MAN1B1-CDG: Three new individuals and associated biochemical profiles
Congenital disorders of glycosylation (CDG) constitute an ever-growing group of genetic diseases affecting the glycosylation of proteins. CDG individuals usually present with severe multisystem disorders. MAN1B1-CDG is a CDG with nonspecific clinical symptoms such as intellectual deficiency and deve...
Main Authors: | , , , , , , , , , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Elsevier
2021-09-01
|
Series: | Molecular Genetics and Metabolism Reports |
Subjects: | |
Online Access: | http://www.sciencedirect.com/science/article/pii/S2214426921000690 |
id |
doaj-034a12e529784f2f8fecf4cbb92a51e7 |
---|---|
record_format |
Article |
spelling |
doaj-034a12e529784f2f8fecf4cbb92a51e72021-06-03T04:56:50ZengElsevierMolecular Genetics and Metabolism Reports2214-42692021-09-0128100775MAN1B1-CDG: Three new individuals and associated biochemical profilesSoraya Sakhi0Sophie Cholet1Samer Wehbi2Bertrand Isidor3Benjamin Cogne4Sandrine Vuillaumier-Barrot5Thierry Dupré6Trost Detleft7Emmanuelle Schmitt8Bruno Leheup9Céline Bonnet10François Feillet11Christine Muti12François Fenaille13Arnaud Bruneel14AP-HP, Biochimie Métabolique et Cellulaire, Hôpital Bichat-Claude Bernard, Paris, FranceUniversité Paris-Saclay, CEA, INRAE, Département Médicaments et Technologies pour la Santé (DMTS), MetaboHUB, F-91191 Gif sur Yvette, FranceService de Pédiatrie, Centre hospitalier de Versailles, Le Chesnay, FranceCentre Hospitalier Universitaire de Nantes, Service de Génétique Médicale, 44093 Nantes, France; Université de Nantes, CNRS, INSERM, l'institut du thorax, 44000 Nantes, FranceCentre Hospitalier Universitaire de Nantes, Service de Génétique Médicale, 44093 Nantes, France; Université de Nantes, CNRS, INSERM, l'institut du thorax, 44000 Nantes, FranceAP-HP, Biochimie Métabolique et Cellulaire, Hôpital Bichat-Claude Bernard, Paris, FranceAP-HP, Biochimie Métabolique et Cellulaire, Hôpital Bichat-Claude Bernard, Paris, FranceLaboratoire CERBA, 95310 Saint-Ouen l'Aumone, FranceService de Neuroradiologie Diagnostique et Thérapeutique, Centre Hospitalier Universitaire de Nancy, Nancy, FranceCentre de Référence Syndromes Malformatifs et Anomalies du Développement - Service de Génétique Clinique, Centre Hospitalier Universitaire de Nancy, F-54000 Nancy, FranceLaboratoire de Génétique, Centre Hospitalier Universitaire de Nancy, F-54000 Nancy, FranceReference Center for Inborn Errors of Metabolism, University Hospital of Nancy, F-54000 Nancy, FranceUnité de Génétique Constitutionnelle, Service de Biologie, Centre Hospitalier de Versailles, Le Chesnay, FranceUniversité Paris-Saclay, CEA, INRAE, Département Médicaments et Technologies pour la Santé (DMTS), MetaboHUB, F-91191 Gif sur Yvette, FranceAP-HP, Biochimie Métabolique et Cellulaire, Hôpital Bichat-Claude Bernard, Paris, France; INSERM UMR1193, Mécanismes cellulaires et moléculaires de l'adaptation au stress et cancérogenèse, Université Paris-Sud, Châtenay-Malabry, France; Corresponding author at: Hôpital Bichat, Biochimie Métabolique et Cellulaire, 46 rue Henri Huchard, 75018 Paris, France.Congenital disorders of glycosylation (CDG) constitute an ever-growing group of genetic diseases affecting the glycosylation of proteins. CDG individuals usually present with severe multisystem disorders. MAN1B1-CDG is a CDG with nonspecific clinical symptoms such as intellectual deficiency and developmental delay. Although up to 40 affected individuals were described so far, its final diagnosis is not straightforward using common biochemical methods due to the trace-level accumulation of defective glycan structures. In this study, we present three unreported MAN1B1-CDG individuals and propose a decision tree to reach diagnosis using a panel of techniques ranging from exome sequencing to gel electrophoresis and mass spectrometry. The occurrence of MAN1B1-CDG in patients showing unexplained intellectual disability and development delay, as well as a particular transferrin glycosylation profile, can be ascertained notably using matrix assisted laser desorption/ionization – time of flight (MALDI-TOF) mass spectrometry analysis of endo-β-acetylglucosaminidase H-released serum N-glycans. In addition to reporting new pathogenic variants and additional clinical signs such as hypersialorrhea, we highlight particular biochemical features of MAN1B1-CDG with potential glycoprotein-specific glycosylation defects.http://www.sciencedirect.com/science/article/pii/S2214426921000690CDGHypersialorrheaIntellectual disabilityMAN1B1N-glycan mass spectrometry |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Soraya Sakhi Sophie Cholet Samer Wehbi Bertrand Isidor Benjamin Cogne Sandrine Vuillaumier-Barrot Thierry Dupré Trost Detleft Emmanuelle Schmitt Bruno Leheup Céline Bonnet François Feillet Christine Muti François Fenaille Arnaud Bruneel |
spellingShingle |
Soraya Sakhi Sophie Cholet Samer Wehbi Bertrand Isidor Benjamin Cogne Sandrine Vuillaumier-Barrot Thierry Dupré Trost Detleft Emmanuelle Schmitt Bruno Leheup Céline Bonnet François Feillet Christine Muti François Fenaille Arnaud Bruneel MAN1B1-CDG: Three new individuals and associated biochemical profiles Molecular Genetics and Metabolism Reports CDG Hypersialorrhea Intellectual disability MAN1B1 N-glycan mass spectrometry |
author_facet |
Soraya Sakhi Sophie Cholet Samer Wehbi Bertrand Isidor Benjamin Cogne Sandrine Vuillaumier-Barrot Thierry Dupré Trost Detleft Emmanuelle Schmitt Bruno Leheup Céline Bonnet François Feillet Christine Muti François Fenaille Arnaud Bruneel |
author_sort |
Soraya Sakhi |
title |
MAN1B1-CDG: Three new individuals and associated biochemical profiles |
title_short |
MAN1B1-CDG: Three new individuals and associated biochemical profiles |
title_full |
MAN1B1-CDG: Three new individuals and associated biochemical profiles |
title_fullStr |
MAN1B1-CDG: Three new individuals and associated biochemical profiles |
title_full_unstemmed |
MAN1B1-CDG: Three new individuals and associated biochemical profiles |
title_sort |
man1b1-cdg: three new individuals and associated biochemical profiles |
publisher |
Elsevier |
series |
Molecular Genetics and Metabolism Reports |
issn |
2214-4269 |
publishDate |
2021-09-01 |
description |
Congenital disorders of glycosylation (CDG) constitute an ever-growing group of genetic diseases affecting the glycosylation of proteins. CDG individuals usually present with severe multisystem disorders. MAN1B1-CDG is a CDG with nonspecific clinical symptoms such as intellectual deficiency and developmental delay. Although up to 40 affected individuals were described so far, its final diagnosis is not straightforward using common biochemical methods due to the trace-level accumulation of defective glycan structures. In this study, we present three unreported MAN1B1-CDG individuals and propose a decision tree to reach diagnosis using a panel of techniques ranging from exome sequencing to gel electrophoresis and mass spectrometry. The occurrence of MAN1B1-CDG in patients showing unexplained intellectual disability and development delay, as well as a particular transferrin glycosylation profile, can be ascertained notably using matrix assisted laser desorption/ionization – time of flight (MALDI-TOF) mass spectrometry analysis of endo-β-acetylglucosaminidase H-released serum N-glycans. In addition to reporting new pathogenic variants and additional clinical signs such as hypersialorrhea, we highlight particular biochemical features of MAN1B1-CDG with potential glycoprotein-specific glycosylation defects. |
topic |
CDG Hypersialorrhea Intellectual disability MAN1B1 N-glycan mass spectrometry |
url |
http://www.sciencedirect.com/science/article/pii/S2214426921000690 |
work_keys_str_mv |
AT sorayasakhi man1b1cdgthreenewindividualsandassociatedbiochemicalprofiles AT sophiecholet man1b1cdgthreenewindividualsandassociatedbiochemicalprofiles AT samerwehbi man1b1cdgthreenewindividualsandassociatedbiochemicalprofiles AT bertrandisidor man1b1cdgthreenewindividualsandassociatedbiochemicalprofiles AT benjamincogne man1b1cdgthreenewindividualsandassociatedbiochemicalprofiles AT sandrinevuillaumierbarrot man1b1cdgthreenewindividualsandassociatedbiochemicalprofiles AT thierrydupre man1b1cdgthreenewindividualsandassociatedbiochemicalprofiles AT trostdetleft man1b1cdgthreenewindividualsandassociatedbiochemicalprofiles AT emmanuelleschmitt man1b1cdgthreenewindividualsandassociatedbiochemicalprofiles AT brunoleheup man1b1cdgthreenewindividualsandassociatedbiochemicalprofiles AT celinebonnet man1b1cdgthreenewindividualsandassociatedbiochemicalprofiles AT francoisfeillet man1b1cdgthreenewindividualsandassociatedbiochemicalprofiles AT christinemuti man1b1cdgthreenewindividualsandassociatedbiochemicalprofiles AT francoisfenaille man1b1cdgthreenewindividualsandassociatedbiochemicalprofiles AT arnaudbruneel man1b1cdgthreenewindividualsandassociatedbiochemicalprofiles |
_version_ |
1721399664063807488 |