Agl28 and Agl29 are key components of a Halobacterium salinarum N-glycosylation pathway

Zlata Vershinin, Marianna Zaretsky, Ziqiang Guan, Jerry Eichler

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


Although Halobacterim salinarum provided the first example of N-glycosylation outside the Eukarya, only recently has attention focused on delineating the pathway responsible for the assembly of the N-linked tetrasaccharide decorating selected proteins in this haloarchaeon. In the present report, the roles of VNG1053G and VNG1054G, two proteins encoded by genes clustered together with a set of genes demonstrated to encode N-glycosylation pathway components, were considered. Relying on both bioinformatics and gene deletion and subsequent mass spectrometry analysis of known N-glycosylated proteins, VNG1053G was determined to be the glycosyltransferase responsible for addition of the linking glucose, while VNG1054G was deemed to be the flippase that translocates the lipid-bound tetrasaccharide across the plasma membrane to face the cell exterior, or to contribute to such activity. As observed with Hbt. salinarum lacking other components of the N-glycosylation machinery, both cell growth and motility were compromised in the absence of VNG1053G or VNG1054G. Thus, given their demonstrated roles in Hbt. salinarum N-glycosylation, VNG1053G and VNG1054G were re-annotated as Agl28 and Agl29, according to the nomenclature used to define archaeal N-glycosylation pathway components.

Original languageEnglish
Article numberfnad017
JournalFEMS Microbiology Letters
StatePublished - 2 Mar 2023


  • Halobacterium salinarum
  • N-glycosylation
  • archaea
  • glycoproteins
  • glycosyltransferase

ASJC Scopus subject areas

  • General Medicine


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