Willems, Esther, Gloerich, Jolein, Suppers, Anouk, van der Flier, Michiel, van den Heuvel, Lambert P, van de Kar, Nicole, Philipsen, Ria HLA, van Dael, Maurice, Kaforou, Myrsini, Wright, Victoria J et al (show 9 more authors)
(2023)
Impact of infection on proteome-wide glycosylation revealed by distinct signatures for bacterial and viral pathogens.
iScience, 26 (8).
107257-.
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Impact of infection on proteome-wide glycosolation signature I Science 2023.pdf - Open Access published version Download (5MB) | Preview |
Abstract
Mechanisms of infection and pathogenesis have predominantly been studied based on differential gene or protein expression. Less is known about posttranslational modifications, which are essential for protein functional diversity. We applied an innovative glycoproteomics method to study the systemic proteome-wide glycosylation in response to infection. The protein site-specific glycosylation was characterized in plasma derived from well-defined controls and patients. We found 3862 unique features, of which we identified 463 distinct intact glycopeptides, that could be mapped to more than 30 different proteins. Statistical analyses were used to derive a glycopeptide signature that enabled significant differentiation between patients with a bacterial or viral infection. Furthermore, supported by a machine learning algorithm, we demonstrated the ability to identify the causative pathogens based on the distinctive host blood plasma glycopeptide signatures. These results illustrate that glycoproteomics holds enormous potential as an innovative approach to improve the interpretation of relevant biological changes in response to infection.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PERFORM consortium |
| Divisions: | Faculty of Health and Life Sciences Faculty of Health and Life Sciences > Institute of Infection, Veterinary and Ecological Sciences |
| Depositing User: | Symplectic Admin |
| Date Deposited: | 05 Aug 2023 15:22 |
| Last Modified: | 17 Mar 2024 23:39 |
| DOI: | 10.1016/j.isci.2023.107257 |
| Related URLs: | |
| URI: | https://livrepository.liverpool.ac.uk/id/eprint/3172061 |
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