Emerging roles of protein mannosylation in inflammation and infection

Molecular Aspects of Medicine

Volumn 51, Issue , 2016, Pages 31-55

  Loke, Ian ^a   Kolarich, Daniel ^b   Packer, Nicolle H ^a   Thaysen Andersen, Morten ^a  

^a MACQUARIE UNIVERSITY   (Australia)

^b MAX PLANCK INSTITUTE OF COLLOIDS AND INTERFACES   (Germany)

Author keywords

C type lectin; Glycoprotein; Infection; Inflammation; Mannose; Paucimannosylation

Indexed keywords

ASPARAGINE; COLLECTIN; DECTIN 2; EPITOPE; GLYCOPROTEIN; LANGERIN; LECTIN RECEPTOR; MANNOSE BINDING LECTIN; MANNOSE RECEPTOR; LECTIN; MANNOSE;

ALLERGY; ASTHMA; AUTOIMMUNITY; BACTERIAL INFECTION; BIOSYNTHESIS; BREAST CANCER; COLORECTAL CANCER; CYSTIC FIBROSIS; HEMATOLOGIC DISEASE; HUMAN; IMMUNE RESPONSE; INFLAMMATION; LUNG ADENOCARCINOMA; MYCOBACTERIUM TUBERCULOSIS; MYCOSIS; NONHUMAN; OVARY CANCER; PANCREAS CANCER; PATHOGENESIS; PNEUMONIA; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN GLYCOSYLATION; PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW; TUBERCULOSIS; VASCULAR DISEASE; VIRUS INFECTION; ANIMAL; BIOLOGICAL MODEL; CARBOHYDRATE ANALYSIS; GLYCOSYLATION; IMMUNOLOGY; IMMUNOPATHOLOGY; MOLECULAR MODEL; NEOPLASM; PHYSIOLOGY;

ANIMALS; BACTERIAL INFECTIONS; CARBOHYDRATE SEQUENCE; GLYCOPROTEINS; GLYCOSYLATION; HUMANS; IMMUNE SYSTEM DISEASES; INFLAMMATION; LECTINS, C-TYPE; MANNOSE; MODELS, IMMUNOLOGICAL; MODELS, MOLECULAR; MYCOSES; NEOPLASMS;

EID: 84963971188     PISSN: 00982997     EISSN: 18729452     Source Type: Journal    
DOI: 10.1016/j.mam.2016.04.004     Document Type: Review

References (363)

1. Aebi, M., N-linked protein glycosylation in the ER. Biochim. Biophys. Acta 1833:11 (2013), 2430–2437, 10.1016/j.bbamcr.2013.04.001.
2. Aebi, M., Bernasconi, R., Clerc, S., Molinari, M., N-glycan structures: recognition and processing in the ER. Trends Biochem. Sci 35:2 (2010), 74–82, 10.1016/j.tibs.2009.10.001.
3. Al-Ghouleh, A., Johal, R., Sharquie, I.K., Emara, M., Harrington, H., Shakib, F., et al. The glycosylation pattern of common allergens: the recognition and uptake of Der p 1 by epithelial and dendritic cells is carbohydrate dependent. PLoS ONE, 7(3), 2012, 10.1371/journal.pone.0033929 e33929.
4. Algars, A., Irjala, H., Vaittinen, S., Huhtinen, H., Sundstrom, J., Salmi, M., et al. Type and location of tumor-infiltrating macrophages and lymphatic vessels predict survival of colorectal cancer patients. Int. J. Cancer 131:4 (2012), 864–873, 10.1002/ijc.26457.
5. Amaral, E.P., Lasunskaia, E.B., D'Imperio-Lima, M.R., Innate immunity in tuberculosis: how the sensing of mycobacteria and tissue damage modulates macrophage death. Microbes Infect, 2015, 10.1016/j.micinf.2015.09.005.
6. Amin, R., Mourcin, F., Uhel, F., Pangault, C., Ruminy, P., Dupre, L., et al. DC-SIGN expressing macrophages trigger activation of mannosylated IgM B-cell receptor in follicular lymphoma. Blood, 2015, 10.1182/blood-2015-04-640912.
7. An, H.J., Gip, P., Kim, J., Wu, S., Park, K.W., McVaugh, C.T., et al. Extensive determination of glycan heterogeneity reveals an unusual abundance of high mannose glycans in enriched plasma membranes of human embryonic stem cells. Mol. Cell. Proteomics, 11(4), 2012, 10.1074/mcp.M111.010660 M111.010660.
8. Anugraham, M., Jacob, F., Nixdorf, S., Everest-Dass, A.V., Heinzelmann-Schwarz, V., Packer, N.H., Specific glycosylation of membrane proteins in epithelial ovarian cancer cell lines: glycan structures reflect gene expression and DNA methylation status. Mol. Cell. Proteomics 13:9 (2014), 2213–2232, 10.1074/mcp.M113.037085.
9. Appelmelk, B.J., van Die, I., van Vliet, S.J., Vandenbroucke-Grauls, C.M.J.E., Geijtenbeek, T.B.H., van Kooyk, Y., Cutting edge: carbohydrate profiling identifies new pathogens that interact with dendritic cell-specific ICAM-3-grabbing nonintegrin on dendritic cells. J. Immunol 170:4 (2003), 1635–1639, 10.4049/jimmunol.170.4.1635.
10. Appelmelk, B.J., den Dunnen, J., Driessen, N.N., Ummels, R., Pak, M., Nigou, J., et al. The mannose cap of mycobacterial lipoarabinomannan does not dominate the mycobacterium-host interaction. Cell. Microbiol 10:4 (2008), 930–944, 10.1111/j.1462-5822.2007.01097.x.
11. Arnold, J.N., Wormald, M.R., Suter, D.M., Radcliffe, C.M., Harvey, D.J., Dwek, R.A., et al. Human serum IgM glycosylation: identification of glycoforms that can bind to mannan-binding lectin. J. Biol. Chem 280:32 (2005), 29080–29087, 10.1074/jbc.M504528200.
12. Azad, A.K., Rajaram, M.V.S., Metz, W.L., Cope, F.O., Blue, M.S., Vera, D.R., et al. γ-Tilmanocept, a new radiopharmaceutical tracer for cancer sentinel lymph nodes, binds to the mannose receptor (CD206). J. Immunol, 2015, 10.4049/jimmunol.1402005.
13. Balog, C.I., Stavenhagen, K., Fung, W.L., Koeleman, C.A., McDonnell, L.A., Verhoeven, A., et al. N-glycosylation of colorectal cancer tissues: a liquid chromatography and mass spectrometry-based investigation. Mol. Cell. Proteomics 11:9 (2012), 571–585, 10.1074/mcp.M111.011601.
14. Bantleon, F., Wolf, S., Seismann, H., Dam, S., Lorentzen, A., Miehe, M., et al. Human IgE is efficiently produced in glycosylated and biologically active form in lepidopteran cells. Mol. Immunol 72 (2016), 49–56, 10.1016/j.molimm.2016.02.013.
15. Barrett, N.A., Maekawa, A., Rahman, O.M., Austen, K.F., Kanaoka, Y., Dectin-2 recognition of house dust mite triggers cysteinyl leukotriene generation by dendritic cells. J. Immunol 182:2 (2009), 1119–1128, 10.4049/jimmunol.182.2.1119.
16. Behrens, A.-J., Vasiljevic, S., Pritchard, L.K., Harvey, D.J., Andev, R.S., Krumm, S.A., et al. Composition and antigenic effects of individual glycan sites of a trimeric HIV-1 envelope glycoprotein. Cell Rep, 2016, 10.1016/j.celrep.2016.02.058.
17. Biedron, R., Konopinski, M.K., Marcinkiewicz, J., Jozefowski, S., Oxidation by neutrophils-derived HOCl increases immunogenicity of proteins by converting them into ligands of several endocytic receptors involved in antigen uptake by dendritic cells and macrophages. PLoS ONE, 10(4), 2015, 10.1371/journal.pone.0123293 e0123293.
18. Blattes, E., Vercellone, A., Eutamene, H., Turrin, C.O., Theodorou, V., Majoral, J.P., et al. Mannodendrimers prevent acute lung inflammation by inhibiting neutrophil recruitment. Proc. Natl. Acad. Sci. U.S.A. 110:22 (2013), 8795–8800, 10.1073/pnas.1221708110.
19. Bloem, K., Vuist, I.M., van der Plas, A.J., Knippels, L.M., Garssen, J., Garcia-Vallejo, J.J., et al. Ligand binding and signaling of dendritic cell immunoreceptor (DCIR) is modulated by the glycosylation of the carbohydrate recognition domain. PLoS ONE, 8(6), 2013, 10.1371/journal.pone.0066266 e66266.
20. Bloem, K., Vuist, I.M., van den Berk, M., Klaver, E.J., van Die, I., Knippels, L.M., et al. DCIR interacts with ligands from both endogenous and pathogenic origin. Immunol. Lett 158:1–2 (2014), 33–41, 10.1016/j.imlet.2013.11.007.
21. Bobryshev, Y.V., Dendritic cells and their role in atherogenesis. Lab. Invest 90:7 (2010), 970–984, 10.1038/labinvest.2010.94.
22. Bonomelli, C., Doores, K.J., Dunlop, D.C., Thaney, V., Dwek, R.A., Burton, D.R., et al. The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade. PLoS ONE, 6(8), 2011, 10.1371/journal.pone.0023521 e23521.
23. Botos, I., Wlodawer, A., Proteins that bind high-mannose sugars of the HIV envelope. Prog. Biophys. Mol. Biol 88:2 (2005), 233–282, 10.1016/j.pbiomolbio.2004.05.001.
24. Bouckaert, J., Mackenzie, J., de Paz, J.L., Chipwaza, B., Choudhury, D., Zavialov, A., et al. The affinity of the FimH fimbrial adhesin is receptor-driven and quasi-independent of Escherichia coli pathotypes. Mol. Microbiol 61:6 (2006), 1556–1568, 10.1111/j.1365-2958.2006.05352.x.
25. Bouckaert, J., Li, Z., Xavier, C., Almant, M., Caveliers, V., Lahoutte, T., et al. Heptyl alpha-d-mannosides grafted on a beta-cyclodextrin core to interfere with Escherichia coli adhesion: an in vivo multivalent effect. Chemistry (Easton) 19:24 (2013), 7847–7855, 10.1002/chem.201204015.
26. Bugarcic, A., Hitchens, K., Beckhouse, A.G., Wells, C.A., Ashman, R.B., Blanchard, H., Human and mouse macrophage-inducible c-type lectin (mincle) bind candida albicans. Glycobiology 18:9 (2008), 679–685, 10.1093/glycob/cwn046.
27. Cambi, A., Figdor, C.G., Dual function of c-type lectin-like receptors in the immune system. Curr. Opin. Cell Biol 15:5 (2003), 539–546, 10.1016/j.ceb.2003.08.004.
28. Cambi, A., Netea, M.G., Mora-Montes, H.M., Gow, N.A., Hato, S.V., Lowman, D.W., et al. Dendritic cell interaction with candida albicans critically depends on n-linked mannan. J. Biol. Chem 283:29 (2008), 20590–20599, 10.1074/jbc.M709334200.
29. Campbell, E.J., Owen, C.A., The sulfate groups of chondroitin sulfate- and heparan sulfate-containing proteoglycans in neutrophil plasma membranes are novel binding sites for human leukocyte elastase and cathepsin G. J. Biol. Chem 282:19 (2007), 14645–14654, 10.1074/jbc.M608346200.
30. Campbell, E.J., Campbell, M.A., Owen, C.A., Bioactive proteinase 3 on the cell surface of human neutrophils: quantification, catalytic activity, and susceptibility to inhibition. J. Immunol 165:6 (2000), 3366–3374.
31. Chacko, B.K., Scott, D.W., Chandler, R.T., Patel, R.P., Endothelial surface n-glycans mediate monocyte adhesion and are targets for anti-inflammatory effects of peroxisome proliferator-activated receptorgamma ligands. J. Biol. Chem 286:44 (2011), 38738–38747, 10.1074/jbc.M111.247981.
32. Chatwell, L., Holla, A., Kaufer, B.B., Skerra, A., The carbohydrate recognition domain of langerin reveals high structural similarity with the one of DC-SIGN but an additional, calcium-independent sugar-binding site. Mol. Immunol 45:7 (2008), 1981–1994, 10.1016/j.molimm.2007.10.030.
33. Christiansen, M.N., Chik, J., Lee, L., Anugraham, M., Abrahams, J.L., Packer, N.H., Cell surface protein glycosylation in cancer. Proteomics 14:4–5 (2014), 525–546, 10.1002/pmic.201300387.
34. Chui, D., Oh-Eda, M., Liao, Y.F., Panneerselvam, K., Lal, A., Marek, K.W., et al. Alpha-mannosidase-II deficiency results in dyserythropoiesis and unveils an alternate pathway in oligosaccharide biosynthesis. Cell 90:1 (1997), 157–167, 10.1016/S0092-8674(00)80322-0.
35. Chui, D., Sellakumar, G., Green, R.S., Sutton-Smith, M., McQuistan, T., Marek, K.W., et al. Genetic remodeling of protein glycosylation in vivo induces autoimmune disease. Proc. Natl. Acad. Sci. U.S.A. 98:3 (2001), 1142–1147, 10.1073/pnas.98.3.1142.
36. Coelho, V., Krysov, S., Ghaemmaghami, A.M., Emara, M., Potter, K.N., Johnson, P., et al. Glycosylation of surface Ig creates a functional bridge between human follicular lymphoma and microenvironmental lectins. Proc. Natl. Acad. Sci. U.S.A. 107:43 (2010), 18587–18592, 10.1073/pnas.1009388107.
37. Cohen, M., Notable aspects of glycan-protein interactions. Biomolecules 5:3 (2015), 2056–2072, 10.3390/biom5032056.
38. Cohen, M., Varki, A., The sialome–far more than the sum of its parts. OMICS 14:4 (2010), 455–464, 10.1089/omi.2009.0148.
39. Cohen, M., Varki, A., Modulation of glycan recognition by clustered saccharide patches. Int. Rev. Cell Mol. Biol 308 (2014), 75–125, 10.1016/B978-0-12-800097-7.00003-8.
40. Coico, R., Sunshine, G., Immunology: A Short Course. sixth ed., 2009, John Wiley, New Jersey.
41. Couser, W.G., Johnson, R.J., What is myeloperoxidase doing in ANCA-associated glomerulonephritis?. Kidney Int 88:5 (2015), 938–940, 10.1038/ki.2015.259.
42. Crocker, P.R., Paulson, J.C., Varki, A., Siglecs and their roles in the immune system. Nat. Rev. Immunol 7:4 (2007), 255–266, 10.1038/nri2056.
43. Crouch, E., McDonald, B., Smith, K., Cafarella, T., Seaton, B., Head, J., Contributions of phenylalanine 335 to ligand recognition by human surfactant protein d: ring interactions with sp-d ligands. J. Biol. Chem 281:26 (2006), 18008–18014, 10.1074/jbc.M601749200.
44. Cummings, R.D., Doering, T.L., Fungi. Varki, A., Cummings, R.D., Esko, J.D., Freeze, H.H., Stanley, P., Bertozzi, C.R., et al. (eds.) Essentials of Glycobiology, second ed., 2009, Cold Spring Harbor, New York, 309–320.
45. de Leoz, M.L., Young, L.J., An, H.J., Kronewitter, S.R., Kim, J., Miyamoto, S., et al. High-mannose glycans are elevated during breast cancer progression. Mol. Cell. Proteomics, 10(1), 2011, 10.1074/mcp.M110.002717 M110 002717.
46. de Witte, L., Nabatov, A., Pion, M., Fluitsma, D., de Jong, M.A., de Gruijl, T., et al. Langerin is a natural barrier to HIV-1 transmission by langerhans cells. Nat. Med 13:3 (2007), 367–371, 10.1038/nm1541.
47. Dahmen, A.C., Fergen, M.T., Laurini, C., Schmitz, B., Loke, I., Thaysen-Andersen, M., et al. Paucimannosidic glycoepitopes are functionally involved in proliferation of neural progenitor cells in the subventricular zone. Glycobiology 25:8 (2015), 869–880, 10.1093/glycob/cwv027.
48. Dam, S., Thaysen-Andersen, M., Stenkjaer, E., Lorentzen, A., Roepstorff, P., Packer, N.H., et al. Combined n-glycome and n-glycoproteome analysis of the lotus japonicus seed globulin fraction shows conservation of protein structure and glycosylation in legumes. J. Proteome Res 12:7 (2013), 3383–3392, 10.1021/pr400224s.
49. Dam, T.K., Brewer, C.F., Lectins as pattern recognition molecules: the effects of epitope density in innate immunity. Glycobiology 20:3 (2010), 270–279, 10.1093/glycob/cwp186.
50. Dasgupta, S., Navarrete, A.M., Bayry, J., Delignat, S., Wootla, B., Andre, S., et al. A role for exposed mannosylations in presentation of human therapeutic self-proteins to CD4+ T lymphocytes. Proc. Natl. Acad. Sci. U.S.A. 104:21 (2007), 8965–8970, 10.1073/pnas.0702120104.
51. Davies, J.C., Pseudomonas aeruginosa in cystic fibrosis: pathogenesis and persistence. Paediatr. Respir. Rev 3:2 (2002), 128–134, 10.1016/S1526-0550(02)00003-3.
52. Day, C.J., Tran, E.N., Semchenko, E.A., Tram, G., Hartley-Tassell, L.E., Ng, P.S., et al. Glycan:glycan interactions: high affinity biomolecular interactions that can mediate binding of pathogenic bacteria to host cells. Proc. Natl. Acad. Sci. U.S.A., 2015, 10.1073/pnas.1421082112.
53. Degn, S.E., Thiel, S., Humoral pattern recognition and the complement system. Scand. J. Immunol 78:2 (2013), 181–193, 10.1111/sji.12070.
54. Deslée, G., Charbonnier, A.S., Hammad, H., Angyalosi, G., Tillie-Leblond, I., Mantovani, A., et al. Involvement of the mannose receptor in the uptake of der p 1, a major mite allergen, by human dendritic cells. J. Allergy Clin. Immunol 110:5 (2002), 763–770, 10.1067/mai.2002.129121.
55. Doores, K.J., Bonomelli, C., Harvey, D.J., Vasiljevic, S., Dwek, R.A., Burton, D.R., et al. Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens. Proc. Natl. Acad. Sci. U.S.A. 107:31 (2010), 13800–13805, 10.1073/pnas.1006498107.
56. Drickamer, K., Engineering galactose-binding activity into a c-type mannose-binding protein. Nature 360:6400 (1992), 183–186, 10.1038/360183a0.
57. Drickamer, K., C-type lectin-like domains. Curr. Opin. Struct. Biol 9:5 (1999), 585–590, 10.1016/S0959-440X(99)00009-3.
58. Drickamer, K., Taylor, M.E., Recent insights into structures and functions of c-type lectins in the immune system. Curr. Opin. Struct. Biol 34 (2015), 26–34, 10.1016/j.sbi.2015.06.003.
59. Duus, K., Sandhu, N., Jorgensen, C.S., Hansen, P.R., Steino, A., Thaysen-Andersen, M., et al. Interaction of the chaperone calreticulin with proteins and peptides of different structural classes. Protein Pept. Lett 16:11 (2009), 1414–1423.
60. East, L., Isacke, C.M., The mannose receptor family. Biochim. Biophys. Acta 1572:2–3 (2002), 364–386, 10.1016/S0304-4165(02)00319-7.
61. Ehrenforth, S., Kreuz, W., Scharrer, I., Linde, R., Funk, M., Gungor, T., et al. Incidence of development of factor VIII and factor IX inhibitors in haemophiliacs. Lancet 339:8793 (1992), 594–598, 10.1016/0140-6736(92)90874-3.
62. Endo, Y., Takahashi, M., Fujita, T., Lectin complement system and pattern recognition. Immunobiology 211:4 (2006), 283–293, 10.1016/j.imbio.2006.01.003.
63. Eriksson, J., Woschnagg, C., Fernvik, E., Venge, P., A SELDI-TOF MS study of the genetic and post-translational molecular heterogeneity of eosinophil cationic protein. J. Leukoc. Biol 82:6 (2007), 1491–1500, 10.1189/jlb.0507272.
64. Ernst, J.F., Prill, S.K., O-glycosylation. Med. Mycol 39:Suppl. 1 (2001), 67–74, 10.1080/mmy.39.1.67.74.
65. Esparza, M., Palomares, B., García, T., Espinosa, P., Zenteno, E., Mancilla, R., PstS-1, the 38-kDa mycobacterium tuberculosis glycoprotein, is an adhesin, which binds the macrophage mannose receptor and promotes phagocytosis. Scand. J. Immunol 81:1 (2015), 46–55, 10.1111/sji.12249.
66. Fanibunda, S.E., Modi, D.N., Gokral, J.S., Bandivdekar, A.H., HIV gp120 binds to mannose receptor on vaginal epithelial cells and induces production of matrix metalloproteinases. PLoS ONE, 6(11), 2011, 10.1371/journal.pone.0028014 e28014.
67. Farinha, P., Masoudi, H., Skinnider, B.F., Shumansky, K., Spinelli, J.J., Gill, K., et al. Analysis of multiple biomarkers shows that lymphoma-associated macrophage (LAM) content is an independent predictor of survival in follicular lymphoma (FL). Blood 106:6 (2005), 2169–2174, 10.1182/blood-2005-04-1565.
68. Feinberg, H., Park-Snyder, S., Kolatkar, A.R., Heise, C.T., Taylor, M.E., Weis, W.I., Structure of a c-type carbohydrate recognition domain from the macrophage mannose receptor. J. Biol. Chem 275:28 (2000), 21539–21548, 10.1074/jbc.M002366200.
69. Feinberg, H., Mitchell, D.A., Drickamer, K., Weis, W.I., Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR. Science 294:5549 (2001), 2163–2166, 10.1126/science.1066371.
70. Feinberg, H., Guo, Y., Mitchell, D.A., Drickamer, K., Weis, W.I., Extended neck regions stabilize tetramers of the receptors DC-SIGN and DC-SIGNR. J. Biol. Chem 280:2 (2005), 1327–1335, 10.1074/jbc.M409925200.
71. Feinberg, H., Castelli, R., Drickamer, K., Seeberger, P.H., Weis, W.I., Multiple modes of binding enhance the affinity of DC-SIGN for high mannose n-linked glycans found on viral glycoproteins. J. Biol. Chem 282:6 (2007), 4202–4209, 10.1074/jbc.M609689200.
72. Feinberg, H., Taylor, M.E., Razi, N., McBride, R., Knirel, Y.A., Graham, S.A., et al. Structural basis for langerin recognition of diverse pathogen and mammalian glycans through a single binding site. J. Mol. Biol 405:4 (2011), 1027–1039, 10.1016/j.jmb.2010.11.039.
73. Ferguson, M.A.J., Kinoshita, T., Hart, G.W., Glycosylphosphatidylinositol anchors. Varki, A., Cummings, R.D., Esko, J.D., Freeze, H.H., Stanley, P., Bertozzi, C.R., et al. (eds.) Essentials of Glycobiology, second ed., 2009, Cold Spring Harbor (NY), New York, 143–162.
74. Fiete, D.J., Beranek, M.C., Baenziger, J.U., A cysteine-rich domain of the “mannose” receptor mediates GalNAc-4-SO4 binding. Proc. Natl. Acad. Sci. U.S.A. 95:5 (1998), 2089–2093.
75. Figdor, C.G., van Kooyk, Y., Adema, G.J., C-type lectin receptors on dendritic cells and Langerhans cells. Nat. Rev. Immunol 2:2 (2002), 77–84, 10.1038/nri723.
76. Freeze, H.H., Understanding human glycosylation disorders: biochemistry leads the charge. J. Biol. Chem 288:10 (2013), 6936–6945, 10.1074/jbc.R112.429274.
77. Furmanek, A., Hofsteenge, J., Protein c-mannosylation: facts and questions. Acta Biochim. Pol 47:3 (2000), 781–789.
78. Furukawa, A., Kamishikiryo, J., Mori, D., Toyonaga, K., Okabe, Y., Toji, A., et al. Structural analysis for glycolipid recognition by the c-type lectins mincle and MCL. Proc. Natl. Acad. Sci. U.S.A. 110:43 (2013), 17438–17443, 10.1073/pnas.1312649110.
79. Fuster, M.M., Esko, J.D., The sweet and sour of cancer: glycans as novel therapeutic targets. Nat. Rev. Cancer 5:7 (2005), 526–542, 10.1038/nrc1649.
80. Gabius, H.-J., Kaltner, H., Kopitz, J., André, S., The glycobiology of the CD system: a dictionary for translating marker designations into glycan/lectin structure and function. Trends Biochem. Sci 40:7 (2015), 360–376, 10.1016/j.tibs.2015.03.013.
81. Gabius, H.J., Andre, S., Jimenez-Barbero, J., Romero, A., Solis, D., From lectin structure to functional glycomics: principles of the sugar code. Trends Biochem. Sci 36:6 (2011), 298–313, 10.1016/j.tibs.2011.01.005.
82. Galkina, E., Ley, K., Immune and inflammatory mechanisms of atherosclerosis. Annu. Rev. Immunol 27 (2009), 165–197, 10.1146/annurev.immunol.021908.132620.
83. Garcia-Parajo, M.F., Cambi, A., Torreno-Pina, J.A., Thompson, N., Jacobson, K., Nanoclustering as a dominant feature of plasma membrane organization. J. Cell Sci 127:Pt 23 (2014), 4995–5005, 10.1242/jcs.146340.
84. Garcia-Vallejo, J.J., Van Dijk, W., Van Het Hof, B., Van Die, I., Engelse, M.A., Van Hinsbergh, V.W., et al. Activation of human endothelial cells by tumor necrosis factor-alpha results in profound changes in the expression of glycosylation-related genes. J. Cell. Physiol 206:1 (2006), 203–210, 10.1002/jcp.20458.
85. Garcia-Vallejo, J.J., Koning, N., Ambrosini, M., Kalay, H., Vuist, I., Sarrami-Forooshani, R., et al. Glycodendrimers prevent HIV transmission via DC-SIGN on dendritic cells. Int. Immunol 25:4 (2013), 221–233, 10.1093/intimm/dxs115.
86. Garcia-Vallejo, J.J., Bloem, K., Knippels, L.M., Garssen, J., van Vliet, S.J., van Kooyk, Y., The consequences of multiple simultaneous c-type lectin-ligand interactions: DCIR alters the endo-lysosomal routing of DC-SIGN. Front. Immunol, 6, 2015, 87, 10.3389/fimmu.2015.00087.
87. Gazi, U., Martinez-Pomares, L., Influence of the mannose receptor in host immune responses. Immunobiology 214:7 (2009), 554–561, 10.1016/j.imbio.2008.11.004.
88. Geijtenbeek, T.B., Gringhuis, S.I., Signalling through c-type lectin receptors: shaping immune responses. Nat. Rev. Immunol 9:7 (2009), 465–479, 10.1038/nri2569.
89. Geijtenbeek, T.B., Krooshoop, D.J., Bleijs, D.A., van Vliet, S.J., van Duijnhoven, G.C., Grabovsky, V., et al. DC-SIGN-ICAM-2 interaction mediates dendritic cell trafficking. Nat. Immunol 1:4 (2000), 353–357, 10.1038/79815.
90. Geijtenbeek, T.B., Kwon, D.S., Torensma, R., van Vliet, S.J., van Duijnhoven, G.C., Middel, J., et al. DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells. Cell 100:5 (2000), 587–597, 10.1016/S0092-8674(00)80694-7.
91. Geijtenbeek, T.B.H., van Vliet, S.J., Koppel, E.A., Sanchez-Hernandez, M., Vandenbroucke-Grauls, C.M.J.E., Appelmelk, B., et al. Mycobacteria target DC-SIGN to suppress dendritic cell function. J. Exp. Med 197:1 (2002), 7–17, 10.1084/jem.20021229.
92. Goetz, J.A., Mechref, Y., Kang, P., Jeng, M.H., Novotny, M.V., Glycomic profiling of invasive and non-invasive breast cancer cells. Glycoconj. J. 26:2 (2009), 117–131, 10.1007/s10719-008-9170-4.
93. Graham, L.M., Gupta, V., Schafer, G., Reid, D.M., Kimberg, M., Dennehy, K.M., et al. The c-type lectin receptor CLECSF8 (CLEC4D) is expressed by myeloid cells and triggers cellular activation through Syk kinase. J. Biol. Chem 287:31 (2012), 25964–25974, 10.1074/jbc.M112.384164.
94. Green, R.S., Stone, E.L., Tenno, M., Lehtonen, E., Farquhar, M.G., Marth, J.D., Mammalian n-glycan branching protects against innate immune self-recognition and inflammation in autoimmune disease pathogenesis. Immunity 27:2 (2007), 308–320, 10.1016/j.immuni.2007.06.008.
95. Grigorian, A., Mkhikian, H., Li, C.F., Newton, B.L., Zhou, R.W., Demetriou, M., Pathogenesis of multiple sclerosis via environmental and genetic dysregulation of n-glycosylation. Semin. Immunopathol 34:3 (2012), 415–424, 10.1007/s00281-012-0307-y.
96. Grimes, J.E., Croll, D., Harrison, W.E., Utzinger, J., Freeman, M.C., Templeton, M.R., The roles of water, sanitation and hygiene in reducing schistosomiasis: a review. Parasit. Vectors, 8, 2015, 156, 10.1186/s13071-015-0766-9.
97. Gunn, B.M., Morrison, T.E., Whitmore, A.C., Blevins, L.K., Hueston, L., Fraser, R.J., et al. Mannose binding lectin is required for alphavirus-induced arthritis/myositis. PLoS Pathog, 8(3), 2012, e1002586, 10.1371/journal.ppat.1002586.
98. Guo, Y., Feinberg, H., Conroy, E., Mitchell, D.A., Alvarez, R., Blixt, O., et al. Structural basis for distinct ligand-binding and targeting properties of the receptors DC-SIGN and DC-SIGNR. Nat. Struct. Mol. Biol 11:7 (2004), 591–598, 10.1038/nsmb784.
99. Hajjar, E., Mihajlovic, M., Witko-Sarsat, V., Lazaridis, T., Reuter, N., Computational prediction of the binding site of proteinase 3 to the plasma membrane. Proteins 71:4 (2008), 1655–1669, 10.1002/prot.21853.
100. Halim, A., Larsen, I.S., Neubert, P., Joshi, H.J., Petersen, B.L., Vakhrushev, S.Y., et al. Discovery of a nucleocytoplasmic o-mannose glycoproteome in yeast. Proc. Natl. Acad. Sci. U.S.A., 2015, 10.1073/pnas.1511743112.
101. Haltiwanger, R.S., Lowe, J.B., Role of glycosylation in development. Annu. Rev. Biochem 73 (2004), 491–537, 10.1146/annurev.biochem.73.011303.074043.
102. Haniffa, M., Collin, M., Ginhoux, F., Ontogeny and functional specialization of dendritic cells in human and mouse. Adv. Immunol 120 (2013), 1–49, 10.1016/B978-0-12-417028-5.00001-6.
103. Hansen, S., Holmskov, U., Lung surfactant protein d (sp-d) and the molecular diverted descendants: conglutinin, CL-43 and CL-46. Immunobiology 205:4–5 (2002), 498–517, 10.1078/0171-2985-00150.
104. Hansen, S., Selman, L., Palaniyar, N., Ziegler, K., Brandt, J., Kliem, A., et al. Collectin 11 (CL-11, CL-K1) Is a MASP-1/3–associated plasma collectin with microbial-binding activity. J. Immunol 185:10 (2010), 6096–6104, 10.4049/jimmunol.1002185.
105. Harada, Y., Hirayama, H., Suzuki, T., Generation and degradation of free asparagine-linked glycans. Cell. Mol. Life Sci 72:13 (2015), 2509–2533, 10.1007/s00018-015-1881-7.
106. Hare, N.J., Chan, B., Chan, E., Kaufman, K.L., Britton, W.J., Saunders, B.M., Microparticles released from mycobacterium tuberculosis-infected human macrophages contain increased levels of the type I interferon inducible proteins including ISG15. Proteomics 15:17 (2015), 3020–3029, 10.1002/pmic.201400610.
107. Hart, M.L., Saifuddin, M., Uemura, K., Bremer, E.G., Hooker, B., Kawasaki, T., et al. High mannose glycans and sialic acid on gp120 regulate binding of mannose-binding lectin (MBL) to HIV type 1. AIDS Res. Hum. Retroviruses 18:17 (2002), 1311–1317, 10.1089/088922202320886352.
108. Hartholt, R.B., Peyron, I., Voorberg, J., Hunting down factor VIII in the immunopeptidome. Cell. Immunol, 2015, 10.1016/j.cellimm.2015.11.001.
109. Hartshorn, K.L., Holmskov, U., Hansen, S., Zhang, P., Meschi, J., Mogues, T., et al. Distinctive anti-influenza properties of recombinant collectin 43. Biochem. J. 366:Pt 1 (2002), 87–96, 10.1042/BJ20011868.
110. Hashii, N., Kawasaki, N., Itoh, S., Nakajima, Y., Kawanishi, T., Yamaguchi, T., Alteration of n-glycosylation in the kidney in a mouse model of systemic lupus erythematosus: relative quantification of n-glycans using an isotope-tagging method. Immunology 126:3 (2009), 336–345, 10.1111/j.1365-2567.2008.02898.x.
111. Hauck, D., Joachim, I., Frommeyer, B., Varrot, A., Philipp, B., Moller, H.M., et al. Discovery of two classes of potent glycomimetic inhibitors of pseudomonas aeruginosa LecB with distinct binding modes. ACS Chem. Biol 8:8 (2013), 1775–1784, 10.1021/cb400371r.
112. Heinsbroek, S.E., Taylor, P.R., Martinez, F.O., Martinez-Pomares, L., Brown, G.D., Gordon, S., Stage-specific sampling by pattern recognition receptors during candida albicans phagocytosis. PLoS Pathog, 4(11), 2008, e1000218, 10.1371/journal.ppat.1000218.
113. Hennet, T., Cabalzar, J., Congenital disorders of glycosylation: a concise chart of glycocalyx dysfunction. Trends Biochem. Sci 40:7 (2015), 377–384, 10.1016/j.tibs.2015.03.002.
114. Hilda, J.N., Narasimhan, M., Das, S.D., Mycobacterium tuberculosis strains modify granular enzyme secretion and apoptosis of human neutrophils. Mol. Immunol, 2015, 10.1016/j.molimm.2015.09.019.
115. Hironaka, T., Furukawa, K., Esmon, P.C., Fournel, M.A., Sawada, S., Kato, M., et al. Comparative study of the sugar chains of factor VIII purified from human plasma and from the culture media of recombinant baby hamster kidney cells. J. Biol. Chem 267:12 (1992), 8012–8020.
116. Hirt, C., Eppenberger-Castori, S., Sconocchia, G., Iezzi, G., Tornillo, L., Terracciano, L., et al. Colorectal carcinoma infiltration by myeloperoxidase-expressing neutrophil granulocytes is associated with favorable prognosis. Oncoimmunology, 2(10), 2013, e25990, 10.4161/onci.25990.
117. Holst, S., Deuss, A.J., van Pelt, G.W., van Vliet, S.J., Garcia-Vallejo, J.J., Koeleman, C.A., et al. N-glycosylation profiling of colorectal cancer cell lines reveals association of fucosylation with differentiation and CDX1/villin mRNA expression. Mol. Cell. Proteomics, 2015, 10.1074/mcp.M115.051235.
118. Hottz, E.D., Oliveira, M.F., Nunes, P.C., Nogueira, R.M., Valls-de-Souza, R., Da Poian, A.T., et al. Dengue induces platelet activation, mitochondrial dysfunction and cell death through mechanisms that involve DC-SIGN and caspases. J. Thromb. Haemost 11:5 (2013), 951–962, 10.1111/jth.12178.
119. Hu, F., Ding, G., Zhang, Z., Gatto, L.A., Hawgood, S., Poulain, F.R., et al. Innate immunity of surfactant proteins a and d in urinary tract infection with uropathogenic Escherichia coli. Innate Immun, 2015, 10.1177/1753425915609973.
120. Hurtado, C., Granja, A.G., Bustos, M.J., Nogal, M.L., Gonzalez de Buitrago, G., de Yebenes, V.G., et al. The c-type lectin homologue gene (EP153R) of African swine fever virus inhibits apoptosis both in virus infection and in heterologous expression. Virology 326:1 (2004), 160–170, 10.1016/j.virol.2004.05.019.
121. Hutter, J., Eriksson, M., Johannssen, T., Klopfleisch, R., von Smolinski, D., Gruber, A.D., et al. Role of the c-type lectin receptors MCL and DCIR in experimental colitis. PLoS ONE, 9(7), 2014, 10.1371/journal.pone.0103281 e103281.
122. Hyakumura, M., Walsh, R., Thaysen-Andersen, M., Kingston, N.J., La, M., Lu, L., et al. Modification of asparagine-linked glycan density for the design of hepatitis b virus virus-like particles with enhanced immunogenicity. J. Virol 89:22 (2015), 11312–11322, 10.1128/JVI.01123-15.
123. Hykollari, A., Eckmair, B., Voglmeir, J., Jin, C., Yan, S., Vanbeselaere, J., et al. More than just oligomannose: an n-glycomic comparison of penicillium species. Mol. Cell. Proteomics 15:1 (2016), 73–92, 10.1074/mcp.M115.055061.
124. Ichikawa, M., Scott, D.A., Losfeld, M.-E., Freeze, H.H., The metabolic origins of mannose in glycoproteins. J. Biol. Chem 289:10 (2014), 6751–6761, 10.1074/jbc.M113.544064.
125. Ihara, Y., Inai, Y., Ikezaki, M., Matsui, I.-S.L., Manabe, S., Ito, Y., C-mannosylation: modification on tryptophan in cellular proteins. Taniguchi, N., Endo, T., Hart, G.W., Seeberger, P.H., Wong, C.-H., (eds.) Glycoscience: Biology and Medicine, 2015, 1091–1099 http://dx.doi.org/10.1007/978-4-431-54841-6_67 978-4-431-54841-6 (Online); ISBN: 978-4-431-54840-9 (Print); Springer Date: 20 October 2014.
126. Iobst, S.T., Wormald, M.R., Weis, W.I., Dwek, R.A., Drickamer, K., Binding of sugar ligands to Ca(2+)-dependent animal lectins. I. analysis of mannose binding by site-directed mutagenesis and NMR. J. Biol. Chem 269:22 (1994), 15505–15511.
127. Ip, W.K., Takahashi, K., Ezekowitz, R.A., Stuart, L.M., Mannose-binding lectin and innate immunity. Immunol. Rev 230:1 (2009), 9–21, 10.1111/j.1600-065X.2009.00789.x.
128. Jiang, Y., Zhang, C., Chen, K., Chen, Z., Sun, Z., Zhang, Z., et al. The clinical significance of DC-SIGN and DC-SIGNR, which are novel markers expressed in human colon cancer. PLoS ONE, 9(12), 2014, 10.1371/journal.pone.0114748 e114748.
129. Jin, W., Li, C., Du, T., Hu, K., Huang, X., Hu, Q., DC-SIGN plays a stronger role than DCIR in mediating HIV-1 capture and transfer. Virology 458–459 (2014), 83–92, 10.1016/j.virol.2014.04.016.
130. Johns, T.G., Mellman, I., Cartwright, G.A., Ritter, G., Old, L.J., Burgess, A.W., et al. The antitumor monoclonal antibody 806 recognizes a high-mannose form of the EGF receptor that reaches the cell surface when cells over-express the receptor. FASEB J., 2005, 10.1096/fj.04-1766fje.
131. Johnson, J.L., Jones, M.B., Ryan, S.O., Cobb, B.A., The regulatory power of glycans and their binding partners in immunity. Trends Immunol 34:6 (2013), 290–298, 10.1016/j.it.2013.01.006.
132. Jozefowski, S., The danger model: questioning an unconvincing theory. Immunol. Cell Biol, 2015, 10.1038/icb.2015.68.
133. Kain, R., Rees, A.J., What is the evidence for antibodies to LAMP-2 in the pathogenesis of ANCA associated small vessel vasculitis?. Curr. Opin. Rheumatol 25:1 (2013), 26–34, 10.1097/BOR.0b013e32835b4f8f.
134. Kain, R., Exner, M., Brandes, R., Ziebermayr, R., Cunningham, D., Alderson, C.A., et al. Molecular mimicry in pauci-immune focal necrotizing glomerulonephritis. Nat. Med 14:10 (2008), 1088–1096, 10.1038/nm.1874.
135. Kallenius, G., Correia-Neves, M., Buteme, H., Hamasur, B., Svenson, S.B., Lipoarabinomannan, and its related glycolipids, induce divergent and opposing immune responses to mycobacterium tuberculosis depending on structural diversity and experimental variations. Tuberculosis (Edinb.), 2015, 10.1016/j.tube.2015.09.005.
136. Kang, P.B., Azad, A.K., Torrelles, J.B., Kaufman, T.M., Beharka, A., Tibesar, E., et al. The human macrophage mannose receptor directs mycobacterium tuberculosis lipoarabinomannan-mediated phagosome biogenesis. J. Exp. Med 202:7 (2005), 987–999, 10.1084/jem.20051239.
137. Kaprio, T., Satomaa, T., Heiskanen, A., Hokke, C.H., Deelder, A.M., Mustonen, H., et al. N-glycomic profiling as a tool to separate rectal adenomas from carcinomas. Mol. Cell. Proteomics 14:2 (2015), 277–288, 10.1074/mcp.M114.041632.
138. Karlyshev, A.V., Ketley, J.M., Wren, B.W., The campylobacter jejuni glycome. FEMS Microbiol. Rev 29:2 (2005), 377–390, 10.1016/j.femsre.2005.01.003.
139. Kelly, M., Hwang, J.M., Kubes, P., Modulating leukocyte recruitment in inflammation. J. Allergy Clin. Immunol 120:1 (2007), 3–10, 10.1016/j.jaci.2007.05.017.
140. Kerrigan, A.M., Brown, G.D., C-type lectins and phagocytosis. Immunobiology 214:7 (2009), 562–575, 10.1016/j.imbio.2008.11.003.
141. Khatri, K., Klein, J.A., White, M.R., Grant, O.C., Leymarie, N., Woods, R.J., et al. Integrated omics and computational glycobiology reveal structural basis for influenza A virus glycan microheterogeneity and host interactions. Mol. Cell. Proteomics, 2016, 10.1074/mcp.M116.058016.
142. Khoo, K.H., Chatterjee, D., Caulfield, J.P., Morris, H.R., Dell, A., Structural mapping of the glycans from the egg glycoproteins of Schistosoma mansoni and Schistosoma japonicum: identification of novel core structures and terminal sequences. Glycobiology 7:5 (1997), 663–677.
143. Kjaer, T.R., Thiel, S., Andersen, G.R., Toward a structure-based comprehension of the lectin pathway of complement. Mol. Immunol 56:4 (2013), 413–422, 10.1016/j.molimm.2013.05.007.
144. Klechevsky, E., Flamar, A.L., Cao, Y., Blanck, J.P., Liu, M., O'Bar, A., et al. Cross-priming CD8+ T cells by targeting antigens to human dendritic cells through DCIR. Blood 116:10 (2010), 1685–1697, 10.1182/blood-2010-01-264960.
145. Klenk, H.D., Wagner, R., Heuer, D., Wolff, T., Importance of hemagglutinin glycosylation for the biological functions of influenza virus. Virus Res 82:1–2 (2002), 73–75, 10.1016/S0168-1702(01)00389-6.
146. Kolarich, D., Altmann, F., N-glycan analysis by matrix-assisted laser desorption/ionization mass spectrometry of electrophoretically separated nonmammalian proteins: application to peanut allergen Ara h 1 and olive pollen allergen Ole e 1. Anal. Biochem 285:1 (2000), 64–75, 10.1006/abio.2000.4737.
147. Kolarich, D., Leonard, R., Hemmer, W., Altmann, F., The n-glycans of yellow jacket venom hyaluronidases and the protein sequence of its major isoform in vespula vulgaris. FEBS J. 272:20 (2005), 5182–5190, 10.1111/j.1742-4658.2005.04841.x.
148. Kolarich, D., Altmann, F., Sunderasan, E., Structural analysis of the glycoprotein allergen Hev b 4 from natural rubber latex by mass spectrometry. Biochim. Biophys. Acta 1760:4 (2006), 715–720, 10.1016/j.bbagen.2005.11.012.
149. Kolattukudy, P.E., Fernandes, N.D., Azad, A.K., Fitzmaurice, A.M., Sirakova, T.D., Biochemistry and molecular genetics of cell-wall lipid biosynthesis in mycobacteria. Mol. Microbiol 24:2 (1997), 263–270.
150. Kondo, A., Thaysen-Andersen, M., Hjerno, K., Jensen, O.N., Characterization of sialylated and fucosylated glycopeptides of beta2-glycoprotein I by a combination of HILIC LC and MALDI MS/MS. J. Sep. Sci 33:6–7 (2010), 891–902, 10.1002/jssc.200900802.
151. Kranjcec, B., Papes, D., Altarac, S., D-mannose powder for prophylaxis of recurrent urinary tract infections in women: a randomized clinical trial. World J. Urol 32:1 (2014), 79–84, 10.1007/s00345-013-1091-6.
152. Kreisman, L.S., Cobb, B.A., Infection, inflammation and host carbohydrates: a glyco-evasion hypothesis. Glycobiology 22:8 (2012), 1019–1030, 10.1093/glycob/cws070.
153. Lai, J., Bernhard, O.K., Turville, S.G., Harman, A.N., Wilkinson, J., Cunningham, A.L., Oligomerization of the macrophage mannose receptor enhances gp120-mediated binding of HIV-1. J. Biol. Chem 284:17 (2009), 11027–11038, 10.1074/jbc.M809698200.
154. Lai, J.D., Georgescu, M.T., Hough, C., Lillicrap, D., To clear or to fear: an innate perspective on factor VIII immunity. Cell. Immunol, 2015, 10.1016/j.cellimm.2015.10.011.
155. Lauer, I., Foetisch, K., Kolarich, D., Ballmer-Weber, B.K., Conti, A., Altmann, F., et al. Hazelnut (corylus avellana) vicilin Cor a 11: molecular characterization of a glycoprotein and its allergenic activity. Biochem. J. 383:Pt 2 (2004), 327–334, 10.1042/bj20041062.
156. Le Cabec, V., Emorine, L.J., Toesca, I., Cougoule, C., Maridonneau-Parini, I., The human macrophage mannose receptor is not a professional phagocytic receptor. J. Leukoc. Biol 77:6 (2005), 934–943, 10.1189/jlb.1204705.
157. Lee, J., Breton, G., Oliveira, T.Y., Zhou, Y.J., Aljoufi, A., Puhr, S., et al. Restricted dendritic cell and monocyte progenitors in human cord blood and bone marrow. J. Exp. Med 212:3 (2015), 385–399, 10.1084/jem.20141442.
158. Lee, J.K., Vadas, P., Anaphylaxis: mechanisms and management. Clin. Exp. Allergy 41:7 (2011), 923–938, 10.1111/j.1365-2222.2011.03779.x.
159. Lee, L.Y., Lin, C.H., Fanayan, S., Packer, N.H., Thaysen-Andersen, M., Differential site accessibility mechanistically explains subcellular-specific n-glycosylation determinants. Front. Immunol, 5, 2014, 404, 10.3389/fimmu.2014.00404.
160. Lee, L.Y., Thaysen-Andersen, M., Baker, M.S., Packer, N.H., Hancock, W.S., Fanayan, S., Comprehensive n-glycome profiling of cultured human epithelial breast cells identifies unique secretome n-glycosylation signatures enabling tumorigenic subtype classification. J. Proteome Res 13:11 (2014), 4783–4795, 10.1021/pr500331m.
161. Lee, R.T., Lee, Y.C., Difference in binding-site architecture of the serum-type and liver-type mannose-binding proteins. Glycoconj. J. 14:3 (1997), 357–363.
162. Lee, R.T., Lee, Y.C., Affinity enhancement by multivalent lectin-carbohydrate interaction. Glycoconj. J. 17:7–9 (2000), 543–551, 10.1023/A:1011070425430.
163. Lee, R.T., Hsu, T.L., Huang, S.K., Hsieh, S.L., Wong, C.H., Lee, Y.C., Survey of immune-related, mannose/fucose-binding c-type lectin receptors reveals widely divergent sugar-binding specificities. Glycobiology 21:4 (2011), 512–520, 10.1093/glycob/cwq193.
164. Limpens, J., Stad, R., Vos, C., de Vlaam, C., de Jong, D., van Ommen, G.J., et al. Lymphoma-associated translocation t(14;18) in blood B cells of normal individuals. Blood 85:9 (1995), 2528–2536.
165. Linley, A., Krysov, S., Ponzoni, M., Johnson, P.W., Packham, G., Stevenson, F.K., Lectin binding to surface Ig variable regions provides a universal persistent activating signal for follicular lymphoma cells. Blood 126:16 (2015), 1902–1910, 10.1182/blood-2015-04-640805.
166. Liu, C.F., Tonini, L., Malaga, W., Beau, M., Stella, A., Bouyssie, D., et al. Bacterial protein-o-mannosylating enzyme is crucial for virulence of mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U.S.A. 110:16 (2013), 6560–6565, 10.1073/pnas.1219704110.
167. Liu, X., Nie, H., Zhang, Y., Yao, Y., Maitikabili, A., Qu, Y., et al. Cell surface-specific n-glycan profiling in breast cancer. PLoS ONE, 8(8), 2013, 10.1371/journal.pone.0072704 e72704.
168. Liu, Y., Chirino, A.J., Misulovin, Z., Leteux, C., Feizi, T., Nussenzweig, M.C., et al. Crystal structure of the cysteine-rich domain of mannose receptor complexed with a sulfated carbohydrate ligand. J. Exp. Med 191:7 (2000), 1105–1116, 10.1084/jem.191.7.1105.
169. Liu, Z., Liu, B., Zhang, Z.T., Zhou, T.T., Bian, H.J., Min, M.W., et al. A mannose-binding lectin from sophora flavescens induces apoptosis in HeLa cells. Phytomedicine 15:10 (2008), 867–875, 10.1016/j.phymed.2008.02.025.
170. Lohse, S., Meyer, S., Meulenbroek, L.A., Jansen, J.H., Nederend, M., Kretschmer, A., et al. An anti-EGFR IgA that displays improved pharmacokinetics and myeloid effector cell engagement in vivo. Cancer Res, 2015, 10.1158/0008-5472.CAN-15-1232.
171. Loibl, M., Strahl, S., Protein o-mannosylation: what we have learned from baker's yeast. Biochim. Biophys. Acta 1833:11 (2013), 2438–2446, 10.1016/j.bbamcr.2013.02.008.
172. Loke, I., Packer, N.H., Thaysen-Andersen, M., Complementary LC-MS/MS-based n-glycan, n-glycopeptide, and intact n-glycoprotein profiling reveals unconventional Asn71-glycosylation of human neutrophil cathepsin G. Biomolecules 5:3 (2015), 1832–1854, 10.3390/biom5031832.
173. Lombardi, V.C., Khaiboullina, S.F., Rizvanov, A.A., Plasmacytoid dendritic cells, a role in neoplastic prevention and progression. Eur. J. Clin. Invest 45:Suppl. 1 (2015), 1–8, 10.1111/eci.12363.
174. Lommel, M., Strahl, S., Protein o-mannosylation: conserved from bacteria to humans. Glycobiology 19:8 (2009), 816–828, 10.1093/glycob/cwp066.
175. Loures, F.V., Rohm, M., Lee, C.K., Santos, E., Wang, J.P., Specht, C.A., et al. Recognition of aspergillus fumigatus hyphae by human plasmacytoid dendritic cells is mediated by dectin-2 and results in formation of extracellular traps. PLoS Pathog, 11(2), 2015, e1004643, 10.1371/journal.ppat.1004643.
176. Lowe, J.B., Glycan-dependent leukocyte adhesion and recruitment in inflammation. Curr. Opin. Cell Biol 15:5 (2003), 531–538, 10.1016/j.ceb.2003.08.002.
177. Lu, J., Teh, C., Kishore, U., Reid, K.B., Collectins and ficolins: sugar pattern recognition molecules of the mammalian innate immune system. Biochim. Biophys. Acta 1572:2–3 (2002), 387–400, 10.1016/S0304-4165(02)00320-3.
178. Lu, J.H., Thiel, S., Wiedemann, H., Timpl, R., Reid, K.B., Binding of the pentamer/hexamer forms of mannan-binding protein to zymosan activates the proenzyme C1r2C1s2 complex, of the classical pathway of complement, without involvement of C1q. J. Immunol 144:6 (1990), 2287–2294.
179. Lyons, J.J., Milner, J.D., Rosenzweig, S.D., Glycans instructing immunity: the emerging role of altered glycosylation in clinical immunology. Front Pediatr, 3, 2015, 54, 10.3389/fped.2015.00054.
180. Ma, Y.J., Hein, E., Munthe-Fog, L., Skjoedt, M.O., Bayarri-Olmos, R., Romani, L., et al. Soluble collectin-12 (CL-12) is a pattern recognition molecule initiating complement activation via the alternative pathway. J. Immunol, 2015, 10.4049/jimmunol.1500493.
181. Maeda, N., Nigou, J., Herrmann, J.L., Jackson, M., Amara, A., Lagrange, P.H., et al. The cell surface receptor DC-SIGN discriminates between mycobacterium species through selective recognition of the mannose caps on lipoarabinomannan. J. Biol. Chem 278:8 (2003), 5513–5516, 10.1074/jbc.C200586200.
182. Margreet, A.W., Geert-Jan, B., Adaptive immune activation: glycosylation does matter. Nat. Chem. Bio 9:12 (2013), 776–784, 10.1038/nchembio.1403.
183. Marotte, K., Sabin, C., Preville, C., Moume-Pymbock, M., Wimmerova, M., Mitchell, E.P., et al. X-ray structures and thermodynamics of the interaction of PA-IIL from pseudomonas aeruginosa with disaccharide derivatives. ChemMedChem 2:9 (2007), 1328–1338, 10.1002/cmdc.200700100.
184. Martinez-Pomares, L., The mannose receptor. J. Leukoc. Biol 92:6 (2012), 1177–1186, 10.1189/jlb.0512231.
185. Martinez-Pomares, L., Mahoney, J.A., Kaposzta, R., Linehan, S.A., Stahl, P.D., Gordon, S., A functional soluble form of the murine mannose receptor is produced by macrophages in vitro and is present in mouse serum. J. Biol. Chem 273:36 (1998), 23376–23380, 10.1074/jbc.273.36.23376.
186. Mason, C.P., Tarr, A.W., Human lectins and their roles in viral infections. Molecules 20:2 (2015), 2229–2271, 10.3390/molecules20022229.
187. Masuoka, J., Surface glycans of candida albicans and other pathogenic fungi: physiological roles, clinical uses, and experimental challenges. Clin. Microbiol. Rev 17:2 (2004), 281–310, 10.1128/cmr.17.2.281-310.2004.
188. Matsumoto, M., Tanaka, T., Kaisho, T., Sanjo, H., Copeland, N.G., Gilbert, D.J., et al. A novel LPS-inducible c-type lectin is a transcriptional target of NF-IL6 in macrophages. J. Immunol 163:9 (1999), 5039–5048.
189. Matthijsen, R.A., de Winther, M.P., Kuipers, D., van der Made, I., Weber, C., Herias, M.V., et al. Macrophage-specific expression of mannose-binding lectin controls atherosclerosis in low-density lipoprotein receptor-deficient mice. Circulation 119:16 (2009), 2188–2195, 10.1161/circulationaha.108.830661.
190. Maverakis, E., Kim, K., Shimoda, M., Gershwin, M.E., Patel, F., Wilken, R., et al. Glycans in the immune system and the altered glycan theory of autoimmunity: a critical review. J. Autoimmun 57 (2015), 1–13, 10.1016/j.jaut.2014.12.002.
191. Mazumder, P., Mukhopadhyay, C., Conformations, dynamics and interactions of di-, tri- and pentamannoside with mannose binding lectin: a molecular dynamics study. Carbohydr. Res 349 (2012), 59–72, 10.1016/j.carres.2011.11.021.
192. McCarthy, T.R., Torrelles, J.B., MacFarlane, A.S., Katawczik, M., Kutzbach, B., Desjardin, L.E., et al. Overexpression of mycobacterium tuberculosis manB, a phosphomannomutase that increases phosphatidylinositol mannoside biosynthesis in mycobacterium smegmatis and mycobacterial association with human macrophages. Mol. Microbiol 58:3 (2005), 774–790, 10.1111/j.1365-2958.2005.04862.x.
193. McGreal, E.P., Rosas, M., Brown, G.D., Zamze, S., Wong, S.Y., Gordon, S., et al. The carbohydrate-recognition domain of dectin-2 is a c-type lectin with specificity for high mannose. Glycobiology 16:5 (2006), 422–430, 10.1093/glycob/cwj077.
194. Medzihradszky, K.F., Besman, M.J., Burlingame, A.L., Structural characterization of site-specific n-glycosylation of recombinant human factor VIII by reversed-phase high-performance liquid chromatography-electrospray ionization mass spectrometry. Anal. Chem 69:19 (1997), 3986–3994, 10.1021/ac970372z.
195. Menon, S., Rosenberg, K., Graham, S.A., Ward, E.M., Taylor, M.E., Drickamer, K., et al. Binding-site geometry and flexibility in DC-SIGN demonstrated with surface force measurements. Proc. Natl. Acad. Sci. U.S.A. 106:28 (2009), 11524–11529, 10.1073/pnas.0901783106.
196. Mesman, A.W., de Vries, R.D., McQuaid, S., Duprex, W.P., de Swart, R.L., Geijtenbeek, T.B., A prominent role for DC-SIGN+ dendritic cells in initiation and dissemination of measles virus infection in non-human primates. PLoS ONE, 7(12), 2012, 10.1371/journal.pone.0049573 e49573.
197. Mildner, A., Jung, S., Development and function of dendritic cell subsets. Immunity 40:5 (2014), 642–656, 10.1016/j.immuni.2014.04.016.
198. Mir-Shekari, S.Y., Ashford, D.A., Harvey, D.J., Dwek, R.A., Schulze, I.T., The glycosylation of the influenza A virus hemagglutinin by mammalian cells. A site-specific study. J. Biol. Chem 272:7 (1997), 4027–4036.
199. Mitchell, D.A., Fadden, A.J., Drickamer, K., A novel mechanism of carbohydrate recognition by the c-type lectins DC-SIGN and DC-SIGNR. subunit organization and binding to multivalent ligands. J. Biol. Chem 276:31 (2001), 28939–28945, 10.1074/jbc.M104565200.
200. Mocsai, A., Ruland, J., Tybulewicz, V.L., The SYK tyrosine kinase: a crucial player in diverse biological functions. Nat. Rev. Immunol 10:6 (2010), 387–402, 10.1038/nri2765.
201. Moh, E.S., Lin, C.H., Thaysen-Andersen, M., Packer, N.H., Site-specific n-glycosylation of recombinant pentameric and hexameric human IgM. J. Am. Soc. Mass Spectrom, 2016, 10.1007/s13361-016-1378-0.
202. Mollegaard, K.M., Duus, K., Traeholt, S.D., Thaysen-Andersen, M., Liu, Y., Palma, A.S., et al. The interactions of calreticulin with immunoglobulin G and immunoglobulin Y. Biochim. Biophys. Acta 1814:7 (2011), 889–899, 10.1016/j.bbapap.2011.03.015.
203. Moore, P.L., Gray, E.S., Wibmer, C.K., Bhiman, J.N., Nonyane, M., Sheward, D.J., et al. Evolution of an HIV glycan-dependent broadly neutralizing antibody epitope through immune escape. Nat. Med 18:11 (2012), 1688–1692, 10.1038/nm.2985.
204. Moremen, K.W., Tiemeyer, M., Nairn, A.V., Vertebrate protein glycosylation: diversity, synthesis and function. Nat. Rev. Mol. Cell Biol 13:7 (2012), 448–462, 10.1038/nrm3383.
205. Morfini, M., Coppola, A., Franchini, M., Di Minno, G., Clinical use of factor VIII and factor IX concentrates. Blood Transfus 11:Suppl. 4 (2013), s55–s63, 10.2450/2013.010s.
206. Mullin, N.P., Hall, K.T., Taylor, M.E., Characterization of ligand binding to a carbohydrate-recognition domain of the macrophage mannose receptor. J. Biol. Chem 269:45 (1994), 28405–28413.
207. Mullin, N.P., Hitchen, P.G., Taylor, M.E., Mechanism of Ca2+ and monosaccharide binding to a c-type carbohydrate-recognition domain of the macrophage mannose receptor. J. Biol. Chem 272:9 (1997), 5668–5681, 10.1074/jbc.272.9.5668.
208. Mulvey, M.A., Schilling, J.D., Martinez, J.J., Hultgren, S.J., Bad bugs and beleaguered bladders: interplay between uropathogenic Escherichia coli and innate host defenses. Proc. Natl. Acad. Sci. U.S.A. 97:16 (2000), 8829–8835, 10.1073/pnas.97.16.8829.
209. Mydock-McGrane, L.K., Cusumano, Z.T., Janetka, J.W., Mannose-derived FimH antagonists: a promising anti-virulence therapeutic strategy for urinary tract infections and Crohn's disease. Expert Opin. Ther. Pat, 2015, 10.1517/13543776.2016.1131266.
210. Nagae, M., Ikeda, A., Hanashima, S., Kojima, T., Matsumoto, N., Yamamoto, K., et al. Crystal structure of human dendritic cell inhibitory receptor (DCIR) C-type lectin domain reveals the binding mode with n-glycan. FEBS Lett, 2016, 10.1002/1873-3468.12162.
211. Nauseef, W.M., Borregaard, N., Neutrophils at work. Nat. Immunol 15:7 (2014), 602–611, 10.1038/ni.2921.
212. Nauta, A.J., Raaschou-Jensen, N., Roos, A., Daha, M.R., Madsen, H.O., Borrias-Essers, M.C., et al. Mannose-binding lectin engagement with late apoptotic and necrotic cells. Eur. J. Immunol 33:10 (2003), 2853–2863, 10.1002/eji.200323888.
213. Neefjes, J., Ovaa, H., A peptide's perspective on antigen presentation to the immune system. Nat. Chem. Biol 9:12 (2013), 769–775, 10.1038/nchembio.1391.
214. Netea, M.G., Gow, N.A., Munro, C.A., Bates, S., Collins, C., Ferwerda, G., et al. Immune sensing of Candida albicans requires cooperative recognition of mannans and glucans by lectin and Toll-like receptors. J. Clin. Invest 116:6 (2006), 1642–1650, 10.1172/JCI27114.
215. Netea, M.G., Joosten, L.A., van der Meer, J.W., Kullberg, B.J., van de Veerdonk, F.L., Immune defence against candida fungal infections. Nat. Rev. Immunol 15:10 (2015), 630–642, 10.1038/nri3897.
216. Ng, K.K., Drickamer, K., Weis, W.I., Structural analysis of monosaccharide recognition by rat liver mannose-binding protein. J. Biol. Chem 271:2 (1996), 663–674, 10.1074/jbc.271.2.663.
217. Ng, K.K., Kolatkar, A.R., Park-Snyder, S., Feinberg, H., Clark, D.A., Drickamer, K., et al. Orientation of bound ligands in mannose-binding proteins. Implications for multivalent ligand recognition. J. Biol. Chem 277:18 (2002), 16088–16095, 10.1074/jbc.M200493200.
218. Nichollas, E.S., Marzook, N.B., Joel, A.C., Nestor, S., Morten, T.-A., Steven, P.D., et al. Comparative proteomics and glycoproteomics reveal increased n-linked glycosylation and relaxed sequon specificity in Campylobacter jejuni NCTC11168 O. J. Proteome Res 13:11 (2014), 5136–5150, 10.1021/pr5005554.
219. Nicholson, R.I., Gee, J.M., Harper, M.E., EGFR and cancer prognosis. Eur. J. Cancer 37:Suppl. 4 (2001), S9–S15, 10.1016/S0959-8049(01)00231-3.
220. Nonaka, M., Imaeda, H., Matsumoto, S., Yong Ma, B., Kawasaki, N., Mekata, E., et al. Mannan-binding protein, a c-type serum lectin, recognizes primary colorectal carcinomas through tumor-associated Lewis glycans. J. Immunol 192:3 (2014), 1294–1301, 10.4049/jimmunol.1203023.
221. Obermajer, N., Sattin, S., Colombo, C., Bruno, M., Svajger, U., Anderluh, M., et al. Design, synthesis and activity evaluation of mannose-based DC-SIGN antagonists. Mol. Divers 15:2 (2011), 347–360, 10.1007/s11030-010-9285-y.
222. Ohtsubo, K., Marth, J.D., Glycosylation in cellular mechanisms of health and disease. Cell 126:5 (2006), 855–867, 10.1016/j.cell.2006.08.019.
223. Olczak, M., Watorek, W., Structural analysis of n-glycans from human neutrophil azurocidin. Biochem. Biophys. Res. Commun 293:1 (2002), 213–219, 10.1016/S0006-291X(02)00201-2.
224. Olejnik, B., Jarzab, A., Kratz, E.M., Zimmer, M., Gamian, A., Ferens-Sieczkowska, M., Terminal mannose residues in seminal plasma glycoproteins of infertile men compared to fertile donors. Int. J. Mol. Sci 16:7 (2015), 14933–14950, 10.3390/ijms160714933.
225. Ozcan, S., Barkauskas, D.A., Renee Ruhaak, L., Torres, J., Cooke, C.L., An, H.J., et al. Serum glycan signatures of gastric cancer. Cancer Prev. Res. (Phila) 7:2 (2014), 226–235, 10.1158/1940-6207.CAPR-13-0235.
226. Pak, J., Pu, Y., Zhang, Z.T., Hasty, D.L., Wu, X.R., Tamm-horsfall protein binds to type 1 fimbriated Escherichia coli and prevents E. coli from binding to uroplakin Ia and Ib receptors. J. Biol. Chem 276:13 (2001), 9924–9930, 10.1074/jbc.M008610200.
227. Park, H.M., Hwang, M.P., Kim, Y.W., Kim, K.J., Jin, J.M., Kim, Y.H., et al. Mass spectrometry-based n-linked glycomic profiling as a means for tracking pancreatic cancer metastasis. Carbohydr. Res 413 (2015), 5–11, 10.1016/j.carres.2015.04.019.
228. Parker, B.L., Thaysen-Andersen, M., Solis, N., Scott, N.E., Larsen, M.R., Graham, M.E., et al. Site-specific glycan-peptide analysis for determination of n-glycoproteome heterogeneity. J. Proteome Res 12:12 (2013), 5791–5800, 10.1021/pr400783j.
229. Parker, B.L., Thaysen-Andersen, M., Fazakerley, D.J., Holliday, M., Packer, N.H., James, D.E., Terminal galactosylation and sialylation switching on membrane glycoproteins upon TNF-alpha-induced insulin resistance in adipocytes. Mol. Cell. Proteomics, 2015, 10.1074/mcp.M115.054221.
230. Patterson, J.H., Waller, R.F., Jeevarajah, D., Billman-Jacobe, H., McConville, M.J., Mannose metabolism is required for mycobacterial growth. Biochem. J. 372:Pt 1 (2003), 77–86, 10.1042/BJ20021700.
231. Pejchal, R., Doores, K.J., Walker, L.M., Khayat, R., Huang, P.S., Wang, S.K., et al. A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield. Science 334:6059 (2011), 1097–1103, 10.1126/science.1213256.
232. Peterson, R., Cheah, W.Y., Grinyer, J., Packer, N., Glycoconjugates in human milk: protecting infants from disease. Glycobiology 23:12 (2013), 1425–1438, 10.1093/glycob/cwt072.
233. Pichl, C.M., Feilhauer, S., Schwaigerlehner, R.M., Gabor, F., Wirth, M., Neutsch, L., Glycan-mediated uptake in urothelial primary cells: perspectives for improved intravesical drug delivery in urinary tract infections. Int. J. Pharm 495:2 (2015), 710–718, 10.1016/j.ijpharm.2015.09.017.
234. Pinho, S.S., Reis, C.A., Glycosylation in cancer: mechanisms and clinical implications. Nat. Rev. Cancer 15:9 (2015), 540–555, 10.1038/nrc3982.
235. Plomp, R., Hensbergen, P.J., Rombouts, Y., Zauner, G., Dragan, I., Koeleman, C.A., et al. Site-specific n-glycosylation analysis of human immunoglobulin e. J. Proteome Res 13:2 (2014), 536–546, 10.1021/pr400714w.
236. Pohlmann, S., Soilleux, E.J., Baribaud, F., Leslie, G.J., Morris, L.S., Trowsdale, J., et al. DC-SIGNR, a DC-SIGN homologue expressed in endothelial cells, binds to human and simian immunodeficiency viruses and activates infection in trans. Proc. Natl. Acad. Sci. U.S.A. 98:5 (2001), 2670–2675, 10.1073/pnas.051631398.
237. Praissman, J.L., Wells, L., Mammalian o-mannosylation pathway: glycan structures, enzymes, and protein substrates. Biochemistry 53:19 (2014), 3066–3078, 10.1021/bi500153y.
238. Pritchard, L.K., Spencer, D.I., Royle, L., Bonomelli, C., Seabright, G.E., Behrens, A.J., et al. Glycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodies. Nat. Commun, 6, 2015, 7479, 10.1038/ncomms8479.
239. Qu, C., Edwards, E.W., Tacke, F., Angeli, V., Llodra, J., Sanchez-Schmitz, G., et al. Role of CCR8 and other chemokine pathways in the migration of monocyte-derived dendritic cells to lymph nodes. J. Exp. Med 200:10 (2004), 1231–1241, 10.1084/jem.20032152.
240. Rabinovich, G.A., Toscano, M.A., Turning ‘sweet’ on immunity: galectin-glycan interactions in immune tolerance and inflammation. Nat. Rev. Immunol 9:5 (2009), 338–352, 10.1038/nri2536.
241. Rachmilewitz, J., Glycosylation: an intrinsic sign of “danger”. Self Nonself 1:3 (2010), 250–254, 10.4161/self.1.3.12330.
242. Radcliffe, C.M., Arnold, J.N., Suter, D.M., Wormald, M.R., Harvey, D.J., Royle, L., et al. Human follicular lymphoma cells contain oligomannose glycans in the antigen-binding site of the B-cell receptor. J. Biol. Chem 282:10 (2007), 7405–7415, 10.1074/jbc.M602690200.
243. Rajaram, M.V., Ni, B., Morris, J.D., Brooks, M.N., Carlson, T.K., Bakthavachalu, B., et al. Mycobacterium tuberculosis lipomannan blocks TNF biosynthesis by regulating macrophage MAPK-activated protein kinase 2 (MK2) and microRNA miR-125b. Proc. Natl. Acad. Sci. U.S.A. 108:42 (2011), 17408–17413, 10.1073/pnas.1112660108.
244. Rajaram, M.V., Ni, B., Dodd, C.E., Schlesinger, L.S., Macrophage immunoregulatory pathways in tuberculosis. Semin. Immunol 26:6 (2014), 471–485, 10.1016/j.smim.2014.09.010.
245. Ravnsborg, T., Houen, G., Hojrup, P., The glycosylation of myeloperoxidase. Biochim. Biophys. Acta 1804:10 (2010), 2046–2053, 10.1016/j.bbapap.2010.07.001.
246. Richardson, M.B., Williams, S.J., MCL and mincle: c-type lectin receptors that sense damaged self and pathogen-associated molecular patterns. Front. Immunol, 5, 2014, 288, 10.3389/fimmu.2014.00288.
247. Rini, J., Esko, J., Varki, A., Glycosyltransferases and glycan-processing Enzymes. Varki, A., Cummings, R.D., Esko, J.D., Freeze, H.H., Stanley, P., Bertozzi, C.R., et al. (eds.) Essentials of Glycobiology, second ed., 2009, Cold Spring Harbor, New York, 63–74.
248. Robajac, D., Vanhooren, V., Masnikosa, R., Miković, Ž., Mandić, V., Libert, C., et al. Preeclampsia transforms membrane N-glycome in human placenta. Exp. Mol. Pathol, 2015, 10.1016/j.yexmp.2015.11.029.
249. Robinson, M.J., Sancho, D., Slack, E.C., LeibundGut-Landmann, S., Reis e Sousa, C., Myeloid C-type lectins in innate immunity. Nat. Immunol 7:12 (2006), 1258–1265, 10.1038/ni1417.
250. Robinson, M.J., Osorio, F., Rosas, M., Freitas, R.P., Schweighoffer, E., Gross, O., et al. Dectin-2 is a Syk-coupled pattern recognition receptor crucial for Th17 responses to fungal infection. J. Exp. Med 206:9 (2009), 2037–2051, 10.1084/jem.20082818.
251. Rock, K.L., Latz, E., Ontiveros, F., Kono, H., The sterile inflammatory response. Annu. Rev. Immunol 28 (2010), 321–342, 10.1146/annurev-immunol-030409-101311.
252. Roth, A.J., Brown, M.C., Smith, R.N., Badhwar, A.K., Parente, O., Chung, H., et al. Anti-LAMP-2 antibodies are not prevalent in patients with antineutrophil cytoplasmic autoantibody glomerulonephritis. J. Am. Soc. Nephrol 23:3 (2012), 545–555, 10.1681/asn.2011030273.
253. Roth, J., Zuber, C., Park, S., Jang, I., Lee, Y., Kysela, K.G., et al. Protein N-glycosylation, protein folding, and protein quality control. Mol. Cells 30:6 (2010), 497–506, 10.1007/s10059-010-0159-z.
254. Ruhaak, L.R., Taylor, S.L., Stroble, C., Nguyen, U.T., Parker, E.A., Song, T., et al. Differential n-glycosylation patterns in lung adenocarcinoma tissue. J. Proteome Res 14:11 (2015), 4538–4549, 10.1021/acs.jproteome.5b00255.
255. Russell, D.G., Mycobacterium tuberculosis and the intimate discourse of a chronic infection. Immunol. Rev 240:1 (2011), 252–268, 10.1111/j.1600-065X.2010.00984.x.
256. Sabin, C., Mitchell, E.P., Pokorna, M., Gautier, C., Utille, J.P., Wimmerova, M., et al. Binding of different monosaccharides by lectin PA-IIL from pseudomonas aeruginosa: thermodynamics data correlated with x-ray structures. FEBS Lett 580:3 (2006), 982–987, 10.1016/j.febslet.2006.01.030.
257. Saeland, E., Belo, A.I., Mongera, S., van Die, I., Meijer, G.A., van Kooyk, Y., Differential glycosylation of MUC1 and CEACAM5 between normal mucosa and tumour tissue of colon cancer patients. Int. J. Cancer 131:1 (2012), 117–128, 10.1002/ijc.26354.
258. Sahly, H., Ofek, I., Podschun, R., Brade, H., He, Y., Ullmann, U., et al. Surfactant protein d binds selectively to klebsiella pneumoniae lipopolysaccharides containing mannose-rich o-antigens. J. Immunol 169:6 (2002), 3267–3274, 10.4049/jimmunol.169.6.3267.
259. Sallusto, F., Lanzavecchia, A., Efficient presentation of soluble antigen by cultured human dendritic cells is maintained by granulocyte/macrophage colony-stimulating factor plus interleukin 4 and downregulated by tumor necrosis factor alpha. J. Exp. Med 179:4 (1994), 1109–1118.
260. Sancho, D., Reis e Sousa, C., Signaling by myeloid c-type lectin receptors in immunity and homeostasis. Annu. Rev. Immunol 30 (2012), 491–529, 10.1146/annurev-immunol-031210-101352.
261. Sandborn, W.J., Serologic markers in inflammatory bowel disease: state of the art. Rev. Gastroenterol. Disord 4:4 (2004), 167–174.
262. Sanders, R.W., Venturi, M., Schiffner, L., Kalyanaraman, R., Katinger, H., Lloyd, K.O., et al. The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120. J. Virol 76:14 (2002), 7293–7305, 10.1128/JVI.76.14.7293-7305.2002.
263. Santiago, C., Celma, M.L., Stehle, T., Casasnovas, J.M., Structure of the measles virus hemagglutinin bound to the CD46 receptor. Nat. Struct. Mol. Biol 17:1 (2010), 124–129, 10.1038/nsmb.1726.
264. Sato, K., Yang, X.L., Yudate, T., Chung, J.S., Wu, J., Luby-Phelps, K., et al. Dectin-2 is a pattern recognition receptor for fungi that couples with the Fc receptor gamma chain to induce innate immune responses. J. Biol. Chem 281:50 (2006), 38854–38866, 10.1074/jbc.M606542200.
265. Sauer, M.M., Jakob, R.P., Eras, J., Baday, S., Eris, D., Navarra, G., et al. Catch-bond mechanism of the bacterial adhesin FimH. Nat. Commun, 7, 2016, 10738, 10.1038/ncomms10738.
266. Scanlan, C.N., Offer, J., Zitzmann, N., Dwek, R.A., Exploiting the defensive sugars of HIV-1 for drug and vaccine design. Nature 446:7139 (2007), 1038–1045, 10.1038/nature05818.
267. Schachter, H., Paucimannose n-glycans in Caenorhabditis elegans and Drosophila melanogaster. Carbohydr. Res 344:12 (2009), 1391–1396, 10.1016/j.carres.2009.04.028.
268. Schedin-Weiss, S., Winblad, B., Tjernberg, L.O., The role of protein glycosylation in Alzheimer disease. FEBS J. 281:1 (2014), 46–62, 10.1111/febs.12590.
269. Schlesinger, L.S., Hull, S.R., Kaufman, T.M., Binding of the terminal mannosyl units of lipoarabinomannan from a virulent strain of mycobacterium tuberculosis to human macrophages. J. Immunol 152:8 (1994), 4070–4079.
270. Schlesinger, L.S., Kaufman, T.M., Iyer, S., Hull, S.R., Marchiando, L.K., Differences in mannose receptor-mediated uptake of lipoarabinomannan from virulent and attenuated strains of mycobacterium tuberculosis by human macrophages. J. Immunol 157:10 (1996), 4568–4575.
271. Schnaar, R.L., Glycobiology simplified: diverse roles of glycan recognition in inflammation. J. Leukoc. Biol, 2016, 10.1189/jlb.3RI0116-021R.
272. Schweizer, A., Stahl, P.D., Rohrer, J., A di-aromatic motif in the cytosolic tail of the mannose receptor mediates endosomal sorting. J. Biol. Chem 275:38 (2000), 29694–29700, 10.1074/jbc.M000571200.
273. Scordo, J.M., Knoell, D.L., Torrelles, J.B., Alveolar epithelial cells in mycobacterium tuberculosis Infection: active players or innocent bystanders?. J. Innate Immun, 2015, 10.1159/000439275.
274. Scott, D.W., Patel, R.P., Endothelial heterogeneity and adhesion molecules n-glycosylation: implications in leukocyte trafficking in inflammation. Glycobiology 23:6 (2013), 622–633, 10.1093/glycob/cwt014.
275. Scott, D.W., Chen, J., Chacko, B.K., Traylor, J.G. Jr., Orr, A.W., Patel, R.P., Role of endothelial n-glycan mannose residues in monocyte recruitment during atherogenesis. Arterioscler. Thromb. Vasc. Biol 32:8 (2012), e51–e59, 10.1161/atvbaha.112.253203.
276. Scott, D.W., Dunn, T.S., Ballestas, M.E., Litovsky, S.H., Patel, R.P., Identification of a high-mannose ICAM-1 glycoform: effects of ICAM-1 hypoglycosylation on monocyte adhesion and outside in signaling. Am. J. Physiol. Cell Physiol 305:2 (2013), C228–C237, 10.1152/ajpcell.00116.2013.
277. Scott, N.E., Marzook, N.B., Cain, J.A., Solis, N., Thaysen-Andersen, M., Djordjevic, S.P., et al. Comparative proteomics and glycoproteomics reveal increased n-linked glycosylation and relaxed sequon specificity in campylobacter jejuni NCTC11168 O. J. Proteome Res 13:11 (2014), 5136–5150, 10.1021/pr5005554.
278. Segura, E., Amigorena, S., Inflammatory dendritic cells in mice and humans. Trends Immunol 34:9 (2013), 440–445, 10.1016/j.it.2013.06.001.
279. Sendid, B., Colombel, J.F., Jacquinot, P.M., Faille, C., Fruit, J., Cortot, A., et al. Specific antibody response to oligomannosidic epitopes in Crohn's disease. Clin. Diagn. Lab. Immunol 3:2 (1996), 219–226.
280. Sethi, M.K., Thaysen-Andersen, M., Smith, J.T., Baker, M.S., Packer, N.H., Hancock, W.S., et al. Comparative n-glycan profiling of colorectal cancer cell lines reveals unique bisecting GlcNAc and alpha-2,3-linked sialic acid determinants are associated with membrane proteins of the more metastatic/aggressive cell lines. J. Proteome Res 13:1 (2014), 277–288, 10.1021/pr400861m.
281. Sethi, M.K., Kim, H., Park, C.K., Baker, M.S., Paik, Y.K., Packer, N.H., et al. In-depth n-glycome profiling of paired colorectal cancer and non-tumorigenic tissues reveals cancer-, stage- and EGFR-specific protein n-glycosylation. Glycobiology 25:10 (2015), 1064–1078, 10.1093/glycob/cwv042.
282. Shade, K.T., Platzer, B., Washburn, N., Mani, V., Bartsch, Y.C., Conroy, M., et al. A single glycan on IgE is indispensable for initiation of anaphylaxis. J. Exp. Med 212:4 (2015), 457–467, 10.1084/jem.20142182.
283. Sharma, V., Ichikawa, M., Freeze, H.H., Mannose metabolism: more than meets the eye. Biochem. Biophys. Res. Commun 453:2 (2014), 220–228, 10.1016/j.bbrc.2014.06.021.
284. Sheriff, S., Chang, C.Y., Ezekowitz, R.A., Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil. Nat. Struct. Biol 1:11 (1994), 789–794, 10.1038/nsb1194-789.
285. Shibata, N., Ikuta, K., Imai, T., Satoh, Y., Satoh, R., Suzuki, A., et al. Existence of branched side chains in the cell wall mannan of pathogenic yeast, Candida albicans. structure-antigenicity relationship between the cell wall mannans of Candida albicans and Candida parapsilosis. J. Biol. Chem 270:3 (1995), 1113–1122, 10.1074/jbc.270.3.1113.
286. Shreffler, W.G., Castro, R.R., Kucuk, Z.Y., Charlop-Powers, Z., Grishina, G., Yoo, S., et al. The major glycoprotein allergen from arachis hypogaea, Ara h 1, is a ligand of dendritic cell-specific ICAM-grabbing nonintegrin and acts as a Th2 adjuvant in vitro. J. Immunol 177:6 (2006), 3677–3685, 10.4049/jimmunol.177.6.3677.
287. Smagula, R.M., Van Halbeek, H., Decker, J.M., Muchmore, A.V., Moody, C.E., Sherblom, A.P., Pregnancy-associated changes in oligomannose oligosaccharides of human and bovine uromodulin (Tamm-horsfall glycoprotein). Glycoconj. J. 7:6 (1990), 609–624.
288. Smith, G.T., Sweredoski, M.J., Hess, S., O-linked glycosylation sites profiling in mycobacterium tuberculosis culture filtrate proteins. J. Proteomics 97 (2014), 296–306, 10.1016/j.jprot.2013.05.011.
289. Sondergaard, J.N., Vinner, L., Brix, S., Natural mannosylation of HIV-1 gp120 imposes no immunoregulatory effects in primary human plasmacytoid dendritic cells. Mol. Immunol 59:2 (2014), 180–187, 10.1016/j.molimm.2014.02.009.
290. Spiro, R.G., Role of n-linked polymannose oligosaccharides in targeting glycoproteins for endoplasmic reticulum-associated degradation. Cell. Mol. Life Sci 61:9 (2004), 1025–1041, 10.1007/s00018-004-4037-8.
291. Stambach, N.S., Taylor, M.E., Characterization of carbohydrate recognition by langerin, a c-type lectin of langerhans cells. Glycobiology 13:5 (2003), 401–410, 10.1093/glycob/cwg045.
292. Stanley, P., Schachter, H., Taniguchi, N., N-Glycans. Varki, A., Cummings, R.D., Esko, J.D., Freeze, H.H., Stanley, P., Bertozzi, C.R., et al. (eds.) Essentials of Glycobiology, second ed., 2009, Cold Spring Harbor (NY), New York, 101–114.
293. Strahl-Bolsinger, S., Gentzsch, M., Tanner, W., Protein o-mannosylation. Biochim. Biophys. Acta 1426:2 (1999), 297–307, 10.1016/S0304-4165(98)00131-7.
294. Su, Y., Bakker, T., Harris, J., Tsang, C., Brown, G.D., Wormald, M.R., et al. Glycosylation influences the lectin activities of the macrophage mannose receptor. J. Biol. Chem 280:38 (2005), 32811–32820, 10.1074/jbc.M503457200.
295. Swierzko, A.S., Kilpatrick, D.C., Cedzynski, M., Mannan-binding lectin in malignancy. Mol. Immunol 55:1 (2013), 16–21, 10.1016/j.molimm.2012.09.005.
296. Taganna, J., de Boer, A.R., Wuhrer, M., Bouckaert, J., Glycosylation changes as important factors for the susceptibility to urinary tract infection. Biochem. Soc. Trans 39:1 (2011), 349–354, 10.1042/BST0390349.
297. Takakura, D., Tada, M., Kawasaki, N., Membrane glycoproteomics of fetal lung fibroblasts using LC/MS. Proteomics, 2015, 10.1002/pmic.201500003.
298. Tate, M.D., Job, E.R., Deng, Y.M., Gunalan, V., Maurer-Stroh, S., Reading, P.C., Playing hide and seek: how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection. Viruses 6:3 (2014), 1294–1316, 10.3390/v6031294.
299. Taylor, M.E., Bezouska, K., Drickamer, K., Contribution to ligand binding by multiple carbohydrate-recognition domains in the macrophage mannose receptor. J. Biol. Chem 267:3 (1992), 1719–1726.
300. Taylor, P.R., Gordon, S., Martinez-Pomares, L., The mannose receptor: linking homeostasis and immunity through sugar recognition. Trends Immunol 26:2 (2005), 104–110, 10.1016/j.it.2004.12.001.
301. Te Riet, J., Reinieren-Beeren, I., Figdor, C.G., Cambi, A., AFM force spectroscopy reveals how subtle structural differences affect the interaction strength between candida albicans and DC-SIGN. J. Mol. Recognit 28:11 (2015), 687–698, 10.1002/jmr.2481.
302. Tecle, E., Gagneux, P., Sugar-coated sperm: unraveling the functions of the mammalian sperm glycocalyx. Mol. Reprod. Dev 82:9 (2015), 635–650, 10.1002/mrd.22500.
303. Teillet, F., Dublet, B., Andrieu, J.P., Gaboriaud, C., Arlaud, G.J., Thielens, N.M., The two major oligomeric forms of human mannan-binding lectin: chemical characterization, carbohydrate-binding properties, and interaction with MBL-associated serine proteases. J. Immunol 174:5 (2005), 2870–2877, 10.4049/jimmunol.174.5.2870.
304. Thaysen-Andersen, M., Packer, N.H., Site-specific glycoproteomics confirms that protein structure dictates formation of n-glycan type, core fucosylation and branching. Glycobiology 22:11 (2012), 1440–1452, 10.1093/glycob/cws110.
305. Thaysen-Andersen, M., Packer, N.H., Advances in LC-MS/MS-based glycoproteomics: getting closer to system-wide site-specific mapping of the n- and o-glycoproteome. Biochim. Biophys. Acta 1844:9 (2014), 1437–1452, 10.1016/j.bbapap.2014.05.002.
306. Thaysen-Andersen, M., Venkatakrishnan, V., Loke, I., Laurini, C., Diestel, S., Parker, B.L., et al. Human neutrophils secrete bioactive paucimannosidic proteins from azurophilic granules into pathogen-infected sputum. J. Biol. Chem 290:14 (2015), 8789–8802, 10.1074/jbc.M114.631622.
307. Thaysen-Andersen, M., Packer, N.H., Schulz, B.L., Maturing glycoproteomics technologies provide unique structural insights into the N-glycoproteome and its regulation in health and disease. Mol. Cell. Proteomics, 2016, 10.1074/mcp.O115.057638.
308. Tielker, D., Hacker, S., Loris, R., Strathmann, M., Wingender, J., Wilhelm, S., et al. Pseudomonas aeruginosa lectin LecB is located in the outer membrane and is involved in biofilm formation. Microbiology 151:Pt 5 (2005), 1313–1323, 10.1099/mic.0.27701-0.
309. Torrelles, J.B., Schlesinger, L.S., Diversity in mycobacterium tuberculosis mannosylated cell wall determinants impacts adaptation to the host. Tuberculosis (Edinb.) 90:2 (2010), 84–93, 10.1016/j.tube.2010.02.003.
310. Torrelles, J.B., DesJardin, L.E., MacNeil, J., Kaufman, T.M., Kutzbach, B., Knaup, R., et al. Inactivation of mycobacterium tuberculosis mannosyltransferase pimB reduces the cell wall lipoarabinomannan and lipomannan content and increases the rate of bacterial-induced human macrophage cell death. Glycobiology 19:7 (2009), 743–755, 10.1093/glycob/cwp042.
311. Torrelles, J.B., Sieling, P.A., Zhang, N., Keen, M.A., McNeil, M.R., Belisle, J.T., et al. Isolation of a distinct mycobacterium tuberculosis mannose-capped lipoarabinomannan isoform responsible for recognition by CD1b-restricted T cells. Glycobiology 22:8 (2012), 1118–1127, 10.1093/glycob/cws078.
312. Turner, M.W., The role of mannose-binding lectin in health and disease. Mol. Immunol 40:7 (2003), 423–429, 10.1016/s0161-5890(03)00155-x.
313. van der Graaf, C.A., Netea, M.G., Verschueren, I., van der Meer, J.W., Kullberg, B.J., Differential cytokine production and toll-like receptor signaling pathways by candida albicans blastoconidia and hyphae. Infect. Immun 73:11 (2005), 7458–7464, 10.1128/IAI.73.11.7458-7464.2005.
314. van Gisbergen, K.P., Aarnoudse, C.A., Meijer, G.A., Geijtenbeek, T.B., van Kooyk, Y., Dendritic cells recognize tumor-specific glycosylation of carcinoembryonic antigen on colorectal cancer cells through dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin. Cancer Res 65:13 (2005), 5935–5944, 10.1158/0008-5472.can-04-4140.
315. van Gisbergen, K.P., Sanchez-Hernandez, M., Geijtenbeek, T.B., van Kooyk, Y., Neutrophils mediate immune modulation of dendritic cells through glycosylation-dependent interactions between Mac-1 and DC-SIGN. J. Exp. Med 201:8 (2005), 1281–1292, 10.1084/jem.20041276.
316. van Kooyk, Y., Geijtenbeek, T.B., DC-SIGN: escape mechanism for pathogens. Nat. Rev. Immunol 3:9 (2003), 697–709, 10.1038/nri1182.
317. van Kooyk, Y., Rabinovich, G.A., Protein-glycan interactions in the control of innate and adaptive immune responses. Nat. Immunol 9:6 (2008), 593–601, 10.1038/ni.f.203.
318. van Liempt, E., Bank, C.M., Mehta, P., Garcia-Vallejo, J.J., Kawar, Z.S., Geyer, R., et al. Specificity of DC-SIGN for mannose- and fucose-containing glycans. FEBS Lett 580:26 (2006), 6123–6131, 10.1016/j.febslet.2006.10.009.
319. van Remoortere, A., Bank, C.M., Nyame, A.K., Cummings, R.D., Deelder, A.M., van Die, I., Schistosoma mansoni-infected mice produce antibodies that cross-react with plant, insect, and mammalian glycoproteins and recognize the truncated biantennary n-glycan Man3GlcNAc2-R. Glycobiology 13:3 (2003), 217–225, 10.1093/glycob/cwg025.
320. Valladeau, J., Ravel, O., Dezutter-Dambuyant, C., Moore, K., Kleijmeer, M., Liu, Y., et al. Langerin, a novel c-type lectin specific to langerhans cells, is an endocytic receptor that induces the formation of birbeck granules. Immunity 12:1 (2000), 71–81, 10.1016/S1074-7613(00)80160-0.
321. Van Antwerpen, P., Slomianny, M.-C.C., Boudjeltia, K.Z., Delporte, C., Faid, V., Calay, D., et al. Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity. J. Biol. Chem 285:21 (2010), 16351–16359, 10.1074/jbc.M109.089748.
322. Van Iwaarden, J.F., Pikaar, J.C., Storm, J., Brouwer, E., Verhoef, J., Oosting, R.S., et al. Binding of surfactant protein a to the lipid a moiety of bacterial lipopolysaccharides. Biochem. J. 303:Pt 2 (1994), 407–411.
323. Van Rooijen, J.J., Hermentin, P., Kamerling, J.P., Vliegenthart, J.F., The patterns of the complex- and oligomannose-type glycans of uromodulin (Tamm-horsfall glycoprotein) in the course of pregnancy. Glycoconj. J. 18:7 (2001), 539–546, 10.1023/A:1019644413639.
324. Vandewalle-El Khoury, P., Colombel, J.F., Joossens, S., Standaert-Vitse, A., Collot, M., Halfvarson, J., et al. Detection of antisynthetic mannoside antibodies (ASigmaMA) reveals heterogeneity in the ASCA response of Crohn's disease patients and contributes to differential diagnosis, stratification, and prediction. Am. J. Gastroenterol 103:4 (2008), 949–957, 10.1111/j.1572-0241.2007.01648.x.
325. Varga, N., Sutkeviciute, I., Ribeiro-Viana, R., Berzi, A., Ramdasi, R., Daghetti, A., et al. A multivalent inhibitor of the DC-SIGN dependent uptake of HIV-1 and dengue virus. Biomaterials 35:13 (2014), 4175–4184, 10.1016/j.biomaterials.2014.01.014.
326. Varki, A., Kornfeld, S., P-type lectins. Varki, A., Cummings, R.D., Esko, J.D., Freeze, H.H., Stanley, P., Bertozzi, C.R., et al. (eds.) Essentials of Glycobiology, second ed., 2009, Cold Spring Harbor, New York, 425–438.
327. Varki, A., Sharon, N., Historical background and overview. Varki, A., Cummings, R.D., Esko, J.D., Freeze, H.H., Stanley, P., Bertozzi, C.R., et al. (eds.) Essentials of Glycobiology, second ed., 2009, Cold Spring Harbor, New York, 1–22.
328. Varki, A., Freeze, H.H., Vacquier, V.D., Glycans in development and systemic physiology. Varki, A., Cummings, R.D., Esko, J.D., Freeze, H.H., Stanley, P., Bertozzi, C.R., et al. (eds.) Essentials of Glycobiology, second ed., 2009, Cold Spring Harbor, New York, 531–536.
329. Varki, A., Cummings, R.D., Aebi, M., Packer, N.H., Seeberger, P.H., Esko, J.D., et al. Symbol nomenclature for graphical representations of glycans. Glycobiology 25:12 (2015), 1323–1324, 10.1093/glycob/cwv091.
330. Veldhuizen, E.J., van Eijk, M., Haagsman, H.P., The carbohydrate recognition domain of collectins. FEBS J. 278:20 (2011), 3930–3941, 10.1111/j.1742-4658.2011.08206.x.
331. Venkatakrishnan, V., Packer, N.H., Thaysen-Andersen, M., Host mucin glycosylation plays a role in bacterial adhesion in lungs of individuals with cystic fibrosis. Expert Rev. Respir. Med 7:5 (2013), 553–576, 10.1586/17476348.2013.837752.
332. Venkatakrishnan, V., Thaysen-Andersen, M., Chen, S.C., Nevalainen, H., Packer, N.H., Cystic fibrosis and bacterial colonization define the sputum n-glycosylation phenotype. Glycobiology 25:1 (2015), 88–100, 10.1093/glycob/cwu092.
333. Vigerust, D.J., Shepherd, V.L., Virus glycosylation: role in virulence and immune interactions. Trends Microbiol 15:5 (2007), 211–218, 10.1016/j.tim.2007.03.003.
334. Villadangos, J.A., Schnorrer, P., Intrinsic and cooperative antigen-presenting functions of dendritic-cell subsets in vivo. Nat. Rev. Immunol 7:7 (2007), 543–555, 10.1038/nri2103.
335. Villadangos, J.A., Shortman, K., Found in translation: the human equivalent of mouse CD8+ dendritic cells. J. Exp. Med 207:6 (2010), 1131–1134, 10.1084/jem.20100985.
336. Weis, W.I., Drickamer, K., Trimeric structure of a c-type mannose-binding protein. Structure 2:12 (1994), 1227–1240, 10.1016/S0969-2126(94)00124-3.
337. Weis, W.I., Drickamer, K., Structural basis of lectin-carbohydrate recognition. Annu. Rev. Biochem 65 (1996), 441–473, 10.1146/annurev.bi.65.070196.002301.
338. Weis, W.I., Crichlow, G.V., Murthy, H.M., Hendrickson, W.A., Drickamer, K., Physical characterization and crystallization of the carbohydrate-recognition domain of a mannose-binding protein from rat. J. Biol. Chem 266:31 (1991), 20678–20686.
339. Weis, W.I., Drickamer, K., Hendrickson, W.A., Structure of a c-type mannose-binding protein complexed with an oligosaccharide. Nature 360:6400 (1992), 127–134, 10.1038/360127a0.
340. Weis, W.I., Taylor, M.E., Drickamer, K., The c-type lectin superfamily in the immune system. Immunol. Rev 163 (1998), 19–34, 10.1111/j.1600-065X.1998.tb01185.x.
341. Wellens, A., Garofalo, C., Nguyen, H., Van Gerven, N., Slattegard, R., Hernalsteens, J.P., et al. Intervening with urinary tract infections using anti-adhesives based on the crystal structure of the FimH-oligomannose-3 complex. PLoS ONE, 3(4), 2008, 10.1371/journal.pone.0002040 e2040.
342. Wells, C.A., Salvage-Jones, J.A., Li, X., Hitchens, K., Butcher, S., Murray, R.Z., et al. The macrophage-inducible c-type lectin, mincle, is an essential component of the innate immune response to candida albicans. J. Immunol 180:11 (2008), 7404–7413, 10.4049/jimmunol.180.11.7404.
343. Wells, L., The o-mannosylation pathway: glycosyltransferases and proteins implicated in congenital muscular dystrophy. J. Biol. Chem 288:10 (2013), 6930–6935, 10.1074/jbc.R112.438978.
344. Westphal, S., Kolarich, D., Foetisch, K., Lauer, I., Altmann, F., Conti, A., et al. Molecular characterization and allergenic activity of Lyc e 2 (beta-fructofuranosidase), a glycosylated allergen of tomato. Eur. J. Biochem 270:6 (2003), 1327–1337.
345. Woschnagg, C., Rubin, J., Venge, P., Eosinophil cationic protein (ECP) is processed during secretion. J. Immunol 183:6 (2009), 3949–3954, 10.4049/jimmunol.0900509.
346. Wu, G., Hitchen, P.G., Panico, M., North, S.J., Barbouche, M.R., Binet, D., et al. Glycoproteomic studies of IgE from a novel hyper IgE syndrome linked to PGM3 mutation. Glycoconj. J., 2015, 10.1007/s10719-015-9638-y.
347. Wu, L., Sampson, N.S., Fucose, mannose, and beta-n-acetylglucosamine glycopolymers initiate the mouse sperm acrosome reaction through convergent signaling pathways. ACS Chem. Biol 9:2 (2014), 468–475, 10.1021/cb400550j.
348. Xia, B., Asif, G., Arthur, L., Pervaiz, M.A., Li, X., Liu, R., et al. Oligosaccharide analysis in urine by MALDI-TOF mass spectrometry for the diagnosis of lysosomal storage diseases. Clin. Chem 59:9 (2013), 1357–1368, 10.1373/clinchem.2012.201053.
349. Xu, C., Ng, D.T., Glycosylation-directed quality control of protein folding. Nat. Rev. Mol. Cell Biol, 2015, 10.1038/nrm4073.
350. Xu, C., Ng, D.T., O-mannosylation: the other glycan player of ER quality control. Semin. Cell Dev. Biol 41 (2015), 129–134, 10.1016/j.semcdb.2015.01.014.
351. Xu, X.-L., Zhang, P., Shen, Y.-H., Li, H.-Q., Wang, Y.-H., Lu, G.-H., et al. Mannose prevents acute lung injury through mannose receptor pathway and contributes to regulate PPARγ and TGF-β1 level. Int. J. Clin. Exp. Pathol 8:6 (2015), 6214–6224.
352. Yan, H., Kamiya, T., Suabjakyong, P., Tsuji, N.M., Targeting c-type lectin receptors for cancer immunity. Front. Immunol, 6, 2015, 408, 10.3389/fimmu.2015.00408.
353. Yao, W., Peng, Y., Du, M., Luo, J., Zong, L., Preventative vaccine-loaded mannosylated chitosan nanoparticles intended for nasal mucosal delivery enhance immune responses and potent tumor immunity. Mol. Pharm 10:8 (2013), 2904–2914, 10.1021/mp4000053.
354. Yonekawa, A., Saijo, S., Hoshino, Y., Miyake, Y., Ishikawa, E., Suzukawa, M., et al. Dectin-2 Is a direct receptor for mannose-capped lipoarabinomannan of mycobacteria. Immunity 41:3 (2014), 402–413, 10.1016/j.immuni.2014.08.005.
355. Yu, S., Lowe, A.W., The pancreatic zymogen granule membrane protein, GP2, binds Escherichia coli type 1 fimbriae. BMC Gastroenterol, 9, 2009, 58, 10.1186/1471-230X-9-58.
356. Zacchi, L.F., Schulz, B.L., N-glycoprotein macroheterogeneity: biological implications and proteomic characterization. Glycoconj. J., 2015, 10.1007/s10719-015-9641-3.
357. Zelensky, A.N., Gready, J.E., The c-type lectin-like domain superfamily. FEBS J. 272:24 (2005), 6179–6217, 10.1111/j.1742-4658.2005.05031.x.
358. Zhang, W., James, P.M., Ng, B.G., Li, X., Xia, B., Rong, J., et al. A novel n-tetrasaccharide in patients with congenital disorders of glycosylation including asparagine-linked glycosylation protein 1, phosphomannomutase 2, and phosphomannose isomerase deficiencies. Clin. Chem, 2015, 10.1373/clinchem.2015.243279.
359. Zhang, X., Mosser, D.M., Macrophage activation by endogenous danger signals. J. Pathol 214:2 (2008), 161–178, 10.1002/path.2284.
360. Zhu, L.L., Zhao, X.Q., Jiang, C., You, Y., Chen, X.P., Jiang, Y.Y., et al. C-type lectin receptors dectin-3 and dectin-2 form a heterodimeric pattern-recognition receptor for host defense against fungal infection. Immunity 39:2 (2013), 324–334, 10.1016/j.immuni.2013.05.017.
361. Ziegler-Heitbrock, L., Ancuta, P., Crowe, S., Dalod, M., Grau, V., Hart, D.N., et al. Nomenclature of monocytes and dendritic cells in blood. Blood 116:16 (2010), e74–e80, 10.1182/blood-2010-02-258558.
362. Zipser, B., Bello-DeOcampo, D., Diestel, S., Tai, M.H., Schmitz, B., Mannitou monoclonal antibody uniquely recognizes paucimannose, a marker for human cancer, stemness, and inflammation. J. Carbohydr. Chem 31:4–6 (2012), 504–518, 10.1080/07328303.2012.661112.
363. Zoega, M., Ravnsborg, T., Hojrup, P., Houen, G., Schou, C., Proteinase 3 carries small unusual carbohydrates and associates with alpha-defensins. J. Proteomics 75:5 (2012), 1472–1485, 10.1016/j.jprot.2011.11.019.