosphate receptor-mediated tissue uptake. Donor vector optimization studies showed that replacing the hGLA cDNA signal peptide sequence with that of human iduronate 2-sulfatase (IDS) achieved higher transgene expression. Intravenous adeno-associated virus (AAV) 2/8-mediated co-delivery of the IDS-hGLA donor and ZFNs targeting the albumin locus resulted in continuous, supraphysiological plasma and tissue α-Gal A activities, which essentially normalized Gb3 and Lyso-Gb3 levels in key tissues of pathology. Notably, this was achieved with <10% of hepatocytes being edited to express hGLA, occurring mostly via non-homologous end joining (NHEJ) rather than homology-directed repair (HDR). These studies indicate that ZFN-mediated in vivo genome editing has the potential to be an effective one-time therapy for Fabry disease.</p>","PeriodicalId":519519,"journal":{"name":"Molecular therapy : the journal of the American Society of Gene Therapy","volume":" ","pages":"3230-3242"},"PeriodicalIF":0.0000,"publicationDate":"2021-11-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.ymthe.2021.03.018","citationCount":"7","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Molecular therapy : the journal of the American Society of Gene Therapy","FirstCategoryId":"3","ListUrlMain":"https://doi.org/10.1016/j.ymthe.2021.03.018","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2021/3/26 0:00:00","PubModel":"Epub","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 7

Abstract

Fabry disease, a lysosomal storage disorder resulting from the deficient activity of α-galactosidase A (α-Gal A), is characterized by cardiac, renal, and/or cerebrovascular disease due to progressive accumulation of the enzyme's substrates, globotriaosylceramide (Gb3) and globotriaosylsphingosine (Lyso-Gb3). We report here the preclinical evaluation of liver-targeted in vivo genome editing using zinc-finger nuclease (ZFN) technology to insert the human α-galactosidase A (hGLA) cDNA into the albumin "safe harbor" locus of Fabry mice, thereby generating an albumin-α-Gal A fusion protein. The mature α-Gal A protein is secreted into the circulation for subsequent mannose-6-phosphate receptor-mediated tissue uptake. Donor vector optimization studies showed that replacing the hGLA cDNA signal peptide sequence with that of human iduronate 2-sulfatase (IDS) achieved higher transgene expression. Intravenous adeno-associated virus (AAV) 2/8-mediated co-delivery of the IDS-hGLA donor and ZFNs targeting the albumin locus resulted in continuous, supraphysiological plasma and tissue α-Gal A activities, which essentially normalized Gb3 and Lyso-Gb3 levels in key tissues of pathology. Notably, this was achieved with <10% of hepatocytes being edited to express hGLA, occurring mostly via non-homologous end joining (NHEJ) rather than homology-directed repair (HDR). These studies indicate that ZFN-mediated in vivo genome editing has the potential to be an effective one-time therapy for Fabry disease.

Abstract Image

Abstract Image

Abstract Image

zfn介导的肝细胞内基因编辑导致Fabry小鼠的超生理α-Gal A活性和有效底物减少。
法布里病是由α-半乳糖苷酶a (α-Gal a)活性不足引起的溶酶体贮积障碍,其特征是由于酶底物球三烷基神经酰胺(Gb3)和球三烷基鞘氨酸(Lyso-Gb3)的进行性积累而导致心脏、肾脏和/或脑血管疾病。我们在此报告了利用锌指核酸酶(ZFN)技术进行肝脏靶向体内基因组编辑的临床前评估,将人α-半乳糖苷酶A (hGLA) cDNA插入Fabry小鼠的白蛋白“安全港”位点,从而产生白蛋白-α-半乳糖苷A融合蛋白。成熟的α-Gal A蛋白分泌到循环中,随后甘露糖-6-磷酸受体介导的组织摄取。供体载体优化研究表明,用人iduronate 2-sulfatase (IDS)信号肽序列替代hGLA cDNA信号肽序列可获得更高的转基因表达。静脉注射腺相关病毒(AAV) 2/8介导的IDS-hGLA供体和靶向白蛋白位点的ZFNs共同递送导致持续的、超生理的血浆和组织α-Gal A活性,这基本上使关键病理组织中Gb3和Lyso-Gb3水平正常化。值得注意的是,这是通过
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信
小红书