Novel loci associated with plasma immunoglobulin G N-glycosylation identified by a multivariate analysis

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Alexandra S. Shadrina1, Alexander S. Zlobin2, Olga O. Zaytseva3, Gordan Lauc4, Lucija Klaric5, Sodbo Z. Sharapov6, Yurii S. Aulchenko7, Yakov A. Tsepilov8
1Laboratory of Glycogenomics, Institute of Cytology and Genetics, Novosibirsk, Russia, weiner.alexserg@gmail.com
2Laboratory of Recombination and Segregation Analysis, Institute of Cytology and Genetics, Novosibirsk, Russia, defrag12@gmail.com
3Genos Glycoscience Research Laboratory, Zagreb, Croatia, lomur00@gmail.com
4Genos Glycoscience Research Laboratory, Zagreb, Croatia, glauc@genos.hr
5MRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, United Kingdom, Lucija.Klaric@ed.ac.uk
6Laboratory of Glycogenomics, Institute of Cytology and Genetics, Novosibirsk, Russia, sharapovsodbo@gmail.com
7Laboratory of Glycogenomics, Institute of Cytology and Genetics, Novosibirsk, Russia, y.s.aulchenko@polyomica.com
8Laboratory of Theoretical and Applied Functional Genomics, Novosibirsk State University, Novosibirsk, Russia, drosophila.simulans@gmail.com

Immunoglobulin G (IgG) is the most prevalent human plasma N-glycosylated protein, which makes a significant impact into the total plasma protein glycosylation profile. Glycosylation of IgG is known to affect its biological properties; for example, sialylation of glycans attached to IgG is known to have an anti-inflammatory effect, while the absence of a core fucose in the IgG glycan structure can increase antigen-dependent cell cytotoxicity. The biochemical processes underlying protein glycosylation are well-studied; at the same time, little is known about biological network regulating these reactions. In the present study, we performed a multivariate analysis based on the summary statistics obtained in the previously published IgG N-glycome GWAS in order to discover new loci influencing IgG N-glycosylation patterns. We revealed thirty-four loci associated with the levels of plasma IgG N-glycosylation. Of these loci, eight loci have not been reported in previous works. Our results significantly expand the number of identified IgG N-glycome-associated loci and contribute to understanding the mechanisms of the genetic control of glycosylation.

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elgaeva.liza@yandex.ru
Elizaveta Elgaeva
4 years ago

1. What was the 9th group of traits (I could not find it on the second slide)?
2. How did you test for association with each group? Was the association with initial traits checked at first followed by assigning to the specific group?

Alexandra Shadrina
Alexandra Shadrina
4 years ago

Thank you for your questions
1) The 9th group is BisectingGlcNAc, you can see it if you press Zoom “-” button;
2) The traits were combined in the groups first (as in Shen et al. study, doi:10.1038/s41467-017-00453-3), and then MANOVA results were obtained using the summary statistics-based method described by Ning et al. (doi:10.1101/022269)

elgaeva.liza@yandex.ru
Elizaveta Elgaeva
4 years ago

Alexandra, thank you for your answer.

1) Oh, yes, noe I can see it, thank you.

2) Thank you for the provided links, I will look through them.

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2 months ago

Novel loci associated with plasma immunoglobulin G N-glycosylation identified by a multivariate analysis

https://korea-page.com/우주-탐사선의-역사와-발전-과정/