Severe allergic reactions to certain types of meat following tick bites have been reported in geographic regions which are endemic with ticks. This immune response is directed to a carbohydrate... Show moreSevere allergic reactions to certain types of meat following tick bites have been reported in geographic regions which are endemic with ticks. This immune response is directed to a carbohydrate antigen (galactose-alpha-1,3-galactose or alpha-Gal), which is present in glycoproteins of mammalian meats. At the moment, asparagine-linked complex carbohydrates (N-glycans) with alpha-Gal motifs in meat glycoproteins and in which cell types or tissue morphologies these alpha-Gal moieties are present in mammalian meats are still unclear. In this study, we analyzed alpha-Gal-containing N-glycans in beef, mutton, and pork tenderloin and provided for the first time the spatial distribution of these types of N-glycans in various meat samples. Terminal alpha-Gal-modified N-glycans were found to be highly abundant in all analyzed samples (55, 45, and 36% of N-glycome in beef, mutton, and pork, respectively). Visualizations of the N-glycans with alpha-Gal modification revealed that this motif was mainly present in the fibroconnective tissue. To conclude, this study contributes to a better understanding of the glycosylation biology of meat samples and provides guidance for processed meat products, in which only meat fibers are required as an ingredient (i.e., sausages or canned meat). Show less
Vreeker, G.C.M.; Bladergroen, M.R.; Nicolardi, S.; Mesker, W.E.; Tollenaar, R.A.E.M.; Burgt, Y.E.M. van der; Wuhrer, M. 2019
In this thesis, methods were developed, and antibody glycosylation was characterized in order to further the clinical application of antibody glycosylation analysis. New mass spectrometric... Show moreIn this thesis, methods were developed, and antibody glycosylation was characterized in order to further the clinical application of antibody glycosylation analysis. New mass spectrometric workflows were introduced in Chapters 2 and 8. Chapter 7 showed the differential characteristics of murine IgG glycosylation of different strains and highlighted the profound differences between humans and mice, with regard to IgG glycosylation. Chapters 4 and 8 showed the use of controlled human situations to study the regulatory mechanisms of IgG and IgA glycosylation. Finally, Chapters 3, 5 and 6, identified glycosidic differences with specified (patho)physiological conditions, which might be exploited for patient stratification in the future. Show less
Dotz, V.; Lemmers, R.F.H.; Reiding, K.R.; Ederveen, A.L.H.; Lieverse, A.G.; Mulder, M.T.; ... ; Hoek, M. van 2018
Glycosylation on the fragment crystallizable (Fc) region of immunoglobulin G (IgG) has a large influence on the interaction of the antibody with Fc gamma receptors (Fc gamma Rs). IgG consists of... Show moreGlycosylation on the fragment crystallizable (Fc) region of immunoglobulin G (IgG) has a large influence on the interaction of the antibody with Fc gamma receptors (Fc gamma Rs). IgG consists of four subclasses that all have distinct affinities for the different Fc gamma Rs. Knowledge about the Fc-glycosylation in healthy human is valuable as reference for new biomarkers and in the design of biopharmaceuticals that rely on IgG Fc-glycosylation. Previously, subclass-specific characterization of IgG Fc-glycosylation was performed for healthy adults, pregnant women, and newborns. For young healthy children, however, the subclass-specific description of IgG Fc-glycosylation is still lacking. Therefore, we performed the IgG subclass-specific analysis of the Fc-glycosylation of 130 healthy humans between birth and 40 years of age, including 22 samples derived from the umbilical cords of newborns. The analysis was performed by a previously published matrix-assisted laser desorption/ionization (MALDI)-time-of-flight (TOF)-mass spectrometry (MS) workflow, including a derivatization step for the linkage-specific stabilization of sialic acids. The characterization revealed that when children start to produce their own IgG they have a decreased galactosylation, sialylation, and bisection and an increased fucosylation compared with newborns. During childhood, the fucosylation and sialylation decrease, whereas bisection increases and galactosylation stays constant. Show less
Borelli, V.; Vanhooren, V.; Lonardi, E.; Reiding, K.R.; Capri, M.; Libert, C.; ... ; Wuhrer, M. 2015
