ArticleHuman molecular genetics2013
Mutations in STT3A and STT3B cause two congenital disorders of glycosylation.
Article in Human molecular genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 83 citations in OpenAlex.
- A homozygous nonsense variant in the oligosaccharyltransferase complex gene, RPN1, causes a congenital disorder of glycosylation.HGG advances · 2026Article
- Expanded Clinical Spectrum of Autosomal-Dominant STT3A-CDG.Biomolecules · 2026Review
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- Heterozygous pathogenic STT3A variation leads to dominant congenital glycosylation disorders and functional validation in zebrafish.Orphanet journal of rare diseases · 2025Article
- Article
- N-glycosylation as a eukaryotic protective mechanism against protein aggregation.Science advances · 2024Article
- Mannose: A Promising Player in Clinical and Biomedical Applications.Current drug delivery · 2024Review
- Deciphering the Properties and Functions of Glycoproteins Using Quantitative Proteomics.Journal of proteome research · 2023Review
- DDOST-CDG: Clinical and molecular characterization of a third patient with a milder and a predominantly movement disorder phenotype.Journal of inherited metabolic disease · 2023Article
- Article
- Article
- The second DDOST-CDG patient with lactose intolerance, developmental delay, and situs inversus totalis.Journal of human genetics · 2022Article
- B7 family protein glycosylation: Promising novel targets in tumor treatment.Frontiers in immunology · 2022Review
- Active site variants in STT3A cause a dominant type I congenital disorder of glycosylation with neuromusculoskeletal findings.American journal of human genetics · 2021Article
- Genome-wide association studies identify two novel loci conferring susceptibility to diabetic retinopathy in Japanese patients with type 2 diabetes.Human molecular genetics · 2021Article
- Integrated Glycoproteomics Identifies a Role of N-Glycosylation and Galectin-1 on Myogenesis and Muscle Development.Molecular & cellular proteomics : MCP · 2021Article
- N-Glycan Biosynthesis: Basic Principles and Factors Affecting Its Outcome.Experientia supplementum (2012) · 2021Review
- Comparative and evolutionary analyses of the divergence of plant oligosaccharyltransferase STT3 isoforms.FEBS open bio · 2020Article
- Defective glycosylation and multisystem abnormalities characterize the primary immunodeficiency XMEN disease.The Journal of clinical investigation · 2020Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
We describe two unreported types of congenital disorders of glycosylation (CDG) which are caused by mutations in different isoforms of the catalytic subunit of the oligosaccharyltransferase (OST). Each isoform is encoded by a different gene (STT3A or STT3B), resides in a different OST complex and has distinct donor and acceptor substrate specificities with partially overlapping functions in N-glycosylation. The two cases from unrelated consanguineous families both show neurologic abnormalities, hypotonia, intellectual disability, failure to thrive and feeding problems. A homozygous mutation (c.1877T > C) in STT3A causes a p.Val626Ala change and a homozygous intronic mutation (c.1539 + 20G > T) in STT3B causes the other disorder. Both mutations impair glycosylation of a GFP biomarker and are rescued with the corresponding cDNA. Glycosylation of STT3A- and STT3B-specific acceptors is decreased in fibroblasts carrying the corresponding mutated gene and expression of the STT3A (p.Val626Ala) allele in STT3A-deficient HeLa cells does not rescue glycosylation. No additional cases were found in our collection or in reviewing various databases. The STT3A mutation significantly impairs glycosylation of the biomarker transferrin, but the STT3B mutation only slightly affects its glycosylation. Additional cases of STT3B-CDG may be missed by transferrin analysis and will require exome or genome sequencing.
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