A general approach to explore prokaryotic protein glycosylation reveals the unique surface layer modulation of an anammox bacterium.

ABSTRACT: The enormous chemical diversity and strain variability of prokaryotic protein glycosylation makes their large-scale exploration exceptionally challenging. Therefore, despite the universal relevance of protein glycosylation across all domains of life, the understanding of their biological significance and the evolutionary forces shaping oligosaccharide structures remains highly limited. Here, we report on a newly established mass binning glycoproteomics approach that establishes the chemical identity of the carbohydrate components and performs untargeted exploration of prokaryotic oligosaccharides from large-scale proteomics data directly. We demonstrate our approach by exploring an enrichment culture of the globally relevant anaerobic ammonium-oxidizing bacterium Ca. Kuenenia stuttgartiens

SUBMITTER: Pabst M 

PROVIDER: S-EPMC8776859 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature