N-glycosylation in Haloferax volcanii: Adjusting the sweetness

Jerry Eichler, Adi Arbiv, Chen Cohen-Rosenzweig, Lina Kaminski, Lina Kandiba, Zvia Konrad

Research output: Contribution to journalShort surveypeer-review

17 Scopus citations


Long believed to be restricted to Eukarya, it is now known that cells of all three domains of life perform N-glycosylation, the covalent attachment of glycans to select target protein asparagine residues. Still, it is only in the last decade that pathways of N-glycosylation in Archaea have been delineated. In the haloarchaeon Haloferax volcanii, a series of Agl (archaeal glycosylation) proteins is responsible for the addition of an N-linked pentasaccharide to modified proteins, including the surface (S)-layer glycoprotein, the sole component of the surface layer surrounding the cell. The S-layer glycoprotein N-linked glycosylation profile changes, however, as a function of surrounding salinity. Upon growth at different salt concentrations, the S-layer glycoprotein is either decorated by the N-linked pentasaccharide introduced above or by both this pentasaccharide as well as a tetrasaccharide of distinct composition. Recent efforts have identified Agl5-Agl15 as components of a second Hfx. volcanii N-glycosylation pathway responsible for generating the tetrasaccharide attached to S-layer glycoprotein when growth occurs in 1.75 M but not 3.4 M NaCl-containing medium.

Original languageEnglish
JournalFrontiers in Microbiology
Issue numberDEC
StatePublished - 1 Jan 2013


  • Archaea
  • Haloferax volcanii
  • N-glycosylation
  • Post-translational modification
  • Protein glycosylation
  • S-layer glycoprotein

ASJC Scopus subject areas

  • Microbiology
  • Microbiology (medical)


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