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

SUBMITTER: Willems E 

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

REPOSITORIES: biostudies-literature