A prognostic value of the study of the exposure of glycosyl determinants to IgG molecules in the blood serum of patients with multiple sclerosis depending on the performed drug therapy

M.O. Boichuk, T.I. Nehrych, R.O. Bilyy


Background. The definition of antibodies to the body’s own antigens is of great importance in autoimmune processes in multiple sclerosis. The functions of immunoglobulins (Ig) are determined by the composition of the biomolecules of glycan residues attached to the N-glycosylated domain in the crystallizing fragment (Fc region) of the immunoglobulin heavy chains. The changes in the structure of glycans are believed to be able to affect the functioning of Ig. So, the presence or absence of certain carbohydrate residues in the composition of antibodies is associated with their pro- or anti-inflammatory properties. In turn, this modifies the course of inflammatory reactions in autoimmune diseases and can determine the activity of multiple sclerosis. Therefore, studies of structural changes in the blood serum Ig of patients with multiple sclerosis is of great clinical importance. Materials and methods. The serum samples of 6 cohorts of patients with multiple sclerosis was sdudied depending on the group of the drug of the disease-modifying therapy that the patients were taking. Namely, 17 patients, prior to the time of blood sampling for these studies, had never received any therapy; 15 patients with multiple sclerosis received disease-modifying therapy with drugs from the interferon group β-1b; 12 people received pulse therapy with methylpredni-solone at a dose of 1000 mg for 5–7 days; 12 patients with multiple sclerosis of different sexes and ages received therapy with drugs from the group of monoclonal antibodies, namely ocrelizumab at a dose of 600 mg once per 6 months; 9 people received glatiramer acetate at a dose of 40 mg three times a week; 10 patients with multiple sclerosis were treated with teriflunomide at a dose of 14 mg
once a day; there were 23 healthy individuals. Results. The results of the studies demonstrated that various types of therapy impact the change in the immunoglobulins glycosyl determinants. Conclusions. Glycan markers can be used as high-sensitive and specific biomarkers for diagnosing multiple sclerosis and predicting its course.


multiple sclerosis; IgG; glycosylation


Begum F. Immunology. Immunology. 2014. 71-82.

Jefferis R., Lund J., Mizutani H. et al. A comparative study of the N-linked oligosaccharide structures of human IgG subclass proteins. Biochem. J. 1990. 268. 529-537. Available from:

Wormald M.R., Rudd P.M., Harvey D.J. et al. Variations in oligosaccharide-protein interactions in immunoglobulin G determine the site-specific glycosylation profiles and modulate the dynamic motion of the Fc oligosaccharides. Biochemistry. 1997. 36. 1370-1380. Available from:

Stadlmann J., Pabst M., Altmann F. Analytical and Functional Aspects of Antibody Sialylation. J. Clin. Immunol. 2010. 30. 15-19. Available from:

Kaneko Y., Nimmerjahn F., Ravetch J.V. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science. 2006. 313. 670-673. Available from:

Nimmerjahn F., Anthony R.M., Ravetch J.V. Agalactosylated IgG antibodies depend on cellular Fc receptors for in vivo activity. Proc. Natl. Acad. Sci. USA. 2007. 104. 8433-8437. Available from:


Nimmerjahn F., Ravetch J.V. Antibody-mediated modulation of immune responses. Immunol. Rev. 2010. 236. 265-275. Available from:

Lux A., Nimmerjahn F. Impact of differential glycosylation on IgG activity. Adv. Exp. Med. Biol. 2011. 780. 113-124. Available from:


Nimmerjahn F., Gordan S., Lux A. FcγR dependent mechanisms of cytotoxic, agonistic, and neutralizing antibody activities. Trends Immunol. 2015. 36. 325-336.

Jefferis R. Glycosylation as a strategy to improve antibody-based therapeutics. Nat. Rev. Drug Discov. 2009. 8. 226-234. Avai-lable from:

Wahl A., van den Akker E., Klaric L. et al. Genome-Wide Association Study on Immunoglobulin G Glycosylation Patterns. Front. Immunol. 2018. 9. 277. Available from:

Lauc G., Vučković F., Bondt A. et al. Trace N-glycans inclu-ding sulphated species may originate from various plasma glycoproteins and not necessarily IgG. Nat. Commun. 2018. 9. 2916. Available from:

Trbojević-Akmačić I., Vilaj M., Lauc G. High-throughput analysis of immunoglobulin G glycosylation. Expert Rev. Proteomics. 2016. 13. 523-534. Available from:

Dubé R., Rook G.A.W., Steele J. et al. Agalactosyl IgG in inflammatory bowel disease: Correlation with C-reactive protein. Gut. 1990. 31. 431-434.

Mehta A.S., Long R.E., Comunale M.A. et al. Increased Le-vels of Galactose-Deficient Anti-Gal Immunoglobulin G in the Sera of Hepatitis C Virus-Infected Individuals with Fibrosis and Cirrhosis. J. Virol. 2008. 82. 1259-1270. Available from:

Parekh R., Roitt I., Isenber D. et al. Age-Related Galactosylation of the N-Linked Oligosaccharides of Human Serum IgG. J. Exp. Med. 2015. 212. 457-467. Available from:

Van de Geijn F.E., Wuhrer M., Selman M.H.J. et al. Immunoglobulin G galactosylation and sialylation are associated with pregnancy-induced improvement of rheumatoid arthritis and the postpartum flare: Results from a large prospective cohort study. Arthritis Res. Ther. 2009. 11. R193.

Biermann M.H.C., Griffante G., Podolska M.J. et al. Sweet but dangerous — the role of immunoglobulin G glycosylation in autoimmunity and inflammation. Lupus. 2016. 25. 934-942. Available from:

Магорівська І.Б., Томін А.М., Думич Т.І. и др. Спосіб оцінки параметрів молекул імуноглобуліну класу IgG у зразках сироватки крові. UA, UA: Патент України на корисну модель 95297. 2014. 1-6.

Tateno H., Winter H.C., Goldstein I.J. Cloning, expression in Escherichia coli and characterization of the recombinant Neu5Acalpha2,6Galbeta1,4GlcNAc-specific high-affinity lectin and its mutants from the mushroom Polyporus squamosus. Biochem. J. 2004. 382. 667-675.

Baumann I., Kolowos W., Voll R.E. et al. Impaired uptake of apoptotic cells into tingible body macrophages in germinal centers of patients with systemic lupus erythematosus. Arthritis Rheum. 2002. 46. 191-201. Available from:

Scherer H.U., van der Woude D., Ioan-Facsinay A. et al. Glycan profiling of anti-citrullinated protein antibodies isolated from human serum and synovial fluid. Arthritis Rheum. 2010. 62. 1620-1629. Available from:

Blauth K., Owens G.P., Bennett J.L. The Ins and Outs of B Cells in Multiple Sclerosis. Front. Immunol. 2015. 6. 1-7. Avai-lable from:


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