Articles of Significant Interest In This Issue

Abstract

During N-glycosylation in the archaeon Haloferax volcanii, AglD charges the lipid dolichol phosphate (DolP) with mannose, which is then delivered to a protein-bound tetrasaccharide, yielding the N-linked pentasaccharide that decorates glycoproteins in this organism. Relative to other DolP-mannose synthases, AglD contains an extended C-terminal membrane-spanning domain. By creating AglD variants with truncations of this domain, Zaretsky et al. (e00447-21) could separate the ability of AglD to catalyze mannose charging of DolP from a role for this protein in subsequent delivery of mannose to the asparagine-linked tetrasaccharide. Thus, different regions of AglD appear to serve distinct roles in N-glycosylation.