# name
A gene of the beta3-glycosyltransferase family encodes
                N-acetylglucosaminyltransferase II function in Trypanosoma
                brucei

# metadata.dc.description.abstract[].value
The bloodstream form of the human pathogen Trypanosoma brucei
                expresses oligomannose, paucimannose and complex N-linked
                glycans, including some exceptionally large
                poly-N-acetyllactosamine-containing structures. Despite the
                presence of complex N-glycans in this organism, no homologues of
                the canonical N-acetylglucosaminyltransferase I or II genes can
                be found in the T. brucei genome. These genes encode the
                activities that initiate the elaboration of the Manalpha1-3 and
                Manalpha1-6 arms, respectively, of the conserved
                trimannosyl-N-acetylchitobiosyl core of N-linked glycans.
                Previously, we identified a highly divergent T. brucei
                N-acetylglucosaminyltransferase I (TbGnTI) among a set of
                putative T. brucei glycosyltransferase genes belonging to the
                beta3-glycosyltransferase superfamily (1). Here, we demonstrate
                that TbGT15, another member of the same
                beta3-glycosyltransferase family, encodes an equally divergent
                N-acetylglucosaminyltransferase II (TbGnTII) activity. In
                contrast to multicellular organisms, where GnTII activity is
                essential, TbGnTII null mutants of T. brucei grow in culture and
                are still infectious to animals. Characterization of the large
                poly-N-acetyllactosamine containing N-glycans of the TbGnTII
                null mutants by methylation linkage analysis suggests that, in
                wild-type parasites, the Manalpha1-6 arm of the conserved
                trimannosyl core may carry predominantly linear
                poly-N-acetyllactosamine chains whereas the Manalpha1-3 arm may
                carry predominantly branched poly-N-acetyllactosamine chains.
                These results provide further detail on the structure and
                biosynthesis of complex N-glycans in an important human pathogen
                and provide a second example of the adaptation by trypanosomes
                of beta3-glycosyltransferase family members to catalyze beta1-2
                glycosidic linkages.

# metadata.dc.publisher[].value
American Society for Biochemistry and Molecular Biology

# metadata.dc.relation.isformatof[].value
Reproducció del document publicat a:
                http://dx.doi.org/10.1074/jbc.M116.733246

# metadata.dc.relation.ispartof[].value
The Journal of Biological Chemistry, 2016

# metadata.dc.rights[].value
(c) American Society for Biochemistry and Molecular Biology, 2016

# metadata.dc.source[].value
Articles publicats en revistes (ISGlobal)

# metadata.dc.title[].value
A gene of the beta3-glycosyltransferase family encodes
                N-acetylglucosaminyltransferase II function in Trypanosoma
                brucei