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Gewählte Publikation:

Publikationstyp: Zeitschriftenaufsatz
Dokumentart: Originalarbeit

Publikationsjahr: 2018

AutorInnen: Yan, S; Wang, H; Schachter, H; Jin, C; Wilson, IBH; Paschinger, K

Titel: Ablation of N-acetylglucosaminyltransferases in Caenorhabditis induces expression of unusual intersected and bisected N-glycans.

Quelle: Biochim Biophys Acta Gen Subj. 2018; 1862(10):2191-2203

Autor/innen der Vetmeduni Vienna:

Yan Shi

Beteiligte Vetmed-Organisationseinheiten
Institut für Parasitologie

Zugehörige(s) Projekt(e): Biosynthese von Wurm N-Glykoproteinen in Insektenzellen

The modification in the Golgi of N-glycans by N-acetylglucosaminyltransferase I (GlcNAc-TI, MGAT1) can be considered to be a hallmark of multicellular eukaryotes as it is found in all metazoans and plants, but rarely in unicellular organisms. The enzyme is key for the normal processing of N-glycans to either complex or paucimannosidic forms, both of which are found in the model nematode Caenorhabditis elegans. Unusually, this organism has three different GlcNAc-TI genes (gly-12, gly-13 and gly-14); therefore, a complete abolition of GlcNAc-TI activity required the generation of a triple knock-out strain. Previously, the compositions of N-glycans from this mutant were described, but no detailed structures. Using an off-line HPLC-MALDI-TOF-MS approach combined with exoglycosidase digestions and MS/MS, we reveal that the multiple hexose residues of the N-glycans of the gly-12;gly-13;gly-14 triple mutant are not just mannose, but include galactoses in three different positions (β-intersecting, β-bisecting and α-terminal) on isomeric forms of Hex

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