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Mannosyl-Oligosaccharide Glucosidase (Glucosidase I, MOGS)

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Handbook of Glycosyltransferases and Related Genes

Abstract

The synthesis of asparagine-linked glycoproteins in eukaryotes occurs via the transfer of dolichol-linked Glc3Man9GlcNAc2 oligosaccharide at specific Asn-X-Ser/Thr sequons via the oligosaccharyl transferase (Kornfeld and Kornfeld 1985; Waechter and Lennarz 1976). Following transfer of this oligosaccharide to the peptide, sugar residues are removed or added by specific enzymes to create a diverse population of high-mannose, hybrid, or complex-type glycans as the glycoprotein moves through the secretory pathway. The first step in the remodeling of the Glc3Man9GlcNAc2 oligosaccharide is the removal of a single α1,2-linked glucose from the nonreducing terminal end of the α1,3Man branch to produce Glc2Man9GlcNAc2 (Fig. 113.1). This initial processing step is completed by mannosyl-oligosaccharide glucosidase (MOGS), also known as α-glucosidase I, which is a member of CAZy glycosyl hydrolase family 63 (Henrissat 1991). The removal of the terminal α1,2-linked glucose in the endoplasmic reticulum is the initial step in the processing and potential remodeling of N-glycans in the secretory pathway. Following removal of the distal α1,2 glucose residue to produce Glc2Man9GlcNAc2, a second ER α-glucosidase, the hetero-dimeric α-glucosidase II, removes the two remaining glucose residues.

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References

  • Atkinson PH, Lee JT (1984) Co-translational excision of alpha-glucose and alpha-mannose in nascent vesicular stomatitis virus G protein. J Cell Biol 98:2245–2249

    Article  CAS  PubMed  Google Scholar 

  • Barker MK, Wilkinson BL, Faridmoayer A, Scaman CH, Fairbanks AJ, Rose DR (2011) Production and crystallization of processing alpha-glucosidase I: pichia pastoris expression and a two-step purification toward structural determination. Protein Expr Purif 79:96–101

    Article  CAS  PubMed  Google Scholar 

  • Bause E, Erkens R, Schweden J, Jaenicke L (1986) Purification and characterization of trimming glucosidase I from Saccharomyces cerevisiae. FEBS Lett 206:208–212

    Article  CAS  Google Scholar 

  • Bause E, Gross A, Schweden J (1991) N-methyl-N-(5-carboxypentyl)-1-deoxynojirimycin, a new affinity ligand for the purification of trimming glucosidase I. FEBS Lett 278:167–170

    Article  CAS  PubMed  Google Scholar 

  • Bause E, Schweden J, Gross A, Orthen B (1989) Purification and characterization of trimming glucosidase I from pig liver. Eur J Biochem 183:661–669

    Article  CAS  PubMed  Google Scholar 

  • Chang J, Schul W, Butters TD, Yip A, Liu B, Goh A, Lakshminarayana SB, Alonzi D, Reinkensmeier G, Pan X, Qu X, Weidner JM, Wang L, Yu W, Borune N, Kinch MA, Rayahin JE, Moriarty R, Xu X, Shi PY, Guo JT, Block TM (2011) Combination of alpha-glucosidase inhibitor and ribavirin for the treatment of dengue virus infection in vitro and in vivo. Antiviral Res 89:26–34

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  • Chen WW, Lennarz WJ (1978) Enzymatic excision of glucosyl units linked to the oligosaccharide chains of glycoproteins. J Biol Chem 253:5780–5785

    CAS  PubMed  Google Scholar 

  • De Praeter CM, Gerwig GJ, Bause E, Nuytinck LK, Vliegenthart JF, Breuer W, Kamerling JP, Espeel MF, Martin JJ, De Paepe AM, Chan NW, Dacremont GA, Van Coster RN (2000) A novel disorder caused by defective biosynthesis of N-linked oligosaccharides due to glucosidase I deficiency. Am J Hum Genet 66:1744–1756

    Article  PubMed Central  PubMed  Google Scholar 

  • Dhanawansa R, Faridmoayer A, van der Merwe G, Li YX, Scaman CH (2002) Overexpression, purification, and partial characterization of Saccharomyces cerevisiae processing alpha glucosidase I. Glycobiology 12:229–234

    Article  CAS  PubMed  Google Scholar 

  • Durantel D (2009) Celgosivir, an alpha-glucosidase I inhibitor for the potential treatment of HCV infection. Curr Opin Investig Drugs 10:860–870

    CAS  PubMed  Google Scholar 

  • Durantel D, Alotte C, Zoulim F (2007) Glucosidase inhibitors as antiviral agents for hepatitis B and C. Curr Opin Investig Drugs 8:125–129

    CAS  PubMed  Google Scholar 

  • Elbein AD (1991) Glycosidase inhibitors as antiviral and/or antitumor agents. Semin Cell Biol 2:309–317

    CAS  PubMed  Google Scholar 

  • Elbein AD, Mitchell M, Sanford BA, Fellows LE, Evans SV (1984) The pyrrolidine alkaloid, 2,5-dihydroxymethyl-3,4-dihydroxypyrrolidine, inhibits glycoprotein processing. J Biol Chem 259:12409–12413

    CAS  PubMed  Google Scholar 

  • Henrissat B (1991) A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 280(Pt 2):309–316

    CAS  PubMed  Google Scholar 

  • Herscovics A (1999) Processing glycosidases of Saccharomyces cerevisiae. Biochim Biophys Acta 1426:275–285

    Article  CAS  PubMed  Google Scholar 

  • Herscovics A, Bugge B, Jeanloz RW (1977) Glucosyltransferase activity in calf pancreas microsomes. Formation of dolichyl D[14C]glucosyl phosphate and 14C-labeled lipid-linked oligosaccharides from UDP-D-[14C]glucose. J Biol Chem 252:2271–2277

    CAS  PubMed  Google Scholar 

  • Hettkamp H, Bause E, Legler G (1982) Inhibition by nojirimycin and 1-deoxynojirimycin of microsomal glucosidases from calf liver acting on the glycoprotein oligosaccharides Glc1-3Man9GlcNAc2. Biosci Rep 2:899–906

    Article  CAS  PubMed  Google Scholar 

  • Hettkamp H, Legler G, Bause E (1984) Purification by affinity chromatography of glucosidase I, an endoplasmic reticulum hydrolase involved in the processing of asparagine-linked oligosaccharides. Eur J Biochem 142:85–90

    Article  CAS  PubMed  Google Scholar 

  • Hong Y, Sundaram S, Shin DJ, Stanley P (2004) The Lec23 Chinese hamster ovary mutant is a sensitive host for detecting mutations in alpha-glucosidase I that give rise to congenital disorder of glycosylation IIb (CDG IIb). J Biol Chem 279:49894–49901

    Article  CAS  PubMed  Google Scholar 

  • Kalz-Fuller B, Bieberich E, Bause E (1995) Cloning and expression of glucosidase I from human hippocampus. Eur J Biochem 231:344–351

    Article  CAS  PubMed  Google Scholar 

  • Karpas A, Fleet GW, Dwek RA, Petursson S, Namgoong SK, Ramsden NG, Jacob GS, Rademacher TW (1988) Aminosugar derivatives as potential anti-human immunodeficiency virus agents. Proc Natl Acad Sci USA 85:9229–9233

    Article  CAS  PubMed  Google Scholar 

  • Khan FA, Varma GM, Vijay IK (1999) Genomic organization and promoter activity of glucosidase I gene. Glycobiology 9:797–806

    Article  CAS  PubMed  Google Scholar 

  • Kornfeld R, Kornfeld S (1985) Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem 54:631–664

    Article  CAS  PubMed  Google Scholar 

  • Kurakata Y, Uechi A, Yoshida H, Kamitori S, Sakano Y, Nishikawa A, Tonozuka T (2008) Structural insights into the substrate specificity and function of Escherichia coli K12 YgjK, a glucosidase belonging to the glycoside hydrolase family 63. J Mol Biol 381:116–128

    Article  CAS  PubMed  Google Scholar 

  • Li E, Tabas I, Kornfeld S (1978) The synthesis of complex-type oligosaccharides. I. Structure of the lipid-linked oligosaccharide precursor of the complex-type oligosaccharides of the vesicular stomatitis virus G protein. J Biol Chem 253:7762–7770

    CAS  PubMed  Google Scholar 

  • Michael JM, Kornfeld S (1980) Partial purification and characterization of the glucosidases involved in the processing of asparagine-linked oligosaccharides. Arch Biochem Biophys 199:249–258

    Article  CAS  PubMed  Google Scholar 

  • Neverova I, Scaman CH, Srivastava OP, Szweda R, Vijay IK, Palcic MM (1994) A spectrophotometric assay for glucosidase I. Anal Biochem 222:190–195

    Article  CAS  PubMed  Google Scholar 

  • Palcic MM, Scaman CH, Otter A, Szpacenko A, Romaniouk A, Li YX, Vijay IK (1999) Processing alpha-glucosidase I is an inverting glycosidase. Glycoconj J 16:351–355

    Article  CAS  PubMed  Google Scholar 

  • Pan YT, Hori H, Saul R, Sanford BA, Molyneux RJ, Elbein AD (1983) Castanospermine inhibits the processing of the oligosaccharide portion of the influenza viral hemagglutinin. Biochemistry 22:3975–3984

    Article  CAS  PubMed  Google Scholar 

  • Pukazhenthi BS, Muniappa N, Vijay IK (1993) Role of sulfhydryl groups in the function of glucosidase I from mammary gland. J Biol Chem 268:6445–6452

    CAS  PubMed  Google Scholar 

  • Qu X, Pan X, Weidner J, Yu W, Alonzi D, Xu X, Butters T, Block T, Guo JT, Chang J (2011) Inhibitors of endoplasmic reticulum alpha-glucosidases potently suppress hepatitis C virus virion assembly and release. Antimicrob Agents Chemother 55:1036–1044

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  • Ray MK, Yang J, Sundaram S, Stanley P (1991) A novel glycosylation phenotype expressed by Lec23, a Chinese hamster ovary mutant deficient in alpha-glucosidase I. J Biol Chem 266:22818–22825

    CAS  PubMed  Google Scholar 

  • Romaniouk A, Vijay IK (1997) Structure-function relationships in glucosidase I: amino acids involved in binding the substrate to the enzyme. Glycobiology 7:399–404

    Article  CAS  PubMed  Google Scholar 

  • Shailubhai K, Pratta MA, Vijay IK (1987) Purification and characterization of glucosidase I involved in N-linked glycoprotein processing in bovine mammary gland. Biochem J 247:555–562

    CAS  PubMed  Google Scholar 

  • Shailubhai K, Pukazhenthi BS, Saxena ES, Varma GM, Vijay IK (1991) Glucosidase I, a transmembrane endoplasmic reticular glycoprotein with a luminal catalytic domain. J Biol Chem 266:16587–16593

    CAS  PubMed  Google Scholar 

  • Shailubhai K, Saxena ES, Balapure AK, Vijay IK (1990) Developmental regulation of glucosidase I, an enzyme involved in the processing of asparagine-linked glycoproteins in rat mammary gland. J Biol Chem 265:9701–9706

    CAS  PubMed  Google Scholar 

  • Spiro RG, Spiro MJ, Bhoyroo VD (1979) Processing of carbohydrate units of glycoproteins. Characterization of a thyroid glucosidase. J Biol Chem 254:7659–7667

    CAS  PubMed  Google Scholar 

  • Tsuruoka T, Fukuyasu H, Ishii M, Usui T, Shibahara S, Inouye S (1996) Inhibition of mouse tumor metastasis with nojirimycin-related compounds. J Antibiot (Tokyo) 49:155–161

    Article  CAS  Google Scholar 

  • Ugalde RA, Staneloni RJ, Leloir LF (1980) Microsomal glucosidases of rat liver. Partial purification and inhibition by disaccharides. Eur J Biochem 113:97–103

    Article  CAS  PubMed  Google Scholar 

  • Volker C, De Praeter CM, Hardt B, Breuer W, Kalz-Fuller B, Van Coster RN, Bause E (2002) Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb). Glycobiology 12:473–483

    Article  CAS  PubMed  Google Scholar 

  • Waechter CJ, Lennarz WJ (1976) The role of polyprenol-linked sugars in glycoprotein synthesis. Annu Rev Biochem 45:95–112

    Article  CAS  PubMed  Google Scholar 

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Correspondence to Alison V. Nairn .

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Nairn, A.V., Moremen, K.W. (2014). Mannosyl-Oligosaccharide Glucosidase (Glucosidase I, MOGS). In: Taniguchi, N., Honke, K., Fukuda, M., Narimatsu, H., Yamaguchi, Y., Angata, T. (eds) Handbook of Glycosyltransferases and Related Genes. Springer, Tokyo. https://doi.org/10.1007/978-4-431-54240-7_10

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