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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...
Autores principales: | , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8182421/ https://www.ncbi.nlm.nih.gov/pubmed/34141584 http://dx.doi.org/10.1016/j.ymgmr.2021.100775 |
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author | Sakhi, Soraya Cholet, Sophie Wehbi, Samer Isidor, Bertrand Cogne, Benjamin Vuillaumier-Barrot, Sandrine Dupré, Thierry Detleft, Trost Schmitt, Emmanuelle Leheup, Bruno Bonnet, Céline Feillet, François Muti, Christine Fenaille, François Bruneel, Arnaud |
author_facet | Sakhi, Soraya Cholet, Sophie Wehbi, Samer Isidor, Bertrand Cogne, Benjamin Vuillaumier-Barrot, Sandrine Dupré, Thierry Detleft, Trost Schmitt, Emmanuelle Leheup, Bruno Bonnet, Céline Feillet, François Muti, Christine Fenaille, François Bruneel, Arnaud |
author_sort | Sakhi, Soraya |
collection | PubMed |
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. |
format | Online Article Text |
id | pubmed-8182421 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-81824212021-06-16 MAN1B1-CDG: Three new individuals and associated biochemical profiles Sakhi, Soraya Cholet, Sophie Wehbi, Samer Isidor, Bertrand Cogne, Benjamin Vuillaumier-Barrot, Sandrine Dupré, Thierry Detleft, Trost Schmitt, Emmanuelle Leheup, Bruno Bonnet, Céline Feillet, François Muti, Christine Fenaille, François Bruneel, Arnaud Mol Genet Metab Rep Research Paper 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. Elsevier 2021-06-02 /pmc/articles/PMC8182421/ /pubmed/34141584 http://dx.doi.org/10.1016/j.ymgmr.2021.100775 Text en © 2021 The Authors. Published by Elsevier Inc. https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Research Paper Sakhi, Soraya Cholet, Sophie Wehbi, Samer Isidor, Bertrand Cogne, Benjamin Vuillaumier-Barrot, Sandrine Dupré, Thierry Detleft, Trost Schmitt, Emmanuelle Leheup, Bruno Bonnet, Céline Feillet, François Muti, Christine Fenaille, François Bruneel, Arnaud MAN1B1-CDG: Three new individuals and associated biochemical profiles |
title | 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_short | MAN1B1-CDG: Three new individuals and associated biochemical profiles |
title_sort | man1b1-cdg: three new individuals and associated biochemical profiles |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8182421/ https://www.ncbi.nlm.nih.gov/pubmed/34141584 http://dx.doi.org/10.1016/j.ymgmr.2021.100775 |
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