TY - JOUR
T1 - Impaired catabolism of free oligosaccharides due to MAN2C1 variants causes a neurodevelopmental disorder
AU - Maia, Nuno
AU - Potelle, Sven
AU - Yildirim, Hamide
AU - Duvet, Sandrine
AU - Akula, Shyam K
AU - Schulz, Celine
AU - Wiame, Elsa
AU - Gheldof, Alexander
AU - O'Kane, Katherine
AU - Lai, Abbe
AU - Sermon, Karen
AU - Proisy, Maïa
AU - Loget, Philippe
AU - Attié-Bitach, Tania
AU - Quelin, Chloé
AU - Fortuna, Ana Maria
AU - Soares, Ana Rita
AU - de Brouwer, Arjan P M
AU - Van Schaftingen, Emile
AU - Nassogne, Marie-Cécile
AU - Walsh, Christopher A
AU - Stouffs, Katrien
AU - Jorge, Paula
AU - Jansen, Anna C
AU - Foulquier, François
N1 - Funding Information:
We thank the individuals and their families for their invaluable participation in this work. A.J. and K. Stouffs acknowledge the COST-Action CA16118 ( Neuro-MIG-European Network on Brain Malformations ). P.J. acknowledges the COST-Action CA16210 ( MINDDS\u2014Maximizing Impact of Research in Neurodevelopmental Disorders ). F.F. and E.V.S. were supported by the French National Agency ( ANR-18-RAR3-0009-01 ) and the Research Foundation Flanders (FWO), respectively, under the frame of E-Rare-3, the ERA-Net for Research on Rare Diseases (ERA-NET Cofund action no. 64578 ); F.F. received funding from GLYCOLAB4CDG , an International Associated Laboratory grant from the National Centre for Scientific Research (CNRS); M.C.N. received funding from the Fund for Scientific Research (FRS/FNRS). M.C.N. is a member of Metab-ERN. S.P. was supported by a research fellowship from the Fund for Scientific Research (FNRS, Cr\u00E9dit Charg\u00E9 de Recherche); P.J., N.M., and A.M.F. are researchers at Unit for Multidisciplinary Research in Biomedicine (UMIB) and ITR\u2014Laboratory for Integrative and Translational Research in Population Health, supported by national funds through the Foundation for Science and Technology (FCT) Portugal (grant numbers UIDB/00215/2020 , UIDP/00215/2020 , and LA/P/0064/2020 , respectively); N.M. was awarded with CHUPorto grant 2016 Departamento de Ensino, Forma\u00E7\u00E3o e Investiga\u00E7\u00E3o (DEFI)\u2014CHUPorto. H.Y. is supported by a fellowship from the Research Foundation Marguerite-Marie Delacroix ; A.J. is supported by a senior clinical investigator research fellowship of the Research Foundation Flanders (FWO) and is a member of the COST-Action CA16118 Neuro-MIG.
Publisher Copyright:
© 2021
PY - 2022/2/3
Y1 - 2022/2/3
N2 - Free oligosaccharides (fOSs) are soluble oligosaccharide species generated during N-glycosylation of proteins. Although little is known about fOS metabolism, the recent identification of NGLY1 deficiency, a congenital disorder of deglycosylation (CDDG) caused by loss of function of an enzyme involved in fOS metabolism, has elicited increased interest in fOS processing. The catabolism of fOSs has been linked to the activity of a specific cytosolic mannosidase, MAN2C1, which cleaves α1,2-, α1,3-, and α1,6-mannose residues. In this study, we report the clinical, biochemical, and molecular features of six individuals, including two fetuses, with bi-allelic pathogenic variants in MAN2C1; the individuals are from four different families. These individuals exhibit dysmorphic facial features, congenital anomalies such as tongue hamartoma, variable degrees of intellectual disability, and brain anomalies including polymicrogyria, interhemispheric cysts, hypothalamic hamartoma, callosal anomalies, and hypoplasia of brainstem and cerebellar vermis. Complementation experiments with isogenic MAN2C1-KO HAP1 cells confirm the pathogenicity of three of the identified MAN2C1 variants. We further demonstrate that MAN2C1 variants lead to accumulation and delay in the processing of fOSs in proband-derived cells. These results emphasize the involvement of MAN2C1 in human neurodevelopmental disease and the importance of fOS catabolism.
AB - Free oligosaccharides (fOSs) are soluble oligosaccharide species generated during N-glycosylation of proteins. Although little is known about fOS metabolism, the recent identification of NGLY1 deficiency, a congenital disorder of deglycosylation (CDDG) caused by loss of function of an enzyme involved in fOS metabolism, has elicited increased interest in fOS processing. The catabolism of fOSs has been linked to the activity of a specific cytosolic mannosidase, MAN2C1, which cleaves α1,2-, α1,3-, and α1,6-mannose residues. In this study, we report the clinical, biochemical, and molecular features of six individuals, including two fetuses, with bi-allelic pathogenic variants in MAN2C1; the individuals are from four different families. These individuals exhibit dysmorphic facial features, congenital anomalies such as tongue hamartoma, variable degrees of intellectual disability, and brain anomalies including polymicrogyria, interhemispheric cysts, hypothalamic hamartoma, callosal anomalies, and hypoplasia of brainstem and cerebellar vermis. Complementation experiments with isogenic MAN2C1-KO HAP1 cells confirm the pathogenicity of three of the identified MAN2C1 variants. We further demonstrate that MAN2C1 variants lead to accumulation and delay in the processing of fOSs in proband-derived cells. These results emphasize the involvement of MAN2C1 in human neurodevelopmental disease and the importance of fOS catabolism.
KW - Adolescent
KW - Alleles
KW - Brain Stem/metabolism
KW - Cell Line, Tumor
KW - Central Nervous System Cysts/genetics
KW - Cerebellar Vermis/metabolism
KW - Child
KW - Child, Preschool
KW - Congenital Disorders of Glycosylation/genetics
KW - Female
KW - Fetus
KW - Glycosylation
KW - Hamartoma/genetics
KW - Humans
KW - Hypothalamus/metabolism
KW - Intellectual Disability/genetics
KW - Leukocytes/metabolism
KW - Male
KW - Mannose/metabolism
KW - Oligosaccharides/metabolism
KW - Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase/deficiency
KW - Polymicrogyria/genetics
KW - Tongue/metabolism
KW - alpha-Mannosidase/deficiency
UR - http://www.scopus.com/inward/record.url?scp=85123804254&partnerID=8YFLogxK
U2 - 10.1016/j.ajhg.2021.12.010
DO - 10.1016/j.ajhg.2021.12.010
M3 - Article
C2 - 35045343
SN - 0002-9297
VL - 109
SP - 345
EP - 360
JO - American Journal of Human Genetics
JF - American Journal of Human Genetics
IS - 2
ER -