A new approach makes it possible to study prokatiotic glycoproteins of uncultured bacteria

Protein glycosylation is fundamental to all three domains of life. In eukaryotes, the functions of protein glycosylation are well defined. In contrast, in prokaryotes, the situation is more unclear because of the difficulty of studying unculturable bacteria. Historically, protein glycosylation in prokaryotes was initially associated predominantly with pathogens. However, there is now a growing body of literature demonstrating that glycans play multiple roles in all different types of bacterial systems.

One curious group of prokaryotes are anaerobic ammonium oxidizing (anammox) bacteria. They play a key role in the biogeochemical nitrogen cycle. Anammox bacteria have a unique cellular appearance and a high degree of similarity with the ammonia-oxidizing Archaea, which also depend on ammonium uptake. This raises the question of characteristics at the molecular level and the potential role of the glycosylated surface layer recently discovered in anammox bacteria. 

Our amazing colleagues from the Netherlands have proposed a new systematic approach for a compositional study of prokaryotic protein glycosylation. This approach revealed a surprisingly complex set of surface layer oligosaccharides in anammox bacteria formed simultaneously by two seemingly unrelated biosynthetic pathways.

The SciBear team is proud to have participated in this remarkable research project. Our contribution was to analyze bacterial metagenomes. Our team is always happy to work with new colleagues on their amazing research projects. If you have a microbial genome analysis challenge, we look forward to a new collaboration!

The ISME Journal. 2021. doi:10.1038/s41396-021-01073-y