A Novel Homozygous GPAA1 Variant in a Patient with a Glycosylphosphatidylinositol Biosynthesis Defect

Glycosylphosphatidylinositol biosynthesis defect 15 is a rare autosomal recessive disorder due to biallelic loss of function of GPAA1. At the moment, less than twenty patients have been reported, usually compound heterozygous for GPAA1 variants. The main clinical features are intellectual disability...

Full description

Saved in:
Bibliographic Details
Published inGenes Vol. 14; no. 7; p. 1444
Main Authors Fontana, Paolo, Budillon, Alberto, Simeone, Domenico, Del Vecchio Blanco, Francesca, Caiazza, Martina, D'Amico, Alessandra, Lonardo, Fortunato, Nigro, Vincenzo, Limongelli, Giuseppe, Scarano, Gioacchino
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 14.07.2023
MDPI
Subjects
Appendages
Atrophy
Automation
Biosynthesis
Case Report
Cerebellum
Congenital diseases
Enzymes
Genes
Genetic testing
Genomes
Glycosylphosphatidylinositol
Hereditary diseases
Intellectual disabilities
Magnetic resonance imaging
Patients
Peptides
Proteins
Seizures
Ultrasonic imaging
United States > US
transamidase complex
cerebellar atrophy
GPAA1
hypotonia
Online AccessGet full text

Cover

More Information
Summary:Glycosylphosphatidylinositol biosynthesis defect 15 is a rare autosomal recessive disorder due to biallelic loss of function of GPAA1. At the moment, less than twenty patients have been reported, usually compound heterozygous for GPAA1 variants. The main clinical features are intellectual disability, hypotonia, seizures, and cerebellar atrophy. We describe a 4-year-old male with a novel, homozygous variant. The patient presents with typical features, such as developmental delay, hypotonia, seizures, and atypical features, such as macrocephaly, preauricular, and cheek appendages. When he was 15 months, the cerebellum was normal. When he was 33 months old, after the molecular diagnosis, magnetic resonance imaging was repeated, showing cerebellar atrophy. This case extends the clinical spectrum of the GPAA1-related disorder and helps to delineate phenotypic differences with defects of other subunits of the transamidase complex.
Bibliography:These authors contributed equally to this manuscript.
ISSN:2073-4425
2073-4425
DOI:10.3390/genes14071444