Comprehensive glycoproteomics shines new light on the complexity and extent of glycosylation in archaea

Stefan Schulze, Friedhelm Pfeiffer, Benjamin A. Garcia, Mechthild Pohlschroder

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


Glycosylation is one of the most complex posttranslational protein modifications. Its importance has been established not only for eukaryotes but also for a variety of prokaryotic cellular processes, such as biofilm formation, motility, and mating. However, comprehensive glycoproteomic analyses are largely missing in prokaryotes. Here, we extend the phenotypic characterization of N-glycosylation pathway mutants in Haloferax volcanii and provide a detailed glycoproteome for this model archaeon through the mass spectrometric analysis of intact glycopeptides. Using in-depth glycoproteomic datasets generated for the wild-type (WT) and mutant strains as well as a reanalysis of datasets within the Archaeal Proteome Project (ArcPP), we identify the largest archaeal glycoproteome described so far. We further show that different N-glycosylation pathways can modify the same glycosites under the same culture conditions. The extent and complexity of the Hfx. volcanii N-glycoproteome revealed here provide new insights into the roles of N-glycosylation in archaeal cell biology.

Original languageEnglish
Article numbere3001277
JournalPLoS biology
Issue number6
StatePublished - Jun 2021


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