Add salt, add sugar: N-glycosylation in Haloferax volcanii

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

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


Although performed by members of all three domains of life, the archaeal version of N-glycosylation remains the least understood. Studies on Haloferax volcanii have, however, begun to correct this situation. A combination of bioinformatics, molecular biology, biochemical and mass spectrometry approaches have served to delineate the Agl pathway responsible for N-glycosylation of the S-layer glycoprotein, a reporter of this post-translationalmodification in Hfx. volcanii.More recently, differential N-glycosylation of the S-layer glycoprotein as a function of environmental salinity was demonstrated, showing that this post-translational modification serves an adaptive role in Hfx. volcanii. Furthermore, manipulation of the Agl pathway, together with the capability of Hfx. volcanii to N-glycosylate nonnative proteins, forms the basis for establishing this species as a glyco-engineering platform. In the present review, these and other recent findings are addressed.

Original languageEnglish
Pages (from-to)432-435
Number of pages4
JournalBiochemical Society Transactions
Issue number1
StatePublished - 1 Feb 2013


  • Archaea
  • Haloferax volcanii
  • N-glycosylation
  • Post-translational modification
  • Proteomic diversity

ASJC Scopus subject areas

  • Biochemistry


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