| Literature DB >> 30668673 |
Devon L Johnstone1,2, Hilal H Al-Shekaili3,4, Maja Tarailo-Graovac3,4,5,6, Nicole I Wolf7, Autumn S Ivy8, Scott Demarest9, Yann Roussel2, Jolita Ciapaite10, Carlo W T van Roermund11, Kristin D Kernohan1, Ceres Kosuta1,2, Kevin Ban1,2, Yoko Ito1, Skye McBride1, Khalid Al-Thihli12, Rana A Abdelrahim13, Roshan Koul14, Amna Al Futaisi14, Charlotte A Haaxma15, Heather Olson16, Laufey Yr Sigurdardottir17, Georgianne L Arnold18, Erica H Gerkes19, M Boon20, M Rebecca Heiner-Fokkema21, Sandra Noble2, Marjolein Bosma10, Judith Jans10,22, David A Koolen23, Erik-Jan Kamsteeg24, Britt Drögemöller4,25, Colin J Ross4,25, Jacek Majewski26,27, Megan T Cho28, Amber Begtrup28, Wyeth W Wasserman4, Tuan Bui2, Elise Brimble29, Sara Violante30, Sander M Houten30, Ron A Wevers22,31, Martijn van Faassen21, Ido P Kema21, Nathalie Lepage1, Matthew A Lines1,32, David A Dyment1,33, Ronald J A Wanders11,22, Nanda Verhoeven-Duif10,22, Marc Ekker2, Kym M Boycott1,33, Jan M Friedman3,4, Izabella A Pena1,2, Clara D M van Karnebeek4,22,34,35.
Abstract
Biallelic pathogenic variants in PLPBP (formerly called PROSC) have recently been shown to cause a novel form of vitamin B6-dependent epilepsy, the pathophysiological basis of which is poorly understood. When left untreated, the disease can progress to status epilepticus and death in infancy. Here we present 12 previously undescribed patients and six novel pathogenic variants in PLPBP. Suspected clinical diagnoses prior to identification of PLPBP variants included mitochondrial encephalopathy (two patients), folinic acid-responsive epilepsy (one patient) and a movement disorder compatible with AADC deficiency (one patient). The encoded protein, PLPHP is believed to be crucial for B6 homeostasis. We modelled the pathogenicity of the variants and developed a clinical severity scoring system. The most severe phenotypes were associated with variants leading to loss of function of PLPBP or significantly affecting protein stability/PLP-binding. To explore the pathophysiology of this disease further, we developed the first zebrafish model of PLPHP deficiency using CRISPR/Cas9. Our model recapitulates the disease, with plpbp-/- larvae showing behavioural, biochemical, and electrophysiological signs of seizure activity by 10 days post-fertilization and early death by 16 days post-fertilization. Treatment with pyridoxine significantly improved the epileptic phenotype and extended lifespan in plpbp-/- animals. Larvae had disruptions in amino acid metabolism as well as GABA and catecholamine biosynthesis, indicating impairment of PLP-dependent enzymatic activities. Using mass spectrometry, we observed significant B6 vitamer level changes in plpbp-/- zebrafish, patient fibroblasts and PLPHP-deficient HEK293 cells. Additional studies in human cells and yeast provide the first empirical evidence that PLPHP is localized in mitochondria and may play a role in mitochondrial metabolism. These models provide new insights into disease mechanisms and can serve as a platform for drug discovery.Entities:
Keywords: zzm321990 PLPBPzzm321990 ; zzm321990 PROSCzzm321990 ; epilepsy; pyridoxine; vitamin B6-responsive epilepsy
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Year: 2019 PMID: 30668673 PMCID: PMC6391652 DOI: 10.1093/brain/awy346
Source DB: PubMed Journal: Brain ISSN: 0006-8950 Impact factor: 13.501