References
- Khan, D. A. Allergic rhinitis and asthma: epidemiology and common pathophysiology. Allergy Asthma. Proc. 2014, 35(5), 357–361. DOI: https://doi.org/10.2500/aap.2014.35.3794.
- Steiner, I.; Sobieska, M.; Pucher, B.; Grzegorowski, M.; Samborski, W. Examination of acute phase proteins concentrations in children with allergic rhinitis. Ann. Acad. Med. Stetin. 2006, 52(2), 33–37.
- Emeryk, A.; Emeryk-Maksymiuk, J.; Janeczek, K. New guidelines for the treatment of seasonal allergic rhinitis. Postepy. Dermatol. Alergol. 2019, 36(3), 255–260. DOI: https://doi.org/10.5114/ada.2018.75749.
- Calderon, M. A.; Alves, B.; Jacobson, M.; Hurwitz, B.; Sheikh, A.; Durham, S. Allergen injection immunotherapy for seasonal allergic rhinitis. Cochrane Database Syst. Rev. 2007, 5(3), 1279–1379. DOI: https://doi.org/10.1002/14651858.CD001936.pub2.
- Reily, C.; Stewart, T. J.; Renfrow, M.; Novak, B. J. Glycosylation in health and disease. Nat. Rev. Nephrol. 2019, 15(6), 346–366. DOI: https://doi.org/10.1038/s41581-019-0129-4.
- Taylor, M. E.; Drickamer, K. Introduction to Glycobiology. Oxford University Press: Oxford 2011.
- Varki, A. Biological roles of glycans. Glycobiology. 2017, 27(1), 3–49. DOI: https://doi.org/10.1093/glycob/cww086.
- Peracaula, R.; Barrabés, S.; Sarrats, A.; Rudd, P. M.; de Llorens, R. Altered glycosylation in tumours focused to cancer diagnosis. Dis. Markers. 2008, 25(4–5), 207–218. DOI: https://doi.org/10.1155/2008/797629.
- Ghazarian, H.; Idoni, B.; Oppenheimer, S. B. A glycobiology review: carbohydrates, lectins and implications in cancer therapeutics. Acta Histochem. 2011, 113(3), 236–247. DOI: https://doi.org/10.1016/j.acthis.2010.02.004.
- Rudd, P. M.; Wormald, M. R.; Dwek, R. A. Sugar-mediated ligand-receptor interactions in the immune system. Trends Biotechnol. 2004, 22(10), 524–530. DOI: https://doi.org/10.1016/j.tibtech.2004.07.012.
- Monticelli, M.; Ferro, T.; Jaeken, J.; dos Reis Ferreira, V.; Videira, P. A. Immunological aspects of congenital disorders of glycosylation (CDG): a review. J. Inherit. Metab. Dis. 2016, 39(6), 765–780. DOI: https://doi.org/10.1007/s10545-016-9954-9.
- Altmann, F. The role of protein glycosylation in allergy. Int. Arch. Allergy Immunol. 2007, 142(2), 99–115.
- Garrido-Arandia, M.; Murua-García, A.; Palacin, A.; Tordesillas, L.; Gómez-Casado, C.; Blanca-Lopez, N.; Ramos, T.; Canto, G.; Blanco, C.; Cuesta-Herranz, J.; et al. The role of N-glycosylation in kiwi allergy. Food. Sci. Nutr. 2014, 2(3), 260–271. DOI: https://doi.org/10.1002/fsn3.99.
- Do, D. C.; Yang, S.; Yao, X.; Hamilton, R. G.; Schroeder, J.; Gao, T. P. N-glycan in cockroach allergen regulates human basophil function. Immun. Inflamm. Dis. 2017, 5(4), 386–399. DOI: https://doi.org/10.1002/iid3.145.
- Epp, A.; Sullivan, K. C.; Herr, A. B.; Strait, R. T. Immunoglobulin glycosylation effects in allergy and immunity. Curr. Allergy Asthma Rep. 2016, 16(11), 1–13. DOI: https://doi.org/10.1007/s11882-016-0658-x.
- Shade, K. -T.; Conroy, M. E.; Anthony, R. M. IgE glycosylation in health and disease. Curr. Top. Microbiol. Immunol. 2019, 423, 77–93. DOI: https://doi.org/10.1007/82_2019_151.
- Shade, K. -T. C.; Conroy, M. E.; Washburn, N.; Kitaoka, M.; Huynh, D. J.; Laprise, E.; Patil, S. U.; Shreffler, W. G.; Anthony, R. M. Sialylation of immunoglobulin E is a determinant of allergic pathogenicity. Nature. 2020, 582(7811), 265–270. DOI: https://doi.org/10.1038/s41586-020-2311-z.
- Reiding, K. R.; Blank, D.; Kuijper, D. M.; Deelder, A.; Wuhrer, M. M. High-throughput profiling of protein N-glycosylation by MALDI-TOF-MS employing linkage-specific sialic acid esterification. Anal. Chem. 2014, 86(12), 5784–5793. DOI: https://doi.org/10.1021/ac500335t.
- Selman, M. H.; Hemayatkar, M.; Deelder, A.; Wuhrer, M. M. Cotton HILIC SPE microtips for microscale purification and enrichment of glycans and glycopeptides. Anal. Chem. 2011, 83(7), 2492–2499. DOI: https://doi.org/10.1021/ac1027116.
- Suckau, D.; Resemann, A.; Schuerenberg, M.; Hufnagel, P.; Franzen, J.; Holle, A. A novel MALDI LIFT-TOF/TOF mass spectrometer for proteomics. Anal. Bioanal. Chem. 2003, 376(7), 952–965. DOI: https://doi.org/10.1007/s00216-003-2057-0.
- Jansen, B. C.; Reiding, K. R.; Bondt, A.; Hipgrave Ederveen, A. L.; Palmblad, M.; Falck, D.; Wuhrer, M. MassyTools: a high-throughput targeted data processing tool for relative quantitation and quality control developed for glycomic and glycoproteomic MALDI-MS. J Proteome Res. 2015, 14(12), 5088–5098. DOI: https://doi.org/10.1021/acs.jproteome.5b00658.
- Team, R. C. R: A language and environment for statistical computing. 2013.
- Ceroni, A.; Maass, K.; Geyer, H.; Geyer, R.; Dell, A.; Haslam, S. M. GlycoWorkbench: a tool for the computer-assisted annotation of mass spectra of glycans. J. Proteome. Res. 2008, 7(4), 1650–1659. DOI: https://doi.org/10.1021/pr7008252.
- Jansen, B. C.; Bondt, A.; Reiding, K. R.; Scherjon, S. A.; Vidarsson, G.; Wuhrer, M. MALDI-TOF-MS reveals differential N-linked plasma- and IgG-glycosylation profiles between mothers and their newborns. Sci. Rep. 2016, 6, 34001. DOI: https://doi.org/10.1038/srep34001.
- Büyüköztürk, S.; Gelincik, A. A.; Genç, S.; Koçak, H.; Öneriyidogan, Y.; Erden, S.; Dal, M.; Çolakoglu, B. Acute phase reactants in allergic airway disease. Tohoku. J. Exp. Med. 2004, 204(3), 209–213. DOI: https://doi.org/10.1620/tjem.204.209.
- Bhide, G. P.; Colley, K. J. Sialylation of N-glycans: mechanism, cellular compartmentalization and function. Histochem. Cell. Biol. 2017, 147(2), 149–174. DOI: https://doi.org/10.1007/s00418-016-1520-x.
- Pearce, O. M.; Läubli, H. Sialic acids in cancer biology and immunity. Glycobiology. 2016, 26(2), 111–128. DOI: https://doi.org/10.1093/glycob/cwv097.
- Xie, M. M.; Bertozzi, C. R.; Wang, T. T. Immunoglobulin E sialylation regulates allergic responses. Immunol. Cell. Biol. 2020, 98(8), 617–619. DOI: https://doi.org/10.1111/imcb.12368.
- King, C. L.; Poindexter, R. W.; Ragunathan, J.; Fleisher, T. A.; Ottesen, E. A.; Nutman, T. B. Frequency analysis of IgE-secreting B lymphocytes in persons with normal or elevated serum IgE levels. J. Immunol. 1991, 146(5), 1478–1483.
- Ghory, A.; Patterson, R.; Roberts, M.; Suszko, I. In vitro IgE formation by peripheral blood lymphocytes from normal individuals and patients with allergic bronchopulmonary aspergillosis. Clin. Exp. Immunol. 1980, 40(3), 581–585.
- Varki, A. Sialic acids in human health and disease. Trends. Mol. Med. 2008, 14(8), 351–360. DOI: https://doi.org/10.1016/j.molmed.2008.06.002.
- Scherer, H. U.; van der Woude, D.; Ioan-Facsinay, A.; el Bannoudi, H.; Trouw, L. A.; Wang, J.; Häupl, T.; Burmester, G. -R.; Deelder, A. M.; Huizinga, T. W. J.; et al. Glycan profiling of anti–citrullinated protein antibodies isolated from human serum and synovial fluid. Arthritis. Rheum. 2010, 62(6), 1620–1629.
- Ackerman, M. E.; Crispin, M.; Yu, X.; Baruah, K.; Boesch, A. W.; Harvey, D. J.; Dugast, A. -S.; Heizen, E. L.; Ercan, A.; Choi, I.; et al. Natural variation in Fc glycosylation of HIV-specific antibodies impacts antiviral activity. J. Clin. Invest. 2013, 123(5), 2183–2192. DOI: https://doi.org/10.1172/JCI65708.
- Novak, J.; Moldoveanu, Z.; Renfrow, M. B.; Yanagihara, T.; Suzuki, H.; Raska, M.; Hall, S.; Brown, R.; Huang, W. -Q.; Goepfert, A. IgA nephropathy and Henoch-Schoenlein purpura nephritis: aberrant glycosylation of IgA1, formation of IgA1-containing immune complexes, and activation of mesangial cells. IgA. Nephropathy. Today. 2007, 157, 134–138.
- Matsumoto, A.; Shikata, K.; Takeuchi, F.; KojimaN.; Mizuochi, T. Autoantibody activity of IgG rheumatoid factor increases with decreasing levels of galactosylation and sialylation. J. Biochem. 2000, 128(4), 621–628. DOI: https://doi.org/10.1093/oxfordjournals.jbchem.a022794.
- Maverakis, E.; Kim, K.; Shimoda, M.; Gershwin, M. E.; Patel, F.; Wilken, R.; Raychaudhuri, S.; Ruhaak, L. R.; Lebrilla, C. B. Glycans in the immune system and The Altered Glycan Theory of Autoimmunity: a critical review. J. Autoimmun. 2015, 57, 1–13.
- Mehta, A.; Norton, P.; Liang, H.; Comunale, M. A.; Wang, M.; Rodemich-Betesh, L.; Koszycki, A.; Noda, K.; Miyoshi, E.; Block, E. T. Increased levels of tetra-antennary N-linked glycan but not core fucosylation are associated with hepatocellular carcinoma tissue. Cancer Epidemiol. Biomarkers. Prev. 2012, 21(6), 925–933. DOI: https://doi.org/10.1158/1055-9965.EPI-11-1183.
- Arnold, J. N.; Saldova, R.; Hamid, U. M. A.; Rudd, P. M. Evaluation of the serum N-linked glycome for the diagnosis of cancer and chronic inflammation. Proteomics. 2008, 8(16), 3284–3293. DOI: https://doi.org/10.1002/pmic.200800163.
- Stanley, P.; Taniguchi, N.; Aebi, M. N-glycans. Essentials of Glycobiology [Internet]. 3rd edition. Cold Spring Harbor Laboratory Press: Cold Spring Harbor 2017.
- Srivastava, O. P.; Hindsgaul, O.; Shoreibah, M.; Pierce, M. M. Pierce recognition of oligosaccharide substrates by N-acetylglucosaminyltransferase-V. Carbohydr. Res. 1988, 179, 137–161. DOI: https://doi.org/10.1016/0008-6215(88)84115-6.