Naslov
Immunoglobulin G glycosylation profiles in patients with influenza and bacterial pneumonia

Autori
Kljakovic-Gaspic Batinjan, Marina ; Civljak, Rok ; Markotic, Alemka ; Lauc, Gordan ; Huljev, Eva

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, neobjavljeni rad, ostalo

Skup
European Congress of Clinical Microbiology and Infectious Diseases

Mjesto i datum
Amsterdam, Nizozemska, 13.04.2019. - 16.04.2019

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
influenza, bacterial pneumonia, glycosylation, immunoglobulin G

Sažetak
Background: Acute respiratory tract infections, especially influenza and bacterial pneumonia, are among the leading causes of morbidity and mortality. Immunoglobulin G (IgG) plays an important role in protecting the human organism from pathogens and is an example of glycoprotein whose function is regulated by glycosylation. The aim of the study was to compare glycosylation profiles of IgG in patients with influenza and bacterial pneumonia. Materials/methods: A survey was conducted in adult patients hospitalized at the University Hospital for Infectious Diseases, Zagreb, due to acute respiratory tract infection. On three occasions (1st, 7th and 28th day after admission), the Hydrophilic Interaction Liquid Chromatography-Ultra High Performance Liquid Chromatography (HILIC-UHPLC) method was used to determine the glycosylation profile of IgG in the serum of all subjects. The results were compared with the glycosylation profile of 35 controls, which were matched by age and sex. We used a linear mixed model to analyze N- glycoprotein changes in time. We analyzed each of the 3 groups individually. P values were corrected for multiple assays using the Benjamini-Hochberg method. Results: The study included 36 adult patients, of whom 13 had influenza, and 23 bacterial pneumonia. Regarding galactose, in influenza the IgG glycome is changed toward more anti- inflammatory IgG activity ; there are a statistically significant decrease of agalactosylated structures (p < 0, 05) which are repeatedly associated with inflammation and an increase of sialylated moieties (p < 0, 01) associated with IgG anti-inflammation activity. Contrary, in pneumonia digalactosylated structures decrease (p < 0, 02) thus promoting IgG pro-inflammatory activity and acting contrary to the observed changes in influenza. Regarding bisecting N-acetylglucosamine (GlcNAc), a statistically significant decrease (p < 0.001) is observed in pneumonia which leads to enhanced anti-inflammatory activity of IgG and is in opposite to decreased digalactosylation, while bisecting GlcNAc remains unchanged in influenza. Conclusions: Differences in IgG glycome isolated from patients with influenza and pneumonia clearly indicate that IgG glycosylation is affected by distinct molecular pathways underlying the diseases. IgG glycosylation in influenza and bacterial pneumonia patients differs from the glycosylation profile of healthy subjects. Determination of the glycosylation profile of IgG could have a diagnostic and prognostic value.

Izvorni jezik
Engleski

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