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PMID: 31067009 Published · ppublish English Case Reports Journal Article Research Support, Non-U.S. Gov't Review

Novel variants and clinical symptoms in four new ALG3-CDG patients, review of the literature, and identification of AAGRP-ALG3 as a novel ALG3 variant with alanine and glycine-rich N-terminus.

Human mutation ·Vol. 40 ·No. 7 ·2019-00-00 ·Pages 938-951

Himmelreich N, Dimitrov B, Geiger V, Zielonka M, Hutter AM, Beedgen L, Hüllen A, Breuer M, Peters V, Thiemann KC, Hoffmann GF, Sinning I, Dupré T, Vuillaumier-Barrot S, Barrey C, Denecke J, Kölfen W, Düker G, Ganschow R, Lentze MJ, Moore S, Seta N, Ziegler A, Thiel C

Abstract

ALG3-CDG is one of the very rare types of congenital disorder of glycosylation (CDG) caused by variants in the ER-mannosyltransferase ALG3. Here, we summarize the clinical, biochemical, and genetic data of four new ALG3-CDG patients, who were identified by a type I pattern of serum transferrin and the accumulation of Man5 GlcNAc2 -PP-dolichol in LLO analysis. Additional clinical symptoms observed in our patients comprise sensorineural hearing loss, right-descending aorta, obstructive cardiomyopathy, macroglossia, and muscular hypertonia. We add four new biochemically confirmed variants to the list of ALG3-CDG inducing variants: c.350G>C (p.R117P), c.1263G>A (p.W421*), c.1037A>G (p.N346S), and the intron variant c.296+4A>G. Furthermore, in Patient 1 an additional open-reading frame of 141 bp (AAGRP) in the coding region of ALG3 was identified. Additionally, we show that control cells synthesize, to a minor degree, a hybrid protein composed of the polypeptide AAGRP and ALG3 (AAGRP-ALG3), while in Patient 1 expression of this hybrid protein is significantly increased due to the homozygous variant c.160_196del (g.165C>T). By reviewing the literature and combining our findings with previously published data, we further expand the knowledge of this rare glycosylation defect.

Keywords
AAGRP ALG3 CDG-I congenital disorders of glycosylation hybrid protein mannosyltransferase
MeSH Terms
Animals COS Cells Cells, Cultured Child, Preschool Chlorocebus aethiops Congenital Disorders of Glycosylation/genetics Female Humans Infant Male Mannosyltransferases/genetics Mutation Open Reading Frames Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase/deficiency,genetics Polymorphism, Single Nucleotide
Chemicals
ALG3 protein, human Mannosyltransferases Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
Authors & Affiliations
24 authors, click to expand affiliations / ORCID
Himmelreich Nastassja
Center for Child and Adolescent Medicine, Department Pediatrics I, University of Heidelberg, Heidelberg, Germany.
Dimitrov Bianca
Center for Child and Adolescent Medicine, Department Pediatrics I, University of Heidelberg, Heidelberg, Germany.
Geiger Virginia
Center for Child and Adolescent Medicine, Department Pediatrics I, University of Heidelberg, Heidelberg, Germany.
Zielonka Matthias
Center for Child and Adolescent Medicine, Department Pediatrics I, University of Heidelberg, Heidelberg, Germany.
Hutter Anna-Marlen
Center for Child and Adolescent Medicine, Department Pediatrics I, University of Heidelberg, Heidelberg, Germany.
Beedgen Lars
Center for Child and Adolescent Medicine, Department Pediatrics I, University of Heidelberg, Heidelberg, Germany.
Hüllen Andreas
Center for Child and Adolescent Medicine, Department Pediatrics I, University of Heidelberg, Heidelberg, Germany.
Breuer Maximilian
Center for Child and Adolescent Medicine, Department Pediatrics I, University of Heidelberg, Heidelberg, Germany.
Peters Verena
Center for Child and Adolescent Medicine, Department Pediatrics I, University of Heidelberg, Heidelberg, Germany.
Thiemann Kai-Christian
Center for Child and Adolescent Medicine, Department Pediatrics I, University of Heidelberg, Heidelberg, Germany.
Hoffmann Georg F
Center for Child and Adolescent Medicine, Department Pediatrics I, University of Heidelberg, Heidelberg, Germany.
Sinning Irmgard
Biochemistry Center (BZH), Heidelberg University, Heidelberg, Germany.
Dupré Thierry
Department Biochimie, AP-HP, Hôpital Bichat, Biochimie, Paris, France. | Faculté de Médecine Xavier Bichat, INSERM U1149, Université Paris Diderot, Paris, France.
Vuillaumier-Barrot Sandrine
Department Biochimie, AP-HP, Hôpital Bichat, Biochimie, Paris, France. | Faculté de Médecine Xavier Bichat, INSERM U1149, Université Paris Diderot, Paris, France.
Barrey Catherine
Pédiatrie, Hôpital Sainte Camille, Bry-sur-Marne, France.
Denecke Jonas
Department of Pediatrics, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.
Kölfen Wolfgang
Zentrum für Kinder und Jugendmedizin, Städtischen Kliniken Mönchengladbach, Mönchengladbach, Germany.
Düker Gesche
Department of Pediatrics, Children's Hospital Medical Center, University Hospitals Bonn, Bonn, Germany.
Ganschow Rainer
Department of Pediatrics, Children's Hospital Medical Center, University Hospitals Bonn, Bonn, Germany.
Lentze Michael J
Department of Pediatrics, Children's Hospital Medical Center, University Hospitals Bonn, Bonn, Germany.
Moore Stuart
Faculté de Médecine Xavier Bichat, INSERM U1149, Université Paris Diderot, Paris, France.
Seta Nathalie
Department Biochimie, AP-HP, Hôpital Bichat, Biochimie, Paris, France.
Ziegler Andreas
Center for Child and Adolescent Medicine, Department Pediatrics I, University of Heidelberg, Heidelberg, Germany.
Thiel Christian ORCID
Center for Child and Adolescent Medicine, Department Pediatrics I, University of Heidelberg, Heidelberg, Germany.
Supplementary Concepts
NGLY1 deficiency (Disease)
Article Info
Journal
Human mutation
Abbr.
Hum Mutat
ISSN
1098-1004
Published
2019-00-00
Epub
2019-00-08
Pages
938-951
Language
English
Region
United States
NLM ID
9215429
Subset
IM
Grants
Fondation Maladies Rares · High throughput sequencing and Rare Diseases Proje · International
Deutsche Forschungsgemeinschaft · FOR2509: TH1461/7-1 · International
European Union's Horizon 2020 research and innovation program · ERA-NET Cofundation N° 643578 - EURO-CDG 2/ BMB · International
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