Perspectives on Glycosylation and Its Congenital Disorders

Trends in Genetics

Volumn 34, Issue 6, 2018, Pages 466-476

  Ng, Bobby G ^a   Freeze, Hudson H ^a  

^a BURNHAM INSTITUTE   (United States)

Author keywords

Glycosylation; next generation sequencing

Indexed keywords

CONGENITAL DISORDER OF GLYCOSYLATION; GENE IDENTIFICATION; GENE MUTATION; GENETICS; GLYCOBIOLOGY; GLYCOSYLATION; HUMAN; NEXT GENERATION SEQUENCING; PATHOGENESIS; PRIORITY JOURNAL; REVIEW; COMPLICATION; HIGH THROUGHPUT SEQUENCING; HOST PATHOGEN INTERACTION; INFECTION; LIPID METABOLISM; METABOLISM; PATHOLOGY;

CONGENITAL DISORDERS OF GLYCOSYLATION; GLYCOSYLATION; HIGH-THROUGHPUT NUCLEOTIDE SEQUENCING; HOST-PATHOGEN INTERACTIONS; HUMANS; INFECTION; LIPID METABOLISM;

EID: 85046625541     PISSN: 01689525     EISSN: 13624555     Source Type: Journal    
DOI: 10.1016/j.tig.2018.03.002     Document Type: Review

References (106)

1. Bertozzi, C.R., Rabuka, D., et al. Structural basis of glycan diversity. Varki, A., (eds.) Essentials of Glycobiology, 2009, Cold Spring Harbor Laboratory Press, 23–36.
2. Apweiler, R., et al. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim. Biophys. Acta 1473 (1999), 4–8.
3. Jaeken, J., Peanne, R., What is new in CDG?. J. Inherit. Metab. Dis. 40 (2017), 569–586.
4. Freeze, H.H., et al. Neurological aspects of human glycosylation disorders. Annu. Rev. Neurosci. 38 (2015), 105–125.
5. Peanne, R., et al. Congenital disorders of glycosylation (CDG): quo vadis?. Eur. J. Med. Genet., 2017, 10.1016/j.ejmg.2017.10.012 Published online October 25, 2017.
6. Ng, S.B., et al. Exome sequencing identifies the cause of a Mendelian disorder. Nat. Genet. 42 (2010), 30–35.
7. Vissers, L., et al. A clinical utility study of exome sequencing versus conventional genetic testing in pediatric neurology. Genet. Med. 19 (2017), 1055–1063.
8. Monroe, G.R., et al. Effectiveness of whole-exome sequencing and costs of the traditional diagnostic trajectory in children with intellectual disability. Genet. Med. 18 (2016), 949–956.
9. Krawitz, P.M., et al. Identity-by-descent filtering of exome sequence data identifies PIGV mutations in hyperphosphatasia mental retardation syndrome. Nat. Genet. 42 (2010), 827–829.
10. Freeze, H.H., et al. Solving glycosylation disorders: fundamental approaches reveal complicated pathways. Am. J. Hum. Genet. 94 (2014), 161–175.
11. Timal, S., et al. Gene identification in the congenital disorders of glycosylation type I by whole-exome sequencing. Hum. Mol. Genet. 21 (2012), 4151–4161.
12. de Ligt, J., et al. Diagnostic exome sequencing in persons with severe intellectual disability. N. Engl. J. Med. 367 (2012), 1921–1929.
13. Epi, K.C., et al. De novo mutations in epileptic encephalopathies. Nature 501 (2013), 217–221.
14. Michaud, J.L., et al. The genetic landscape of infantile spasms. Hum. Mol. Genet. 23 (2014), 4846–4858.
15. Smith-Packard, B., et al. Girls with seizures due to the c. 320A>G variant in ALG13 do not show abnormal glycosylation pattern on standard testing. JIMD Rep. 22 (2015), 95–98.
16. Dimassi, S., et al. Whole-exome sequencing improves the diagnosis yield in sporadic infantile spasm syndrome. Clin. Genet. 89 (2016), 198–204.
17. Kobayashi, Y., et al. High prevalence of genetic alterations in early-onset epileptic encephalopathies associated with infantile movement disorders. Brain Dev. 38 (2016), 285–292.
18. Ortega-Moreno, L., et al. Molecular diagnosis of patients with epilepsy and developmental delay using a customized panel of epilepsy genes. PLoS One, 12, 2017, e0188978.
19. Galama, W.H., et al. AL-CDG with Infantile Spasms in a Male Patient Due to a De Novo ALG13 Gene Mutation. JIMD Rep., 2017, 10.1007/8904_2017_53 Published online September 9, 2017.
20. Wang, X., et al. Solution structure of Alg13: the sugar donor subunit of a yeast N-acetylglucosamine transferase. Structure 16 (2008), 965–975.
21. Gao, X.D., et al. Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation. J. Biol. Chem. 280 (2005), 36254–36262.
22. Bickel, T., et al. Biosynthesis of lipid-linked oligosaccharides in Saccharomyces cerevisiae: Alg13p and Alg14p form a complex required for the formation of GlcNAc(2)-PP-dolichol. J. Biol. Chem. 280 (2005), 34500–34506.
23. Esposito, T., et al. Dysregulation of the expression of asparagine-linked glycosylation 13 short isoform 2 affects nephrin function by altering its N-linked glycosylation. Nephron 136 (2017), 143–150.
24. Bissar-Tadmouri, N., et al. X chromosome exome sequencing reveals a novel ALG13 mutation in a nonsyndromic intellectual disability family with multiple affected male siblings. Am. J. Med. Genet. A 164A (2014), 164–169.
25. Gadomski, T.E., et al. ALG13-CDG in a male with seizures, normal cognitive development, and normal transferrin isoelectric focusing. Am. J. Med. Genet. A 173 (2017), 2772–2775.
26. Ng, B.G., et al. Mosaicism of the UDP-galactose transporter SLC35A2 causes a congenital disorder of glycosylation. Am. J. Hum. Genet. 92 (2013), 632–636.
27. Kodera, H., et al. De novo mutations in SLC35A2 encoding a UDP-galactose transporter cause early-onset epileptic encephalopathy. Hum. Mutat. 34 (2013), 1708–1714.
28. Kimizu, T., et al. A case of early onset epileptic encephalopathy with de novo mutation in SLC35A2: clinical features and treatment for epilepsy. Brain Dev. 39 (2017), 256–260.
29. Olczak, M., et al. UDP-Gal/UDP-GlcNAc chimeric transporter complements mutation defect in mammalian cells deficient in UDP-Gal transporter. Biochem. Biophys. Res. Commun. 434 (2013), 473–478.
30. Ferguson, M.A.J., et al. Glycosylphosphatidylinositol anchors. Varki, A., (eds.) Essentials of Glycobiology, 2015, Cold Spring Harbor Laboratory Press, 137–150.
31. Johnston, J.J., et al. The phenotype of a germline mutation in PIGA: the gene somatically mutated in paroxysmal nocturnal hemoglobinuria. Am. J. Hum. Genet. 90 (2012), 295–300.
32. van der Crabben, S.N., et al. Expanding the spectrum of phenotypes associated with germline PIGA mutations: a child with developmental delay, accelerated linear growth, facial dysmorphisms, elevated alkaline phosphatase, and progressive CNS abnormalities. Am. J. Med. Genet. A 164A (2014), 29–35.
33. Belet, S., et al. Early frameshift mutation in PIGA identified in a large XLID family without neonatal lethality. Hum. Mutat. 35 (2014), 350–355.
34. Kato, M., et al. PIGA mutations cause early-onset epileptic encephalopathies and distinctive features. Neurology 82 (2014), 1587–1596.
35. Tarailo-Graovac, M., et al. The genotypic and phenotypic spectrum of PIGA deficiency. Orphanet J. Rare Dis., 10, 2015, 23.
36. Hamdan, F.F., et al. High rate of recurrent de novo mutations in developmental and epileptic encephalopathies. Am. J. Hum. Genet. 101 (2017), 664–685.
37. Zelinger, L., et al. A missense mutation in DHDDS, encoding dehydrodolichyl diphosphate synthase, is associated with autosomal-recessive retinitis pigmentosa in Ashkenazi Jews. Am. J. Hum. Genet. 88 (2011), 207–215.
38. Zuchner, S., et al. Whole-exome sequencing links a variant in DHDDS to retinitis pigmentosa. Am. J. Hum. Genet. 88 (2011), 201–206.
39. Sabry, S., et al. A case of fatal type I congenital disorders of glycosylation (CDG I) associated with low dehydrodolichol diphosphate synthase (DHDDS) activity. Orphanet J. Rare Dis., 11, 2016, 84.
40. Park, E.J., et al. Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation. Cell Metab. 20 (2014), 448–457.
41. Wu, X., et al. Deficiency of UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1 phosphate transferase (DPAGT1) causes a novel congenital disorder of glycosylation type Ij. Hum. Mutat. 22 (2003), 144–150.
42. Belaya, K., et al. Mutations in DPAGT1 cause a limb-girdle congenital myasthenic syndrome with tubular aggregates. Am. J. Hum. Genet. 91 (2012), 193–201.
43. Thiel, C., et al. A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis. J. Biol. Chem. 278 (2003), 22498–22505.
44. Cossins, J., et al. Congenital myasthenic syndromes due to mutations in ALG2 and ALG14. Brain 136 (2013), 944–956.
45. Schorling, D.C., et al. Early and lethal neurodegeneration with myasthenic and myopathic features: a new ALG14-CDG. Neurology 89 (2017), 657–664.
46. Doering, T.L., et al. Fungi. Varki, A., (eds.) Essentials of Glycobiology, 2015, Cold Spring Harbor Laboratory Press, 293–304.
47. Huffaker, T.C., Robbins, P.W., Temperature-sensitive yeast mutants deficient in asparagine-linked glycosylation. J. Biol. Chem. 257 (1982), 3203–3210.
48. Huffaker, T.C., Robbins, P.W., Yeast mutants deficient in protein glycosylation. Proc. Natl. Acad. Sci. U. S. A. 80 (1983), 7466–7470.
49. Stanley, P., et al. N-Glycans. Varki, A., (eds.) Essentials of Glycobiology, 2015, Cold Spring Harbor Laboratory Press, 99–111.
50. Patnaik, S.K., Stanley, P., Lectin-resistant CHO glycosylation mutants. Methods Enzymol. 416 (2006), 159–182.
51. Moreau, D., et al. Genome-wide RNAi screens identify genes required for ricin and PE intoxications. Dev. Cell 21 (2011), 231–244.
52. Elling, U., et al. Forward and reverse genetics through derivation of haploid mouse embryonic stem cells. Cell Stem Cell 9 (2011), 563–574.
53. Bassik, M.C., et al. A systematic mammalian genetic interaction map reveals pathways underlying ricin susceptibility. Cell 152 (2013), 909–922.
54. Han, K., et al. Synergistic drug combinations for cancer identified in a CRISPR screen for pairwise genetic interactions. Nat. Biotechnol. 35 (2017), 463–474.
55. Cao, W., et al. Identification of alpha-dystroglycan as a receptor for lymphocytic choriomeningitis virus and Lassa fever virus. Science 282 (1998), 2079–2081.
56. Sheikh, M.O., et al. Recent advancements in understanding mammalian O-mannosylation. Glycobiology 27 (2017), 806–819.
57. Kanagawa, M., Toda, T., Muscular dystrophy with ribitol-phosphate deficiency: a novel post-translational mechanism in dystroglycanopathy. J. Neuromuscul. Dis. 4 (2017), 259–267.
58. Godfrey, C., et al. Dystroglycanopathies: coming into focus. Curr. Opin. Genet. Dev. 21 (2011), 278–285.
59. Manya, H., Endo, T., Glycosylation with ribitol-phosphate in mammals: new insights into the O-mannosyl glycan. Biochim. Biophys. Acta 1861 (2017), 2462–2472.
60. Willer, T., et al. ISPD loss-of-function mutations disrupt dystroglycan O-mannosylation and cause Walker-Warburg syndrome. Nat. Genet. 44 (2012), 575–580.
61. Vuillaumier-Barrot, S., et al. Identification of mutations in TMEM5 and ISPD as a cause of severe cobblestone lissencephaly. Am. J. Hum. Genet. 91 (2012), 1135–1143.
62. Manzini, M.C., et al. Exome sequencing and functional validation in zebrafish identify GTDC2 mutations as a cause of Walker-Warburg syndrome. Am. J. Hum. Genet. 91 (2012), 541–547.
63. Buysse, K., et al. Missense mutations in beta-1,3-N-acetylglucosaminyltransferase 1 (B3GNT1) cause Walker-Warburg syndrome. Hum. Mol. Genet. 22 (2013), 1746–1754.
64. Jae, L.T., et al. Deciphering the glycosylome of dystroglycanopathies using haploid screens for Lassa virus entry. Science 340 (2013), 479–483.
65. Yoshida-Moriguchi, T., et al. SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function. Science 341 (2013), 896–899.
66. Praissman, J.L., et al. The functional O-mannose glycan on alpha-dystroglycan contains a phospho-ribitol primed for matriglycan addition. Elife, 5, 2016, e14473.
67. Gerin, I., et al. ISPD produces CDP-ribitol used by FKTN and FKRP to transfer ribitol phosphate onto alpha-dystroglycan. Nat. Commun., 7, 2016, 11534.
68. Riemersma, M., et al. Human ISPD is a cytidyltransferase required for dystroglycan O-mannosylation. Chem. Biol. 22 (2015), 1643–1652.
69. Marceau, C.D., et al. Genetic dissection of Flaviviridae host factors through genome-scale CRISPR screens. Nature 535 (2016), 159–163.
70. Zhang, R., et al. A CRISPR screen defines a signal peptide processing pathway required by flaviviruses. Nature 535 (2016), 164–168.
71. Pfeffer, S., et al. Dissecting the molecular organization of the translocon-associated protein complex. Nat. Commun., 8, 2017, 14516.
72. Shrimal, S., et al. Mutations in STT3A and STT3 B cause two congenital disorders of glycosylation. Hum. Mol. Genet. 22 (2013), 4638–4645.
73. 2+ revealed by human T-cell immunodeficiency. Nature 475 (2011), 471–476.
74. Losfeld, M.E., et al. A new congenital disorder of glycosylation caused by a mutation in SSR4, the signal sequence receptor 4 protein of the TRAP complex. Hum. Mol. Genet. 23 (2014), 1602–1605.
75. Ng, B.G., et al. Expanding the molecular and clinical phenotype of SSR4-CDG. Hum. Mutat. 36 (2015), 1048–1051.
76. Carette, J.E., et al. Haploid genetic screens in human cells identify host factors used by pathogens. Science 326 (2009), 1231–1235.
77. Guimaraes, C.P., et al. Identification of host cell factors required for intoxication through use of modified cholera toxin. J. Cell Biol. 195 (2011), 751–764.
78. Baggen, J., et al. Enterovirus D68 receptor requirements unveiled by haploid genetics. Proc. Natl. Acad. Sci. U. S. A. 113 (2016), 1399–1404.
79. Tanaka, A., et al. Genome-wide screening uncovers the significance of N-sulfation of heparan sulfate as a host cell factor for chikungunya virus infection. J. Virol. 91 (2017), 17–e00432.
80. Puschnik, A.S., et al. A small-molecule oligosaccharyltransferase inhibitor with pan-flaviviral activity. Cell Rep. 21 (2017), 3032–3039.
81. Niehues, R., et al. Carbohydrate-deficient glycoprotein syndrome type Ib. Phosphomannose isomerase deficiency and mannose therapy. J. Clin. Invest. 101 (1998), 1414–1420.
82. Luhn, K., et al. The gene defective in leukocyte adhesion deficiency II encodes a putative GDP-fucose transporter. Nat. Genet. 28 (2001), 69–72.
83. Lubke, T., et al. Complementation cloning identifies CDG-IIc, a new type of congenital disorders of glycosylation, as a GDP-fucose transporter deficiency. Nat. Genet. 28 (2001), 73–76.
84. van de Vijver, E., et al. Hematologically important mutations: leukocyte adhesion deficiency (first update). Blood Cells Mol. Dis. 48 (2012), 53–61.
85. Tegtmeyer, L.C., et al. Multiple phenotypes in phosphoglucomutase 1 deficiency. N. Engl. J. Med. 370 (2014), 533–542.
86. Morava, E., Galactose supplementation in phosphoglucomutase-1 deficiency; review and outlook for a novel treatable CDG. Mol. Genet. Metab. 112 (2014), 275–279.
87. Nolting, K., et al. Limitations of galactose therapy in phosphoglucomutase 1 deficiency. Mol. Genet. Metab. Rep. 13 (2017), 33–40.
88. Wong, S.Y., et al. Oral D-galactose supplementation in PGM1-CDG. Genet. Med. 19 (2017), 1226–1235.
89. Park, J.H., et al. SLC39A8 deficiency: biochemical correction and major clinical improvement by manganese therapy. Genet. Med. 20 (2017), 259–268.
90. Riley, L.G., et al. A SLC39A8 variant causes manganese deficiency, and glycosylation and mitochondrial disorders. J. Inherit. Metab. Dis. 40 (2017), 261–269.
91. Park, J.H., et al. SLC39A8 deficiency: a disorder of manganese transport and glycosylation. Am. J. Hum. Genet. 97 (2015), 894–903.
92. Koch, J., et al. CAD mutations and uridine-responsive epileptic encephalopathy. Brain 140 (2017), 279–286.
93. Altassan, R., et al. Renal involvement in PMM2-CDG, a mini-review. Mol. Genet. Metab. 123 (2017), 292–296.
94. Vals, M.A., et al. The prevalence of PMM2-CDG in Estonia based on population carrier frequencies and diagnosed patients. JIMD Rep., 2017, 10.1007/8904_2017_41 Published online July 7, 2017.
95. Matthijs, G., et al. Mutations in PMM2, a phosphomannomutase gene on chromosome 16p13, in carbohydrate-deficient glycoprotein type I syndrome (Jaeken syndrome). Nat. Genet. 16 (1997), 88–92.
96. Kjaergaard, S., et al. Failure of short-term mannose therapy of patients with carbohydrate-deficient glycoprotein syndrome type 1A. Acta Paediatr. 87 (1998), 884–888.
97. Panneerselvam, K., Freeze, H.H., Mannose corrects altered N-glycosylation in carbohydrate-deficient glycoprotein syndrome fibroblasts. J. Clin. Invest. 97 (1996), 1478–1487.
98. Yuste-Checa, P., et al. Pharmacological chaperoning: a potential treatment for PMM2-CDG. Hum. Mutat. 38 (2017), 160–168.
99. Matthijs, G., et al. Lack of homozygotes for the most frequent disease allele in carbohydrate-deficient glycoprotein syndrome type 1A. Am. J. Hum. Genet. 62 (1998), 542–550.
100. Kjaergaard, S., et al. Absence of homozygosity for predominant mutations in PMM2 in Danish patients with carbohydrate-deficient glycoprotein syndrome type 1. Eur. J. Hum. Genet. 6 (1998), 331–336.
101. Eklund, E.A., et al. Hydrophobic Man-1-P derivatives correct abnormal glycosylation in type I congenital disorder of glycosylation fibroblasts. Glycobiology 15 (2005), 1084–1093.
102. Taubenschmid, J., et al. A vital sugar code for ricin toxicity. Cell Res. 27 (2017), 1351–1364.
103. Riblett, A.M., et al. A haploid genetic screen identifies heparan sulfate proteoglycans supporting Rift Valley fever virus infection. J. Virol. 90 (2015), 1414–1423.
104. Realegeno, S., et al. Monkeypox virus host factor screen using haploid cells identifies essential role of GARP complex in extracellular virus formation. J. Virol. 91 (2017), e00011–e00017.
105. Lacey, J.M., et al. Rapid determination of transferrin isoforms by immunoaffinity liquid chromatography and electrospray mass spectrometry. Clin. Chem. 47 (2001), 513–518.
106. Jaeken, J., Matthijs, G., Congenital disorders of glycosylation: a rapidly expanding disease family. Annu. Rev. Genomics Hum. Genet. 8 (2007), 261–278.