Impact of infection on proteome-wide glycosylation revealed by distinct signatures for bacterial and viral pathogens
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...
| Main Authors: | , , , , , , , , , , , , , , , , , |
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| Other Authors: | |
| Format: | Journal article |
| Language: | English |
| Published: |
Cell Press
2023
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| _version_ | 1797111034702462976 |
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| author | Willems, E Gloerich, J Suppers, A van der Flier, M van den Heuvel, LP van de Kar, N Philipsen, RHLA van Dael, M Kaforou, M Wright, VJ Herberg, JA Torres, FM Levin, M de Groot, R van Gool, AJ Lefeber, DJ Wessels, HJCT de Jonge, MI |
| author2 | PERFORM consortium |
| author_facet | PERFORM consortium Willems, E Gloerich, J Suppers, A van der Flier, M van den Heuvel, LP van de Kar, N Philipsen, RHLA van Dael, M Kaforou, M Wright, VJ Herberg, JA Torres, FM Levin, M de Groot, R van Gool, AJ Lefeber, DJ Wessels, HJCT de Jonge, MI |
| author_sort | Willems, E |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-07T08:03:04Z |
| format | Journal article |
| id | oxford-uuid:0f5e1e7e-58fb-4070-9397-6c074acb89f0 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T08:03:04Z |
| publishDate | 2023 |
| publisher | Cell Press |
| record_format | dspace |
| spelling | oxford-uuid:0f5e1e7e-58fb-4070-9397-6c074acb89f02023-10-17T10:12:13ZImpact of infection on proteome-wide glycosylation revealed by distinct signatures for bacterial and viral pathogensJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:0f5e1e7e-58fb-4070-9397-6c074acb89f0EnglishSymplectic ElementsCell Press2023Willems, EGloerich, JSuppers, Avan der Flier, Mvan den Heuvel, LPvan de Kar, NPhilipsen, RHLAvan Dael, MKaforou, MWright, VJHerberg, JATorres, FMLevin, Mde Groot, Rvan Gool, AJLefeber, DJWessels, HJCTde Jonge, MIPERFORM consortiumPollard, AJMechanisms 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. |
| spellingShingle | Willems, E Gloerich, J Suppers, A van der Flier, M van den Heuvel, LP van de Kar, N Philipsen, RHLA van Dael, M Kaforou, M Wright, VJ Herberg, JA Torres, FM Levin, M de Groot, R van Gool, AJ Lefeber, DJ Wessels, HJCT de Jonge, MI Impact of infection on proteome-wide glycosylation revealed by distinct signatures for bacterial and viral pathogens |
| title | Impact of infection on proteome-wide glycosylation revealed by distinct signatures for bacterial and viral pathogens |
| title_full | Impact of infection on proteome-wide glycosylation revealed by distinct signatures for bacterial and viral pathogens |
| title_fullStr | Impact of infection on proteome-wide glycosylation revealed by distinct signatures for bacterial and viral pathogens |
| title_full_unstemmed | Impact of infection on proteome-wide glycosylation revealed by distinct signatures for bacterial and viral pathogens |
| title_short | Impact of infection on proteome-wide glycosylation revealed by distinct signatures for bacterial and viral pathogens |
| title_sort | impact of infection on proteome wide glycosylation revealed by distinct signatures for bacterial and viral pathogens |
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