Phylogenetic- and genome-derived insight into the evolution of N-glycosylation in Archaea

Lina Kaminski, Mor N. Lurie-Weinberger, Thorsten Allers, Uri Gophna, Jerry Eichler*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

46 Scopus citations


N-glycosylation, the covalent attachment of oligosaccharides to target protein Asn residues, is a post-translational modification that occurs in all three domains of life. In Archaea, the N-linked glycans that decorate experimentally characterized glycoproteins reveal a diversity in composition and content unequaled by their bacterial or eukaryal counterparts. At the same time, relatively little is known of archaeal N-glycosylation pathways outside of a handful of model strains. To gain insight into the distribution and evolutionary history of the archaeal version of this universal protein-processing event, 168 archaeal genome sequences were scanned for the presence of aglB, encoding the known archaeal oligosaccharyltransferase, an enzyme key to N-glycosylation. Such analysis predicts the presence of AglB in 166 species, with some species seemingly containing multiple versions of the protein. Phylogenetic analysis reveals that the events leading to aglB duplication occurred at various points during archaeal evolution. In many cases, aglB is found as part of a cluster of putative N-glycosylation genes. The presence, arrangement and nucleotide composition of genes in aglB-based clusters in five species of the halophilic archaeon Haloferax points to lateral gene transfer as contributing to the evolution of archaeal N-glycosylation.

Original languageEnglish
Pages (from-to)327-339
Number of pages13
JournalMolecular Phylogenetics and Evolution
Issue number2
StatePublished - Aug 2013


FundersFunder number
German-Israeli Project Cooperation
US Army Research Office201/12, W911NF-11-1-520
Royal Society
Israel Science Foundation30/07


    • Archaea
    • N-glycosylation
    • Oligosaccharyltransferase


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