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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.


IgG glycan MALDI-TOF-MS spectra of maternal and UC origin.(A) Maternal IgG glycome and (B) UC IgG glycome. IgG was captured from plasma, followed by a glycan release and derivatisation as described in literature43. The glycan structures that are shown are based on the most common glycan structures in healthy human IgG47. The displayed maternal and UC samples are of a matching pair.
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f1: IgG glycan MALDI-TOF-MS spectra of maternal and UC origin.(A) Maternal IgG glycome and (B) UC IgG glycome. IgG was captured from plasma, followed by a glycan release and derivatisation as described in literature43. The glycan structures that are shown are based on the most common glycan structures in healthy human IgG47. The displayed maternal and UC samples are of a matching pair.

Mentions: Released glycans from purified IgG and total plasma from paired maternal and UC origin were measured by matrix-assisted laser desorption/ionisation (MALDI)-time-of-flight (TOF)-mass spectrometry (MS) (Fig. 1).


MALDI-TOF-MS reveals differential N -linked plasma- and IgG-glycosylation profiles between mothers and their newborns
IgG glycan MALDI-TOF-MS spectra of maternal and UC origin.(A) Maternal IgG glycome and (B) UC IgG glycome. IgG was captured from plasma, followed by a glycan release and derivatisation as described in literature43. The glycan structures that are shown are based on the most common glycan structures in healthy human IgG47. The displayed maternal and UC samples are of a matching pair.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

f1: IgG glycan MALDI-TOF-MS spectra of maternal and UC origin.(A) Maternal IgG glycome and (B) UC IgG glycome. IgG was captured from plasma, followed by a glycan release and derivatisation as described in literature43. The glycan structures that are shown are based on the most common glycan structures in healthy human IgG47. The displayed maternal and UC samples are of a matching pair.
Mentions: Released glycans from purified IgG and total plasma from paired maternal and UC origin were measured by matrix-assisted laser desorption/ionisation (MALDI)-time-of-flight (TOF)-mass spectrometry (MS) (Fig. 1).

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.