Proteomics

Dataset Information

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Anammox enrichment culture glycoproteomics


ABSTRACT: The physiology of the planctomycetal anammox bacteria makes them particularly special because they share features with all three domains of life. Anammox bacteria have been reported recently to produce surface-layer proteins, which represent the outermost layer and provide structure, shape and protection under extreme conditions. Furthermore, we report on the unique cell surface-layer glycosylation of the anammox bacterium Ca. Kuenenia stuttgartiensis as revealed by a newly established glycoproteomics approach. This approach enables untargeted exploration of prokaryotic protein glycosylation from (high-resolution) shotgun proteomics data directly.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Candidatus Brocadia Sapporoensis Candidatus Kuenenia Stuttgartiensis

SUBMITTER: Martin Pabst  

LAB HEAD: Dr. Martin Pabst

PROVIDER: PXD021600 | Pride | 2021-08-05

REPOSITORIES: Pride

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Publications

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

Pabst Martin M   Grouzdev Denis S DS   Lawson Christopher E CE   Kleikamp Hugo B C HBC   de Ram Carol C   Louwen Rogier R   Lin Yue Mei YM   Lücker Sebastian S   van Loosdrecht Mark C M MCM   Laureni Michele M  

The ISME journal 20210802 2


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 iden  ...[more]

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