Expression of rat β(1,4)-N-acetylglucosaminyltransferase III in Nicotiana tabacum remodels the plant-specific N-glycosylation

Alexander D. Frey, Saskia R. Karg, Pauli T. Kallio

Research output: Contribution to journalArticleScientificpeer-review

45 Citations (Scopus)


Plant N-linked glycans differ substantially from their mammalian counterparts, mainly with respect to modifications of the core glycan, which typically contains a β(1,2)-xylose and an α(1,3)-fucose. The addition of a bisecting N-acetylglucosamine residue by β(1,4)-N- acetylglucosaminyltransferase III (GnTIII) is known to control the processing of N-linked glycans in mammals, for example by preventing α(1,6)- fucosylation of the core glycan. In order to outcompete plant-specific β(1,2)-xylose and α(1,3)-fucose modifications, rat GnTIII was expressed either with its native localization domain (GnTIII) or with the cytoplasmic tail, transmembrane domain and stem region (CTS) of Arabidopsis thaliana mannosidase II (ManII) ( Both CTSs targeted enhanced yellow fluorescent protein (eYFP) to a brefeldin A-sensitive compartment, indicative of Golgi localization. GnTIII expression increased the fraction of N-glycans devoid of xylose and fucose from 13% ± 7% in wild-type plants to 60% ± 8% in plants expressing N-Glycans of plants expressing rat GnTIII contained three major glycan structures of complex bisected, complex, or hybrid bisected type, accounting for 70%-85% of the total N-glycans. On expression of, N-glycans displayed a higher heterogeneity and were of hybrid type. Co-expression of A. thaliana ManII significantly increased the amount of complex bisected structures relative to the plants expressing GnTIII or GnTIII, whereas co-expression of human ManII did not redirect the pool of hybrid structures towards complex-type structures. The method described offers the advantage that it can be implemented in any desired plant system for effective removal of β(1,2)-xylose and α(1,3)-fucose from the N-glycan.

Original languageEnglish
Pages (from-to)33-48
Number of pages16
Issue number1
Publication statusPublished - Jan 2009
MoE publication typeA1 Journal article-refereed


  • α(1,3)-fucose
  • β(1,2)-xylose
  • β(1,4)-N- acetylglucosaminyltransferase III
  • Glycoengineering
  • Localization
  • Plant N-linked glycosylation


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