A novel mutation in GMPPA in siblings with apparent intellectual disability, epilepsy, dysmorphism, and autonomic dysfunction.

TitleA novel mutation in GMPPA in siblings with apparent intellectual disability, epilepsy, dysmorphism, and autonomic dysfunction.
Publication TypeJournal Article
Year of Publication2017
AuthorsGold, WA, Sobreira, N, Wiame, E, Marbaix, A, Van Schaftingen, E, Franzka, P, Riley, LG, Worgan, L, Hübner, CA, Christodoulou, J, Adès, LC
JournalAm J Med Genet A
Volume173
Issue8
Pagination2246-2250
Date Published2017 Aug
ISSN1552-4833
KeywordsAbnormalities, Multiple, Child, Child, Preschool, Craniofacial Abnormalities, Epilepsy, Exome, Facies, Female, Heterozygote, Humans, Intellectual Disability, Microcephaly, Muscular Atrophy, Mutation, Missense, Nucleotidyltransferases, Pedigree, Phenotype, Seizures
Abstract

GMPPA encodes the GDP-mannose pyrophosphorylase A protein (GMPPA). The function of GMPPA is not well defined, however it is a homolog of GMPPB which catalyzes the reaction that converts mannose-1-phosphate and guanosine-5'-triphosphate to GDP-mannose. Previously, biallelic mutations in GMPPA were reported to cause a disorder characterized by achalasia, alacrima, neurological deficits, and intellectual disability. In this study, we report a female proband with achalasia, alacrima, hypohydrosis, apparent intellectual disability, seizures, microcephaly, esotropia, and craniofacial dysmorphism. Exome sequencing identified a previously unreported homozygous c.853+1G>A variant in GMPPA in the proband and her affected sister. Their unaffected parents were heterozygous, and unaffected brother homozygous wild type for this variant. Lymphoblast cells from the affected sisters showed complete loss of the GMPPA protein by Western blotting, and increased levels of GDP-mannose in lymphoblasts on high performance liquid chromatography. Based on our findings and the previous report describing patients with an overlapping phenotype, we conclude that this novel variant in GMPPA, identified by exome sequencing in the proband and her affected sister, is the genetic cause of their phenotype and may expand the known phenotype of this recently described glycosylation disorder.

DOI10.1002/ajmg.a.38292
Alternate JournalAm. J. Med. Genet. A
PubMed ID28574218
Grant ListU54 HG006542 / HG / NHGRI NIH HHS / United States