Use of Endoglycosidase H as a diagnostic tool for MAN1B1-CDG patients

Sandrine Duvet; Dounia Mouajjah; Romain Péanne; Gert Matthijs; Kimiyo Raymond; Jaak Jaeken; Eva Morava; François Foulquier

doi:10.1002/elps.201800020

Use of Endoglycosidase H as a diagnostic tool for MAN1B1-CDG patients

Sandrine Duvet, Dounia Mouajjah, Romain Péanne, Gert Matthijs, Kimiyo Raymond, Jaak Jaeken, Eva Morava, François Foulquier

Medical Genetics

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

Congenital disorders of glycosylation (CDG) are heterogeneous group of genetic protein and lipid glycosylation abnormalities. With some 33 reported patients, MAN1B1-CDG belongs to the more frequent causes of CDG-II. MAN1B1 encodes an α1,2-mannosidase that removes the terminal mannose residue from the middle branch. Several methods have been proposed to characterize the glycosylation changes. In MAN1B1-CDG, the abnormal accumulating N-glycan structures are mostly absent or found in trace amounts in total human serum. To overcome this issue, in this study, we present a straightforward procedure based on the use of Endo-β-N-acetylglucosaminidase H to easily diagnose MAN1B1-CDG patients and mannosidase defects.

Original language	English (US)
Pages (from-to)	3133-3141
Number of pages	9
Journal	ELECTROPHORESIS
Volume	39
Issue number	24
DOIs	https://doi.org/10.1002/elps.201800020
State	Published - Dec 2018

Keywords

CDG
Endo-β-N-acetylglucosaminidase H
Glycomics
MAN1B1
N-Glycans

ASJC Scopus subject areas

Biochemistry
Clinical Biochemistry

Access to Document

10.1002/elps.201800020

Cite this

@article{eca3c53b425c455583528c6ccd70863e,

title = "Use of Endoglycosidase H as a diagnostic tool for MAN1B1-CDG patients",

abstract = "Congenital disorders of glycosylation (CDG) are heterogeneous group of genetic protein and lipid glycosylation abnormalities. With some 33 reported patients, MAN1B1-CDG belongs to the more frequent causes of CDG-II. MAN1B1 encodes an α1,2-mannosidase that removes the terminal mannose residue from the middle branch. Several methods have been proposed to characterize the glycosylation changes. In MAN1B1-CDG, the abnormal accumulating N-glycan structures are mostly absent or found in trace amounts in total human serum. To overcome this issue, in this study, we present a straightforward procedure based on the use of Endo-β-N-acetylglucosaminidase H to easily diagnose MAN1B1-CDG patients and mannosidase defects.",

keywords = "CDG, Endo-β-N-acetylglucosaminidase H, Glycomics, MAN1B1, N-Glycans",

author = "Sandrine Duvet and Dounia Mouajjah and Romain P{\'e}anne and Gert Matthijs and Kimiyo Raymond and Jaak Jaeken and Eva Morava and Fran{\c c}ois Foulquier",

note = "Publisher Copyright: {\textcopyright} 2018 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim",

year = "2018",

month = dec,

doi = "10.1002/elps.201800020",

language = "English (US)",

volume = "39",

pages = "3133--3141",

journal = "ELECTROPHORESIS",

issn = "0173-0835",

publisher = "Wiley-VCH Verlag",

number = "24",

}

TY - JOUR

T1 - Use of Endoglycosidase H as a diagnostic tool for MAN1B1-CDG patients

AU - Duvet, Sandrine

AU - Mouajjah, Dounia

AU - Péanne, Romain

AU - Matthijs, Gert

AU - Raymond, Kimiyo

AU - Jaeken, Jaak

AU - Morava, Eva

AU - Foulquier, François

PY - 2018/12

Y1 - 2018/12

N2 - Congenital disorders of glycosylation (CDG) are heterogeneous group of genetic protein and lipid glycosylation abnormalities. With some 33 reported patients, MAN1B1-CDG belongs to the more frequent causes of CDG-II. MAN1B1 encodes an α1,2-mannosidase that removes the terminal mannose residue from the middle branch. Several methods have been proposed to characterize the glycosylation changes. In MAN1B1-CDG, the abnormal accumulating N-glycan structures are mostly absent or found in trace amounts in total human serum. To overcome this issue, in this study, we present a straightforward procedure based on the use of Endo-β-N-acetylglucosaminidase H to easily diagnose MAN1B1-CDG patients and mannosidase defects.

AB - Congenital disorders of glycosylation (CDG) are heterogeneous group of genetic protein and lipid glycosylation abnormalities. With some 33 reported patients, MAN1B1-CDG belongs to the more frequent causes of CDG-II. MAN1B1 encodes an α1,2-mannosidase that removes the terminal mannose residue from the middle branch. Several methods have been proposed to characterize the glycosylation changes. In MAN1B1-CDG, the abnormal accumulating N-glycan structures are mostly absent or found in trace amounts in total human serum. To overcome this issue, in this study, we present a straightforward procedure based on the use of Endo-β-N-acetylglucosaminidase H to easily diagnose MAN1B1-CDG patients and mannosidase defects.

KW - CDG

KW - Endo-β-N-acetylglucosaminidase H

KW - Glycomics

KW - MAN1B1

KW - N-Glycans

UR - http://www.scopus.com/inward/record.url?scp=85052453155&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85052453155&partnerID=8YFLogxK

U2 - 10.1002/elps.201800020

DO - 10.1002/elps.201800020

M3 - Article

C2 - 29947113

AN - SCOPUS:85052453155

SN - 0173-0835

VL - 39

SP - 3133

EP - 3141

JO - ELECTROPHORESIS

JF - ELECTROPHORESIS

IS - 24

ER -

Use of Endoglycosidase H as a diagnostic tool for MAN1B1-CDG patients

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this