Naslov
N-glycosylation of plasma proteins and immunoglobulin G in multiple sclerosis

Autori
Cvetko, Ana ; Kifer, Domagoj ; Wilson, Jim ; Lauc, Gordan ; Pavić, Tamara

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Skup
GlycoT 2020 12th International Symposium on Glycosyltransferases

Mjesto i datum
Boston (MA), Sjedinjene Američke Države, 21.06.2020. - 23.06.2020

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
N-glycosylation, IgG, plasma proteins, multiple sclerosis

Sažetak
Multiple sclerosis (MS), a disease affecting the central nervous system, is characterized by demyelination and inflammation. Mechanism underlying the development of MS is not yet fully understood, but it is considered to be influenced by both genetic and environmental factors. N- glycosylation is one of the most complex co- and post-translational modifications and a highly regulated process. N-glycans do not only increase protein structural diversity, but can modify their function as well. Multiple studies have shown the importance of N-glycan changes in different autoimmune and inflammatory diseases, which highlights N-glycans as potential diagnostic and/or prognostic biomarkers. Even though plasma protein and immunoglobulin G (IgG) N-glycosylation changes are well investigated in many diseases, the studies on N-glycan changes in multiple sclerosis are scarce. Hence, we aimed to investigate N-glycosylation patterns of plasma proteins and IgG in multiple sclerosis. We have analysed plasma and IgG N-glycosylation profiles in 83 multiple sclerosis cases, 88 age- and sex- matched controls and 85 sex-matched controls, but who passed the majority of lifetime risk for MS development (>70 years of age). Core fucosylation showed to be the most prominently altered IgG glycosylation trait, as it was significantly decreased in MS subjects compared to the healthy controls (adjusted p=0.0069). Among all generated plasma glycosylation traits, the most significant changes were observed in antennary fucosylated and high branched N-glycans, which were both increased in the MS group (adjusted p=0.0067 and 0.0219, respectively). On the other hand, low branched N-glycans were significantly decreased in MS subjects (adjusted p=0.0167). Our results demonstrated that plasma protein and IgG N- glycosylation markedly changes in multiple sclerosis. However, additional studies are needed to determine the background of these changes, their role in multiple sclerosis development and their potential use as diagnostic biomarkers.

Izvorni jezik
Engleski

POVEZANOST RADA