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Impact of infection on proteome-wide glycosylation revealed by distinct signatures for bacterial and viral pathogens.

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.

SUBMITTER: Willems E

PROVIDER: S-EPMC10384227 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature

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Impact of infection on proteome-wide glycosylation revealed by distinct signatures for bacterial and viral pathogens.

Willems Esther E Gloerich Jolein J Suppers Anouk A van der Flier Michiel M van den Heuvel Lambert P LP van de Kar Nicole N Philipsen Ria H L A RHLA van Dael Maurice M Kaforou Myrsini M Wright Victoria J VJ Herberg Jethro A JA Torres Federico Martinon FM Levin Michael M de Groot Ronald R van Gool Alain J AJ Lefeber Dirk J DJ Wessels Hans J C T HJCT de Jonge Marien I MI

iScience 20230704 8

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 ...[more]

PMID: 37520696

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Dataset Information

Impact of infection on proteome-wide glycosylation revealed by distinct signatures for bacterial and viral pathogens.

Publications

Impact of infection on proteome-wide glycosylation revealed by distinct signatures for bacterial and viral pathogens.

Similar Datasets

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