Glycan variation and evolution in the eukaryotes

Trends in Biochemical Sciences

Volumn 40, Issue 7, 2015, Pages 351-359

  Corfield, Anthony P ^a   Berry, Monica ^a  

^a UNIVERSITY OF BRISTOL   (United Kingdom)

Author keywords

Eukaryotes; Evolution; Glycan; Glycosylation; Glycosyltransferase; Molecular mimicry

Indexed keywords

GLYCAN DERIVATIVE; GLYCOSAMINOGLYCAN; GLYCOSPHINGOLIPID; GLYCOSYLPHOSPHATIDYLINOSITOL; GLYCOSYLTRANSFERASE; N GLYCAN DERIVATIVE; O GLYCAN DERIVATIVE; OLIGOSACCHARIDE; SIALIC ACID DERIVATIVE; UNCLASSIFIED DRUG; GLYCOPROTEIN; POLYSACCHARIDE;

ADAPTATION; ARTHROPOD; CARBOHYDRATE ANALYSIS; CELL NUCLEUS; CYTOPLASM; DEUTEROSTOMIA; ENZYME SPECIFICITY; EUKARYOTE; GLYCOSYLATION; HUMAN; MOLECULAR BIOLOGY; MOLECULAR DYNAMICS; MOLECULAR EVOLUTION; NEMATODE; NONHUMAN; PRIORITY JOURNAL; REVIEW; VIRIDIPLANTAE; ANIMAL; CONFORMATION; METABOLISM; MOLECULAR GENETICS; MOLECULAR MIMICRY; PHYSIOLOGY; PROTEIN PROCESSING;

ARTHROPODA; DEUTEROSTOMIA; EUKARYOTA; FUNGI; NEMATODA; VIRIDIPLANTAE;

ANIMALS; CARBOHYDRATE CONFORMATION; CARBOHYDRATE SEQUENCE; EVOLUTION, MOLECULAR; GLYCOPROTEINS; GLYCOSYLATION; HUMANS; MOLECULAR MIMICRY; MOLECULAR SEQUENCE DATA; POLYSACCHARIDES; PROTEIN PROCESSING, POST-TRANSLATIONAL;

EID: 84930822109     PISSN: 09680004     EISSN: 13624326     Source Type: Journal    
DOI: 10.1016/j.tibs.2015.04.004     Document Type: Review

References (80)

1. Corfield A.P. Mucins: a biologically relevant glycan barrier in mucosal protection. Biochim. Biophys. Acta 2015, 1850:236-252.
2. Linden S.K., et al. Mucins in the mucosal barrier to infection. Nat. Mucosal Immunol. 2008, 1:183-197.
3. Solis D., et al. A guide into glycosciences: how chemistry, biochemistry and biology cooperate to crack the sugar code. Biochim. Biophys. Acta 2015, 1850:186-235.
4. Gabius H-J. The magic of the sugar code. Trends Biochem. Sci. 2015, 40:341.
5. Tran D.T., Ten Hagen K.G. Mucin-type O-glycosylation during development. J. Biol. Chem. 2013, 288:6921-6929.
6. Bartling B., et al. Age-associated changes of extracellular matrix collagen impair lung cancer cell migration. FASEB J. 2009, 23:1510-1520.
7. Bassaganas S., et al. Cell surface sialic acid modulates extracellular matrix adhesion and migration in pancreatic adenocarcinoma cells. Pancreas 2014, 43:109-117.
8. Styriak I., et al. Binding of extracellular matrix molecules by probiotic bacteria. Lett. Appl. Microbiol. 2003, 37:329-333.
9. Zhang L., Ten Hagen K.G. The cellular microenvironment and cell adhesion: a role for O-glycosylation. Biochem. Soc. Trans. 2011, 39:378-382.
10. Cortes P.P., et al. Sperm binding to oviductal epithelial cells in the rat: role of sialic acid residues on the epithelial surface and sialic acid-binding sites on the sperm surface. Biol. Reprod. 2004, 71:1262-1269.
11. Albenberg L.G., et al. Food and the gut microbiota in inflammatory bowel diseases: a critical connection. Curr. Opin. Gastroenterol. 2012, 28:314-320.
12. Alemka A., et al. Defense and adaptation: the complex inter-relationship between Campylobacter jejuni and mucus. Front. Cell. Infect. Microbiol. 2012, 2:15.
13. Chow J., et al. Pathobionts of the gastrointestinal microbiota and inflammatory disease. Curr. Opin. Immunol. 2011, 23:473-480.
14. Feng T., Elson C.O. Adaptive immunity in the host-microbiota dialog. Mucosal Immunol. 2011, 4:5-21.
15. Hajishengallis G., et al. The keystone-pathogen hypothesis. Nat. Rev. Microbiol. 2012, 10:717-725.
16. Hormannsperger G., et al. Gut matters: microbe-host interactions in allergic diseases. J. Allergy Clin. Immunol. 2012, 129:1452-1459.
17. Cantarel B.L., et al. The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res. 2009, 37:D233-D238.
18. Imperiali B. The chemistry-glycobiology frontier. J. Am. Chem. Soc. 2012, 134:17835-17839.
19. Gabius H.J., Kayser K. Introduction to glycopathology: the concept, the tools and the perspectives. Diagn. Pathol. 2014, 9:4.
20. Tan F., et al. Sweetening up the opposition: glycans in bacterial-host interaction. Trends Biochem. Sci. 2015, 40:342-350.
21. Hennet T., Cabalzar J. Congenital disorders of glycosylation: a concise chart of glycocalyx dysfunction. Trends Biochem. Sci. 2015, 40:377-384.
22. Peracaula R., et al. Altered glycosylation in tumours focused to cancer diagnosis. Dis. Markers 2008, 25:207-218.
23. Cummings R.D. The repertoire of glycan determinants in the human glycome. Mol. Biosyst. 2009, 5:1087-1104.
24. Ju T., et al. The Tn antigen-structural simplicity and biological complexity. Angew. Chem. Int. Ed Engl. 2011, 50:1770-1791.
25. Paulick M.G., Bertozzi C.R. The glycosylphosphatidylinositol anchor: a complex membrane-anchoring structure for proteins. Biochemistry 2008, 47:6991-7000.
26. Varki A. Evolutionary forces shaping the Golgi glycosylation machinery: why cell surface glycans are universal to living cells. Cold Spring Harb. Perspect. Biol. 2011, 3:a005462.
27. Bull C., et al. Sweet escape: sialic acids in tumor immune evasion. Biochim. Biophys. Acta 2014, 1846:238-246.
28. Aaltomaa S., et al. Strong stromal hyaluronan expression is associated with PSA recurrence in local prostate cancer. Urol. Int. 2002, 69:266-272.
29. Anttila M.A., et al. High levels of stromal hyaluronan predict poor disease outcome in epithelial ovarian cancer. Cancer Res. 2000, 60:150-155.
30. Auvinen P., et al. Hyaluronan synthases (HAS1-3) in stromal and malignant cells correlate with breast cancer grade and predict patient survival. Breast Cancer Res. Treat. 2014, 143:277-286.
31. Reuter G., Gabius H.J. Eukaryotic glycosylation: whim of nature or multipurpose tool?. Cell. Mol. Life Sci. 1999, 55:368-422.
32. Schachter H. Mgat1-dependent N-glycans are essential for the normal development of both vertebrate and invertebrate metazoans. Semin. Cell Dev. Biol. 2010, 21:609-615.
33. Tabak L.A. The role of mucin-type O-glycans in eukaryotic development. Semin. Cell Dev. Biol. 2010, 21:616-621.
34. Liu L., et al. The role of nucleotide sugar transporters in development of eukaryotes. Semin. Cell Dev. Biol. 2010, 21:600-608.
35. Dell A., et al. Similarities and differences in the glycosylation mechanisms in prokaryotes and eukaryotes. Int. J. Microbiol. 2010, 2010:148178.
36. Lauc G., et al. Glycans - the third revolution in evolution. Front. Genet. 2014, 5:145.
37. Mengerink K.J., Vacquier V.D. Glycobiology of sperm-egg interactions in deuterostomes. Glycobiology 2001, 11:37R-43R.
38. Varki A. Nothing in glycobiology makes sense, except in the light of evolution. Cell 2006, 126:841-845.
39. Freeze H.H., Elbein A.D. Glycosylation precursors. Essentials of Glycobiology 2009, 47-61. Cold Spring Harbor Laboratory Press. 2nd edn. A. Varki (Ed.).
40. Schachter H., Brockhausen I. The biosynthesis of serine (threonine)-N-acetylgalactosamine-linked carbohydrate moieties. Glycoconjugates 1992, 263-332. Marcel Dekker. H.J. Allen, E.C. Kisailus (Eds.).
41. Milewski S. Glucosamine-6-phosphate synthase: the multi-facets enzyme. Biochim. Biophys. Acta 2002, 1597:173-192.
42. Miszkiel A., et al. Long range molecular dynamics study of regulation of eukaryotic glucosamine-6-phosphate synthase activity by UDP-GlcNAc. J. Mol. Model. 2011, 17:3103-3115.
43. Keppler O.T., et al. UDP-GlcNAc 2-epimerase: a regulator of cell surface sialic acid. Science 1999, 284:1372-1376.
44. Carlin A.F., et al. Molecular mimicry of host sialylated glycans allows a bacterial pathogen to engage neutrophil Siglec-9 and dampen the innate immune response. Blood 2009, 113:3333-3336.
45. Castilho A., et al. Generation of biologically active multi-sialylated recombinant human EPOFc in plants. PLoS ONE 2013, 8:e54836.
46. Loos A., Steinkellner H. IgG-Fc glycoengineering in non-mammalian expression hosts. Arch. Biochem. Biophys. 2012, 526:167-173.
47. Piirainen M.A., et al. Glycoengineering of yeasts from the perspective of glycosylation efficiency. Nat. Biotechnol. 2014, 31:532-537.
48. Toth A.M., et al. A new insect cell glycoengineering approach provides baculovirus-inducible glycogene expression and increases human-type glycosylation efficiency. J. Biotechnol. 2014, 182-183:19-29.
49. Aebi M. N-linked protein glycosylation in the ER. Biochim. Biophys. Acta 2013, 1833:2430-2437.
50. Kelleher D.J., Gilmore R. An evolving view of the eukaryotic oligosaccharyltransferase. Glycobiology 2006, 16:47R-62R.
51. Freeze H.H., et al. Glycans in glycoprotein quality control. Essentials of Glycobiology 2009, 513-521. Cold Spring Harbor Laboratory Press. 2nd edn. A. Varki (Ed.).
52. Wilson I.B. Glycosylation of proteins in plants and invertebrates. Curr. Opin. Struct. Biol. 2002, 12:569-577.
53. Bennett E.P., et al. Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family. Glycobiology 2012, 22:736-756.
54. Patsos G., Corfield A. O-Glycosylation: structural diversity and functions. The Sugar Code. Fundamentals of Glycoscience 2009, 111-137. Wiley-VCH Verlag GmbH & Co. H.-J. Gabius (Ed.).
55. Butkinaree C., et al. O-linked beta-N-acetylglucosamine (O-GlcNAc): extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress. Biochim. Biophys. Acta 2010, 1800:96-106.
56. Ma J., Hart G.W. O-GlcNAc profiling: from proteins to proteomes. Clin. Proteomics 2014, 11:8.
57. Panin V.M., Wells L. Protein O-mannosylation in metazoan organisms. Curr. Protoc. Protein Sci. 2014, 75:12.
58. Lommel M., Strahl S. Protein O-mannosylation: conserved from bacteria to humans. Glycobiology 2009, 19:816-828.
59. Takeuchi H., Haltiwanger R.S. Significance of glycosylation in Notch signaling. Biochem. Biophys. Res. Commun. 2014, 453:235-242.
60. Freeze H.H., Haltiwanger R.S. Other classes of ER/Golgi-derived glycans. Essentials of Glycobiology 2009, 163-173. Cold Spring Harbor Laboratory Press. 2nd edn. A. Varki (Ed.).
61. Gebauer J.M., et al. O-glucosylation and O-fucosylation occur together in close proximity on the first epidermal growth factor repeat of AMACO (VWA2 protein). J. Biol. Chem. 2008, 283:17846-17854.
62. Takeuchi H., et al. Site-specific O-glucosylation of the epidermal growth factor-like (EGF) repeats of notch: efficiency of glycosylation is affected by proper folding and amino acid sequence of individual EGF repeats. J. Biol. Chem. 2012, 287:33934-33944.
63. Schegg B., et al. Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases. Mol. Cell. Biol. 2009, 29:943-952.
64. Furmanek A., Hofsteenge J. Protein C-mannosylation: facts and questions. Acta Biochim. Pol. 2000, 47:781-789.
65. Perez-Vilar J., et al. C-Mannosylation of MUC5AC and MUC5B cys subdomains. Glycobiology 2004, 14:325-337.
66. Shams-Eldin H., et al. Glycosylphosphatidylinositol anchors: structure, biosynthesis and functions. The Sugar Code 2009, 155-173. Wiley-VCH Verlag GmbH & Co. H.-J. Gabius (Ed.).
67. Varki A., Schauer R. Sialic acids. Essentials of Glycobiology 2009, 199-217. Cold Spring Harbor Laboratory Press. 2nd edn. A. Varki (Ed.).
68. Corfield A.P., Schauer R. Occurrence of sialic acids. Sialic Acids. Chemistry, Metabolism and Function 1982, 5-50. Springer-Verlag. R. Schauer (Ed.).
69. Harduin-Lepers A., et al. The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach. Glycobiology 2005, 15:805-817.
70. Schenkman S., et al. Structural and functional properties of Trypanosoma trans-sialidase. Annu. Rev. Microbiol. 1994, 48:499-523.
71. Sharon N. Lectin-carbohydrate complexes of plants and animals: an atomic view. Trends Biochem. Sci. 1993, 18:221-226.
72. Sharon N. When lectin meets oligosaccharide. Nat. Struct. Biol. 1994, 1:843-845.
73. Smits S.L., et al. Nidovirus sialate-O-acetylesterases: evolution and substrate specificity of coronaviral and toroviral receptor-destroying enzymes. J. Biol. Chem. 2005, 280:6933-6941.
74. Bertozzi C.R., Rabuka D. Structural basis of glycan diversity. Essentials of Glycobiology 2009, 23-36. Cold Spring Harbor Laboratory Press. 2nd edn. A. Varki (Ed.).
75. Cohen M., Varki A. The sialome: far more than the sum of its parts. Omics 2010, 14:455-464.
76. Gagneux P., Varki A. Evolutionary considerations in relating oligosaccharide diversity to biological function. Glycobiology 1999, 9:747-755.
77. Springer S.A., Gagneux P. Glycan evolution in response to coll-aboration, conflict, and constraint. J. Biol. Chem. 2013, 288:6904-6911.
78. Varki A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 1993, 3:97-130.
79. Adibekian A., et al. Comparative bioinformatics analysis of the mammalian and bacterial glycomes. Chem. Sci. 2011, 2:337-344.
80. Sletten E.M., Bertozzi C.R. Bioorthogonal chemistry: fishing for selectivity in a sea of functionality. Angew. Chem. Int. Ed Engl. 2009, 48:6974-6998.