The glycobiology of the CD system: A dictionary for translating marker designations into glycan/lectin structure and function

Trends in Biochemical Sciences

Volumn 40, Issue 7, 2015, Pages 360-376

  Gabius, Hans Joachim ^a   Kaltner, Herbert ^a   Kopitz, Jürgen ^b   André, Sabine ^a  

^a UNIVERSITY OF MUNICH   (Germany)

^b UNIVERSITY OF HEIDELBERG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CD15 ANTIGEN; CD17 ANTIGEN; CD173 ANTIGEN; CD174 ANTIGEN; CD175 ANTIGEN; CD175S ANTIGEN; CD176 ANTIGEN; CD1D ANTIGEN; CD57 ANTIGEN; CD60 ANTIGEN; CD65 ANTIGEN; CD75 ANTIGEN; GLOBOTRIAOSYLCERAMIDE; GLYCAN; GLYCAN DERIVATIVE; LACTOSYLCERAMIDE; LECTIN; LIPID; PROTEIN DERIVATIVE; RECEPTOR; UNCLASSIFIED DRUG; LEUKOCYTE ANTIGEN; POLYSACCHARIDE;

CARBOHYDRATE ANALYSIS; CLASSIFICATION; CLUSTER OF DIFFERENTIATION SYSTEM; GLYCOBIOLOGY; HUMAN; NOMENCLATURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; REVIEW; STRUCTURE ANALYSIS; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; CONFORMATION; GLYCOSYLATION; METABOLISM; MOLECULAR GENETICS; PROTEIN PROCESSING; PROTEIN TERTIARY STRUCTURE;

ANIMALS; ANTIGENS, CD; CARBOHYDRATE CONFORMATION; CARBOHYDRATE SEQUENCE; GLYCOSYLATION; HUMANS; LECTINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; POLYSACCHARIDES; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY;

EID: 84930820197     PISSN: 09680004     EISSN: 13624326     Source Type: Journal    
DOI: 10.1016/j.tibs.2015.03.013     Document Type: Review

References (100)

1. Bernard A., et al. Leucocyte Typing I 1984, Springer-Verlag.
2. Zola H., et al. Human leucocyte differentiation antigen nomenclature: update on CD nomenclature. Report of IUIS/WHO subcommittee. J. Immunol. Methods 2003, 275:1-8.
3. Gallatin W.M., et al. A cell-surface molecule involved in organ-specific homing of lymphocytes. Nature 1983, 304:30-34.
4. Hsu-Lin S-C., et al. A platelet membrane protein expressed during platelet activation and secretion. Studies using a monoclonal antibody specific for thrombin-activated platelets. J. Biol. Chem. 1984, 259:9121-9126.
5. Pober J.S., et al. Two distinct monokines, interleukin 1 and tumor necrosis factor, each independently induce biosynthesis and transient expression of the same antigen on the surface of cultured human vascular endothelial cells. J. Immunol. 1986, 136:1680-1687.
6. Camerini D., et al. Leu-8/TQ1 is the human equivalent of the Mel-14 lymph node homing receptor. Nature 1989, 342:78-82.
7. Bevilacqua M.P. Endothelial leukocyte adhesion molecule I: an induceable receptor for neutrophils related to complement regulatory proteins and lectins. Circulation 1989, 80. II-1 (abstract).
8. The Sugar Code. Fundamentals of Glycosciences 2009, Wiley. H.-J. Gabius (Ed.).
9. Gabius H-J., et al. From lectin structure to functional glycomics: principles of the sugar code. Trends Biochem. Sci. 2011, 36:298-313.
10. Solís 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.
11. Mason D., et al. CD antigens 2002. Blood 2002, 99:3877-3880.
12. Schwartz-Albiez R. Inflammation and glycosciences. The Sugar Code. Fundamentals of Glycosciences 2009, 447-467. Wiley. H.-J. Gabius (Ed.).
13. x. Arch. Biochem. Biophys. 2004, 426:122-131.
14. Kilpatrick D.C., Green C. Lectins as blood typing reagents. Adv. Lectin Res. 1992, 5:51-94.
15. Solter D., Knowles B.B. Monoclonal antibody defining a stage-specific mouse embryonic antigen (SSEA-1). Proc. Natl. Acad. Sci. U.S.A. 1978, 75:5565-5569.
16. Fenderson B.A., et al. Glycoconjugate expression during embryogenesis and its biological significance. Bioessays 1990, 12:173-179.
17. Bucior I., et al. Carbohydrate-carbohydrate interactions. The Sugar Code. Fundamentals of Glycosciences 2009, 347-362. Wiley. H.-J. Gabius (Ed.).
18. x trisaccharide and related glycan ligands. J. Biol. Chem. 2005, 280:22993-22999.
19. Schauer R. Sialic acids and their role as biological masks. Trends Biochem. Sci. 1985, 10:357-360.
20. Reuter G., Gabius H-J. Sialic acids. Structure, analysis, metabolism, and recognition. Biol. Chem. Hoppe Seyler 1996, 377:325-342.
21. Kolter T., Sandhoff K. Sialic acids: why always α-linked?. Glycobiology 1997, 7:vii-ix.
22. Kopitz J. Glycolipids. The Sugar Code. Fundamentals of Glycosciences 2009, 177-198. Wiley. H.-J. Gabius (Ed.).
23. Ledeen R.W., Wu G. Neurobiology meets glycosciences. The Sugar Code. Fundamentals of Glycosciences 2009, 495-516. Wiley. H.-J. Gabius (Ed.).
24. Iwabuchi K., et al. Involvement of very long fatty acid-containing lactosylceramide in lactosylceramide-mediated superoxide generation and migration in neutrophils. Glycoconj. J. 2008, 25:357-374.
25. Abo T., Balch C.M. A differentiation antigen of human NK and K cells identified by a monoclonal antibody (HNK-1). J. Immunol. 1981, 127:1024-1029.
26. Chou D.K., et al. Structure of sulfated glucuronyl glycolipids in the nervous system reacting with HNK-1 antibody and some IgM paraproteins in neuropathy. J. Biol. Chem. 1986, 261:11717-11725.
27. Siebert H-C., et al. Molecular dynamics-derived conformation and intramolecular interaction analysis of the N-acetyl-9-O-acetylneuraminic acid-containing ganglioside GD1a and NMR-based analysis of its binding to a human polyclonal immunoglobulin G fraction with selectivity for O-acetylated sialic acids. Glycobiology 1996, 6:561-572.
28. Levine J.M., et al. The D1.1 antigen: a cell surface marker for germinal cells of the central nervous system. J. Neurosci. 1984, 4:820-831.
29. Cheresh D.A., et al. O-Acetylation of disialoganglioside GD3 by human melanoma cells creates a unique antigenic determinant. Science 1984, 225:844-846.
30. Varki A., et al. Developmental abnormalities in transgenic mice expressing a sialic acid-specific 9-O-acetyltransferase. Cell 1991, 65:65-74.
31. Majdic O., et al. M2, a novel myelomonocytic cell surface antigen and its distribution on leukemic cells. Int. J. Cancer 1984, 33:617-623.
32. Togayachi A., Narimatsu H. Functional analysis of β1,3-N-acetylglucosaminyltransferases and regulation of immunological function by polylactosamine. Trends Glycosci. Glycotechnol. 2012, 24:95-111.
33. Fukuda M.N., et al. Structure of a novel sialylated fucosyl lacto-N-norhexaosylceramide isolated from chronic myelogenous leukemia cells. J. Biol. Chem. 1986, 261:2376-2383.
34. Macher B.A., et al. A novel carbohydrate, differentiation antigen on fucogangliosides of human myeloid cells recognized by monoclonal antibody VIM-2. J. Biol. Chem. 1988, 263:10186-10191.
35. Siebert H-C., et al. α2,3/α2,6-Sialylation of N-glycans: non-synonymous signals with marked developmental regulation in bovine reproductive tracts. Biochimie 2006, 88:399-410.
36. Spitalnik P.F., Spitalnik S.L. The P blood group system: biochemical, serological, and clinical aspects. Transfus. Med. Rev. 1995, 9:110-122.
37. Suchanowska A., et al. A single point mutation in the gene encoding Gb3/CD77 synthase causes a rare inherited polyagglutination syndrome. J. Biol. Chem. 2012, 287:38220-38230.
38. Nudelman E., et al. A glycolipid antigen associated with Burkitt lymphoma defined by a monoclonal antibody. Science 1983, 220:509-511.
39. + hematopoietic progenitors but absent on mature lymphocytes. Glycobiology 2001, 11:677-683.
40. Kayser K., et al. Correlation of expression of binding sites for synthetic blood group A-, B-, and H-trisaccharides and for sarcolectin with survival of patients with bronchial carcinoma. Eur. J. Cancer 1994, 30A:653-657.
41. Patsos G., Corfield A. O-Glycosylation: structural diversity and function. The Sugar Code. Fundamentals of Glycosciences 2009, 111-137. Wiley. H.-J. Gabius (Ed.).
42. Moreau R., et al. Acquired hemolytic anemia with polyagglutinability of erythrocytes by a new factor present in normal blood. Bull. Mem. Soc. Med. Hop. Paris 1957, 73:569-587. (in French).
43. Berger E.G. Tn-syndrome. Biochim. Biophys. Acta 1999, 1455:255-268.
44. Hübner G. Untersuchungen über Iso-agglutination mit besonderer Berücksichtigung scheinbarer Abweichungen vom Gruppenschema. Z. Immunitätsforsch. 1926, 45:223-248. (in German).
45. Thomsen O. Ein vermehrungsfähiges Agens als Veränderer des Iso-agglutinatorischen Verhaltens der roten Blutkörperchen, eine bisher unbekannte Quelle der Fehlbestimmung. Z. Immunitätsforsch. 1927, 52:85-107. (in German).
46. Corfield T. Bacterial sialidases: roles in pathogenicity and nutrition. Glycobiology 1992, 2:509-521.
47. Ju T., et al. The Tn antigen: structural simplicity and biological complexity. Angew. Chem. Int. Ed. Engl. 2011, 50:1770-1791.
48. Wu A.M., et al. Effects of polyvalency of glycotopes and natural modifications of human blood group ABH/Lewis sugars at the Galβ1-terminated core saccharides on the binding of domain-I of recombinant tandem-repeat-type galectin-4 from rat gastrointestinal tract (G4-N). Biochimie 2004, 86:317-326.
49. Ferrer C.M., Reginato M.J. Sticking to sugars at the metastatic site: sialyltransferase ST6GalNAc-II acts as a breast cancer metastasis suppressor. Cancer Discov. 2014, 4:275-277.
50. Kuroki K., et al. Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILRα. Proc. Natl. Acad. Sci. U.S.A. 2014, 111:8877-8882.
51. Ju T., Cummings R.D. A unique molecular chaperone Cosmc required for activity of the mammalian core 1 β3-galactosyltransferase. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:16613-16618.
52. Wang Y., et al. Cosmc is an essential chaperone for correct protein O-glycosylation. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:9228-9233.
53. Krzeminski M., et al. Human galectin-3 (Mac-2 antigen): defining molecular switches of affinity to natural glycoproteins, structural and dynamic aspects of glycan binding by flexible ligand docking and putative regulatory sequences in the proximal promoter region. Biochim. Biophys. Acta 2011, 1810:150-161.
54. Christiansen M.N., et al. Cell surface protein glycosylation in cancer. Proteomics 2014, 14:525-546.
55. Gready J.N., Zelensky A.N. Routes in lectin evolution: case study on the C-type lectin-like domains. The Sugar Code. Fundamentals of Glycosciences 2009, 329-346. Wiley. H.-J. Gabius (Ed.).
56. Young D.C., Moody D.B. T-cell recognition of glycolipids presented by CD1 proteins. Glycobiology 2006, 16:103R-112R.
57. Godfrey D.I., et al. Antigen recognition by CD1d-restricted NKT T cell receptors. Semin. Immunol. 2010, 22:61-67.
58. Pellicci D.G., et al. Recognition of β-linked self glycolipids mediated by natural killer T cell antigen receptors. Nat. Immunol. 2011, 12:827-833.
59. Murphy P.V., et al. The third dimension of reading the sugar code by lectins: design of glycoclusters with cyclic scaffolds as tools with the aim to define correlations between spatial presentation and activity. Molecules 2013, 18:4026-4053.
60. Katayama Y., et al. CD44 is a physiological E-selectin ligand on neutrophils. J. Exp. Med. 2005, 201:1183-1189.
61. Brazil J.C., et al. α3/4 Fucosyltransferase 3-dependent synthesis of sialyl Lewis A on CD44 variant containing exon 6 mediates polymorphonuclear leukocyte detachment from intestinal epithelium during transepithelial migration. J. Immunol. 2013, 191:4804-4817.
62. Clark M.C., Baum L.G. T cells modulate glycans on CD43 and CD45 during development and activation, signal regulation, and survival. Ann. N. Y. Acad. Sci. 2012, 1253:58-67.
63. Xu Z., Weiss A. Negative regulation of CD45 by differential homodimerization of the alternatively spliced isoforms. Nat. Immunol. 2002, 3:764-771.
64. Earl L.A., et al. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. J. Biol. Chem. 2010, 285:2232-2244.
65. + T cells results from de novo synthesis of CD45 glycans. J. Biol. Chem. 2004, 279:36689-36697.
66. Kaltner H., Gabius H-J. A toolbox of lectins for translating the sugar code: the galectin network in phylogenesis and tumors. Histol. Histopathol. 2012, 27:397-416.
67. Smetana K., et al. Context-dependent multifunctionality of galectin-1: a challenge for defining the lectin as therapeutic target. Expert Opin. Ther. Targets 2013, 17:379-392.
68. Sperandio M. Selectins and glycosyltransferases in leukocyte rolling in vivo. FEBS J. 2006, 273:4377-4389.
69. Zarbock A., et al. Leukocyte ligands for endothelial selectins: specialized glycoconjugates that mediate rolling and signaling under flow. Blood 2011, 118:6743-6751.
70. Silvescu C.I., Sackstein R. G-CSF induces membrane expression of a myeloperoxidase glycovariant that operates as an E-selectin ligand on human myeloid cells. Proc. Natl. Acad. Sci. U.S.A. 2014, 111:10696-10701.
71. INK4a: modulator of glycomic profile and galectin-1 expression to increase susceptibility to carbohydrate-dependent induction of anoikis in pancreatic carcinoma cells. FEBS J. 2007, 274:3233-3256.
72. INK4a: downregulation of galectin-3, an endogenous competitor of the pro-anoikis effector galectin-1, in a pancreatic carcinoma model. FEBS J. 2010, 277:3552-3563.
73. INK4a: anoikis-favouring decrease in N/O-glycan/cell surface sialylation by down-regulation of enzymes in sialic acid biosynthesis in tandem in a pancreatic carcinoma model. FEBS J. 2012, 279:4062-4080.
74. Nagae M., et al. Structural change of N-glycan exposes hydrophobic surface of human transferrin. Glycobiology 2014, 24:693-702.
75. Hennet T., Cabalzar J. Congenital disorders of glycosylation: a functional chart of the glycocalyx jungle. Trends Biochem. Sci. 2015, 40:377-384.
76. van de Wouwer M., et al. Nitric oxide changes distinct aspects of the glycophenotype of human neuroblastoma NB69 cells. Nitric Oxide 2011, 24:91-101.
77. André S., et al. Rho GTPase Rac1: molecular switch within the galectin network and for N-glycan α2,6-sialylation/O-glycan core 1 sialylation in colon cancer in vitro. Folia Biol. (Praha) 2014, 60:95-107.
78. Katoh S., et al. A crucial role of sialidase Neu1 in hyaluronan receptor function of CD44 in T helper type 2-mediated airway inflammation of murine acute asthmatic model. Clin. Exp. Immunol. 2010, 161:233-241.
79. Shiozaki K., et al. Regulation of sialyl Lewis antigen expression in colon cancer cells by sialidase NEU4. J. Biol. Chem. 2011, 286:21052-21061.
80. Pshezhetsky A.V., Hinek A. Where catabolism meets signalling: neuraminidase 1 as a modulator of cell receptors. Glycoconj. J. 2011, 28:441-452.
81. Miyagi T., Yamaguchi K. Mammalian sialidases: physiological and pathological roles in cellular functions. Glycobiology 2012, 22:880-896.
82. Wang J., et al. Cross-linking of GM1 ganglioside by galectin-1 mediates regulatory T cell activity involving TRPC5 channel activation: possible role in suppressing experimental autoimmune encephalomyelitis. J. Immunol. 2009, 182:4036-4045.
83. Ledeen R.W., et al. Beyond glycoproteins as galectin counterreceptors: tumor/effector T cell growth control via ganglioside GM1. Ann. N. Y. Acad. Sci. 2012, 1253:206-221.
84. Schengrund C-L. Gangliosides: glycosphingolipids essential for normal neural development and function. Trends Biochem. Sci. 2015, 40:397-406.
85. Abad-Rodríguez J., Díez-Revuelta N. Axon glycoprotein routing in nerve polarity, function and repair. Trends Biochem. Sci. 2015, 40:385-396.
86. Ledeen R.W., Wu G. The multi-tasked life of ganglioside GM1, a true factotum of nature. Trends Biochem. Sci. 2015, 40:407-418.
87. Antonopoulos A., et al. Glycosylation of mouse and human immune cells: insights emerging from N-glycomics analyses. Biochem. Soc. Trans. 2011, 39:1334-1340.
88. Bachhawat-Sikder K., et al. Thermodynamic analyis of the binding of galactose and poly-N-acetyllactosamine derivatives to human galectin-3. FEBS Lett. 2001, 500:75-79.
89. Siebert H-C., et al. Unique conformer selection of human growth-regulatory lectin galectin-1 for ganglioside GM1 versus bacterial toxins. Biochemistry 2003, 42:14762-14773.
90. André S., et al. Substitutions in the N-glycan core as regulators of biorecognition: the case of core-fucose and bisecting GlcNAc moieties. Biochemistry 2007, 46:6984-6995.
91. André S., et al. From structural to functional glycomics: core substitutions as molecular switches for shape and lectin affinity of N-glycans. Biol. Chem. 2009, 390:557-565.
92. Zuber C., Roth J. N-Glycosylation. The Sugar Code. Fundamentals of Glycosciences 2009, 87-110. Wiley. H.-J. Gabius (Ed.).
93. Corfield A., Berry M. Current aspects of eukaryotic glycosylation. Trends Biochem. Sci. 2015, 40:351-359.
94. Joziasse D.H., et al. Branch specificity of bovine colostrum CMP-sialic acid: Galβ1-4GlcNAc-R α2-6-sialyltransferase. Sialylation of bi-, tri-, and tetraantennary oligosaccharides and glycopeptides of the N-acetyllactosamine type. J. Biol. Chem. 1987, 262:2025-2033.
95. Gallala H.D., Sandhoff K. Principles of microdomain formation in biological membranes: are there lipid-ordered domains in living cellular membranes?. Trends Glycosci. Glycotechnol. 2008, 20:277-295.
96. Kopitz J., et al. How adhesion/growth-regulatory galectins-1 and -3 attain cell specificity: case study defining their target on neuroblastoma cells (SK-N-MC) and marked affinity regulation by affecting microdomain organization of the membrane. IUBMB Life 2010, 62:624-628.
97. Ideo H., et al. Galectin-4 binds to sulfated glycosphingolipids and carcinoembryonic antigen in patches on the cell surface of human colon adenocarcinoma cells. J. Biol. Chem. 2005, 280:4730-4737.
98. Stechly L., et al. Galectin-4-regulated delivery of glycoproteins to the brush border membrane of enterocyte-like cells. Traffic 2009, 10:438-450.
99. Velasco S., et al. Neuronal galectin-4 is required for axon growth and for the organization of axonal membrane L1 delivery and clustering. J. Neurochem. 2013, 125:49-62.
100. Morelle W., et al. Glycosylation pattern of brush border-associated glycoproteins in enterocyte-like cells: involvement of complex-type N-glycans in apical trafficking. Biol. Chem. 2009, 390:529-544.