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Authors
Honkpehedji, Yabo J.
Kildemoes, Anna O.
Stam, Koen A.
Nguyen, Dieu L.
Veldhuizen, Tom
van Diepen, Angela
Esen, Meral
Kremsner, Peter G.
Wuhrer, Manfred
Adegnika, Ayôla A.
Hokke, Cornelis H.
Yazdanbakhsh, Maria
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Funding
Funding for this research was provided by:
German Federal Ministry of Education and Research (01KA1307, 01KA1307)
European and Developing Countries Clinical Trials Partnership (2015-1045)
European Health and Digital Executive Agency (101080784)
Dutch Research Council (SPI.2021.004)
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Article History
Received: 18 September 2024
Accepted: 13 December 2024
First Online: 30 December 2024
Declarations
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: The authors declare no competing interests.
: All participants gave their written informed consent before their inclusion in the study. The study was conducted in accordance with the Declaration of Helsinki and was approved by the Institutional Ethical Committee of the CERMEL (CEI-CERMEL Nº13/2013).
: The principal component analysis was performed on all available antibody glycosylation data measured in this study. As variables, we included the main derived traits on the different IgG isotypes, namely galactosylation, bisection, fucosylation and sialylation of IgG1, IgG2 and IgG3/IgG4. Lastly, these variables were scaled to unit variance. The percentage of glycan structures between samples was compared using an unmatched two-sample Wilcoxon test. The identified low/medium/high group of glycosylation for the different traits was based on splitting the values into three equal-sized quantiles for each sample type. To compare these quantiles over time, each sample origin (cord blood, child 9 months, child 12 months) was compared to the mother with Fischer’s exact test for a 3 × 3 table. Using the ‘stats’ package, the statistical test was performed in R (4.3.1), and p-values < 0.05 were considered statistically significant.
