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MALDI-TOF-MS reveals differential N -linked plasma- and IgG-glycosylation profiles between mothers and their newborns

View Article: PubMed Central - PubMed

ABSTRACT

During pregnancy, the mother provides multiple nutrients and substances to the foetus, with maternal immunoglobulin G (IgG) being actively transported to the foetus. Newborns depend on maternal IgG for immune-protection in their first months. The glycosylation of IgG has been shown to influence its dynamics, e.g. receptor binding. While minor differences in IgG glycosylation have been found between IgG derived from maternal blood and umbilical cord blood (UC) of newborn children, the differential glycosylation of maternal and UC plasma has hitherto not been studied. Here, we studied the N-glycosylation of IgG and total plasma proteome of both maternal and UC plasma of 42 pairs of mothers and newborn children. A total of 37 N-glycans were quantified for IgG and 45 for the total plasma N-glycome (TPNG). The study showed slightly higher levels of galactosylation for UC IgG than maternal IgG, confirming previous results, as well as lower bisection and sialylation. Furthermore, the TPNG results showed lower values for galactosylation and sialylation, and higher values for fucosylation in the UC plasma. In conclusion, this study presents some novel insights into IgG glycosylation differences as well as the first broad overview of the differential plasma glycosylation between mothers and newborns.

No MeSH data available.


Glycosylation differences between maternal and UC IgG.The level in both maternal and UC IgG of each individual pair and boxplots for the entire group are displayed. The figure displays 4 calculated derived traits; (A) % galactosylation of diantennary compositions, (B) % bisection of diantennary compositions, (C) % sialylation of diantennary compositions and (D) % sialylation per galactose of diantennary compositions.
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f2: Glycosylation differences between maternal and UC IgG.The level in both maternal and UC IgG of each individual pair and boxplots for the entire group are displayed. The figure displays 4 calculated derived traits; (A) % galactosylation of diantennary compositions, (B) % bisection of diantennary compositions, (C) % sialylation of diantennary compositions and (D) % sialylation per galactose of diantennary compositions.

Mentions: A total of 37 glycoforms was quantified from the purified IgG (Fig. 1; Supplementary Table S1), followed by a Wilcoxon signed-rank test for comparing maternal and UC IgG glycosylation features. Multiple testing correction was performed by Bonferroni adjustment of the significance threshold. This showed for the UC lower levels of the agalactosylated and some monogalactosylated glycans H3N4F1 (mother versus UC: 6.3% vs. 4.8%; p = 1.4∙10−8), H3N5F1 (2.3% vs. 1.9%; p = 1.2∙10−5), H4N4F1E1 (2.4% vs. 1.9%; p = 4.9∙10−7), while other monogalactosylated and digalactosylated structures showed higher levels in UC: H4N5F1 (mother versus UC: 5.6% vs. 6.1%, p = 1.2∙10−5), H5N4 (2.0% vs. 2.4%, p = 5.0∙10−5) and H5N4F1 (23.2% vs. 25.8%, p = 2.6∙10−6). A total of 7 derived traits reflecting specific glycosylation features were calculated from the individual glycans (Supplementary Table S2). These derived traits also showed a higher level of galactosylation for UC (A2G; mother versus UC: 73.0% vs. 75.2%; p = 8.6∙10−8; Fig. 2A), and conversely a lower level of agalactosylation (TaGal, 9.8% vs. 7.8%; p = 3.6∙10−6), matching the previously described change in agalactosylation1213. Three additional traits were lower in UC, which were bisection (A2B; 16.7% vs. 15.6%; p = 3.9∙10−5; Fig. 2B), sialylation (A2S; 19.0% vs. 17.5%; p = 2.1∙10−3; Fig. 2C) and sialylation per galactose (A2GS; 26.1% vs. 23.3%; p-value = 5.0∙10−5; Fig. 2D). All mentioned derived traits were calculated following normalisation to the total area of diantennary complex type glycan compositions. A summary of the derived glycosylation trait results is presented in Table 1. The box plots presented for the derived traits (Fig. 2) also show the differences between maternal and UC plasma on a pair-wise basis, as indicated with the coloured lines.


MALDI-TOF-MS reveals differential N -linked plasma- and IgG-glycosylation profiles between mothers and their newborns
Glycosylation differences between maternal and UC IgG.The level in both maternal and UC IgG of each individual pair and boxplots for the entire group are displayed. The figure displays 4 calculated derived traits; (A) % galactosylation of diantennary compositions, (B) % bisection of diantennary compositions, (C) % sialylation of diantennary compositions and (D) % sialylation per galactose of diantennary compositions.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC5036037&req=5

f2: Glycosylation differences between maternal and UC IgG.The level in both maternal and UC IgG of each individual pair and boxplots for the entire group are displayed. The figure displays 4 calculated derived traits; (A) % galactosylation of diantennary compositions, (B) % bisection of diantennary compositions, (C) % sialylation of diantennary compositions and (D) % sialylation per galactose of diantennary compositions.
Mentions: A total of 37 glycoforms was quantified from the purified IgG (Fig. 1; Supplementary Table S1), followed by a Wilcoxon signed-rank test for comparing maternal and UC IgG glycosylation features. Multiple testing correction was performed by Bonferroni adjustment of the significance threshold. This showed for the UC lower levels of the agalactosylated and some monogalactosylated glycans H3N4F1 (mother versus UC: 6.3% vs. 4.8%; p = 1.4∙10−8), H3N5F1 (2.3% vs. 1.9%; p = 1.2∙10−5), H4N4F1E1 (2.4% vs. 1.9%; p = 4.9∙10−7), while other monogalactosylated and digalactosylated structures showed higher levels in UC: H4N5F1 (mother versus UC: 5.6% vs. 6.1%, p = 1.2∙10−5), H5N4 (2.0% vs. 2.4%, p = 5.0∙10−5) and H5N4F1 (23.2% vs. 25.8%, p = 2.6∙10−6). A total of 7 derived traits reflecting specific glycosylation features were calculated from the individual glycans (Supplementary Table S2). These derived traits also showed a higher level of galactosylation for UC (A2G; mother versus UC: 73.0% vs. 75.2%; p = 8.6∙10−8; Fig. 2A), and conversely a lower level of agalactosylation (TaGal, 9.8% vs. 7.8%; p = 3.6∙10−6), matching the previously described change in agalactosylation1213. Three additional traits were lower in UC, which were bisection (A2B; 16.7% vs. 15.6%; p = 3.9∙10−5; Fig. 2B), sialylation (A2S; 19.0% vs. 17.5%; p = 2.1∙10−3; Fig. 2C) and sialylation per galactose (A2GS; 26.1% vs. 23.3%; p-value = 5.0∙10−5; Fig. 2D). All mentioned derived traits were calculated following normalisation to the total area of diantennary complex type glycan compositions. A summary of the derived glycosylation trait results is presented in Table 1. The box plots presented for the derived traits (Fig. 2) also show the differences between maternal and UC plasma on a pair-wise basis, as indicated with the coloured lines.

View Article: PubMed Central - PubMed

ABSTRACT

During pregnancy, the mother provides multiple nutrients and substances to the foetus, with maternal immunoglobulin G (IgG) being actively transported to the foetus. Newborns depend on maternal IgG for immune-protection in their first months. The glycosylation of IgG has been shown to influence its dynamics, e.g. receptor binding. While minor differences in IgG glycosylation have been found between IgG derived from maternal blood and umbilical cord blood (UC) of newborn children, the differential glycosylation of maternal and UC plasma has hitherto not been studied. Here, we studied the N-glycosylation of IgG and total plasma proteome of both maternal and UC plasma of 42 pairs of mothers and newborn children. A total of 37 N-glycans were quantified for IgG and 45 for the total plasma N-glycome (TPNG). The study showed slightly higher levels of galactosylation for UC IgG than maternal IgG, confirming previous results, as well as lower bisection and sialylation. Furthermore, the TPNG results showed lower values for galactosylation and sialylation, and higher values for fucosylation in the UC plasma. In conclusion, this study presents some novel insights into IgG glycosylation differences as well as the first broad overview of the differential plasma glycosylation between mothers and newborns.

No MeSH data available.