Identification and functional characterization of a highly divergent N-acetylglucosaminyltransferase I (TbGnTI) in Trypanosoma brucei

Manuela Damerow, Joao A. Rodrigues, Di Wu, M. Lucia S. Güther, Angela Mehlert, Michael A. J. Ferguson (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    16 Citations (Scopus)
    185 Downloads (Pure)


    Trypanosoma brucei expresses a diverse repertoire of N-glycans, ranging from oligomannose and paucimannose structures to exceptionally large complex N-glycans. Despite the presence of the latter, no obvious homologues of known ß1-4-galactosyltransferase or ß1-2- or ß1-6-N-acetylglucosaminyltransferase genes have been found in the parasite genome. However, we previously reported a family of putative UDP-sugar-dependent glycosyltransferases with similarity to the mammalian ß1-3-glycosyltransferase family. Here we characterize one of these genes, TbGT11, and show that it encodes a Golgi apparatus resident UDP-GlcNAc:a3-D-mannoside ß1-2-N-acetylglucosaminyltransferase I activity (TbGnTI). The bloodstream-form TbGT11 null mutant exhibited significantly modified protein N-glycans but normal growth in vitro and infectivity to rodents. In contrast to multicellular organisms, where the GnTI reaction is essential for biosynthesis of both complex and hybrid N-glycans, T. brucei TbGT11 null mutants expressed atypical "pseudohybrid" glycans, indicating that TbGnTII activity is not dependent on prior TbGnTI action. Using a functional in vitro assay, we showed that TbGnTI transfers UDP-GlcNAc to biantennary Man3GlcNAc2, but not to triantennary Man5GlcNAc2, which is the preferred substrate for metazoan GnTIs. Sequence alignment reveals that the T. brucei enzyme is far removed from the metazoan GnTI family and suggests that the parasite has adapted the ß3-glycosyltransferase family to catalyze ß1-2 linkages.

    Original languageEnglish
    Pages (from-to)9328-9339
    Number of pages12
    JournalJournal of Biological Chemistry
    Issue number13
    Publication statusPublished - 28 Mar 2014


    • Blood
    • Cell Line
    • Glycosylation
    • Golgi Apparatus
    • Humans
    • Mutation
    • N-Acetylglucosaminyltransferases
    • Phenotype
    • Polysaccharides
    • Protein Transport
    • Substrate Specificity
    • Trypanosoma brucei brucei
    • Uridine Diphosphate


    Dive into the research topics of 'Identification and functional characterization of a highly divergent N-acetylglucosaminyltransferase I (TbGnTI) in Trypanosoma brucei'. Together they form a unique fingerprint.

    Cite this