Naslov
Fc-linked N-glycosylation of IgG subclasses in three mouse strains analyzed with nanoUPLC-ESI-MS

Autori
Zaitseva, Olga ; Jansen, Bas ; Stojković, Ranko ; Pezer, Marija ; Lauc, Gordan

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
EuPA School on Practical Proteomics 2017 : Abstract book / - , 2017, 27-27

Skup
1st EuPA School on Practical Proteomics

Mjesto i datum
Split, Hrvatska, 08.10.2017. - 12.10.2017

Vrsta sudjelovanja
Poster

Vrsta recenzije
Podatak o recenziji nije dostupan

Ključne riječi
IgG glycosylation ; mouse ; nanoUPLC-ESI-MS

Sažetak
Biological activity of immunoglobulin G (IgG) is heavily influenced by the biantennary N-glycans attached to the heavy chains of the fragment crystallizable (Fc). The four IgG subclasses recognized in humans and mice differ both in amino acid composition and in their Fc-region N- glycosylation profiles. The aim of the project is to compare N-glycosylation profiles of the Fc- region of IgG subclasses in three commonly used mouse strains. IgG was isolated from the serum of individual sex- and aged-matched mice of BALB/c, C57BL/6 and C3H strains kept in the same environment. The obtained IgG tryptic glycopeptides corresponding to the Fc region of the four mouse IgG subclasses were separated with nano ultra-performance liquid chromatography and quantified with electrospray ionization mass spectrometry (nanoUPLC-ESI-MS) method. We compared several derived N-glycan traits, describing the relative abundance of N- glycan structural features. We observed differences in Fc-linked N-glycosylation profiles both between mouse strains and between IgG subclasses. Interstingly, the C57BL/6 mice carying a rare IgG1 allotype characterized by a Phe -> Ile substitution in the tryptic Fc-glycopeptide showed increased agalactosylation and reduced sialylation of IgG1 compared to BALB/c and C3H strains. Our next goal is to develop a technique for relative quantification of the IgG allotypes in our experimental setup to determine if they are expressed on equal levels in the heterozygous individuals and if their N-glycosylation profiles are different. We plan to further investigate the connection between the abundance of known IgG allotypes and their N-glycosylation profiles, with a particular focus on known IgG1, IgG2b and IgG2c allelic polymorphism in mice and IgG3 in humans, which will require integration of proteomics, genomics and glycomics data.

Izvorni jezik
Engleski

Znanstvena područja
Biologija, Temeljne medicinske znanosti

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