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Identification of a glycosylphosphatidylinositol anchor-modifying β1-3 galactosyltransferase in Trypanosoma brucei.

Izquierdo L, Acosta-Serrano A, Mehlert A, Ferguson MA - Glycobiology (2014)

Bottom Line: Under nonpermissive conditions, the normal glycosylation of the major glycoprotein of bloodstream form T. brucei, the variant surface glycoprotein and the absence of major alterations in lectin binding to other glycoproteins suggested that the major function of TbGT3 occurs in the procyclic form of the parasite.Consistent with this, the major surface glycoprotein of the procyclic form, procyclin, exhibited a marked reduction in molecular weight due to changes in glycosylphosphatidylinositol (GPI) anchor side chains.Despite the alterations in GPI anchor side chains, TbGT3 conditional mutants remained infectious to tsetse flies under nonpermissive conditions.

View Article: PubMed Central - PubMed

Affiliation: Division of Biological Chemistry and Drug Discovery, The College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK Barcelona Centre for International Health Research, CRESIB, Hospital Clínic-Universitat de Barcelona, Barcelona 08036, Spain.

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Model of GPI anchor side-chain biosynthesis initiation in procyclic form trypanosomes. The first branching point in the GPI anchor side-chain is produced by TbGT8, a GlcNAc-transferase that acts on the terminal digalactose moiety of the GPI anchor (Izquierdo, Nakanishi, et al. 2009; Nakanishi et al. 2014). The resulting GPI structure can be further substituted either by (i) TbGT3 Gal-transferase, described in this paper, that adds a Gal residue to the non-reducing–t-GlcNAc or (ii) an unknown Gal-transferase, labelled as “??”, that adds a Gal-terminal residue to the α1,2-linked mannose.
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CWU131F7: Model of GPI anchor side-chain biosynthesis initiation in procyclic form trypanosomes. The first branching point in the GPI anchor side-chain is produced by TbGT8, a GlcNAc-transferase that acts on the terminal digalactose moiety of the GPI anchor (Izquierdo, Nakanishi, et al. 2009; Nakanishi et al. 2014). The resulting GPI structure can be further substituted either by (i) TbGT3 Gal-transferase, described in this paper, that adds a Gal residue to the non-reducing–t-GlcNAc or (ii) an unknown Gal-transferase, labelled as “??”, that adds a Gal-terminal residue to the α1,2-linked mannose.

Mentions: With respect to the GPI anchor modifying activity of TbGT3, we postulate that it acts on the product of TbGT8, either directly or after the action of an unknown α1-3 Gal-transferase (Figure 7).Fig. 7.


Identification of a glycosylphosphatidylinositol anchor-modifying β1-3 galactosyltransferase in Trypanosoma brucei.

Izquierdo L, Acosta-Serrano A, Mehlert A, Ferguson MA - Glycobiology (2014)

Model of GPI anchor side-chain biosynthesis initiation in procyclic form trypanosomes. The first branching point in the GPI anchor side-chain is produced by TbGT8, a GlcNAc-transferase that acts on the terminal digalactose moiety of the GPI anchor (Izquierdo, Nakanishi, et al. 2009; Nakanishi et al. 2014). The resulting GPI structure can be further substituted either by (i) TbGT3 Gal-transferase, described in this paper, that adds a Gal residue to the non-reducing–t-GlcNAc or (ii) an unknown Gal-transferase, labelled as “??”, that adds a Gal-terminal residue to the α1,2-linked mannose.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4339879&req=5

CWU131F7: Model of GPI anchor side-chain biosynthesis initiation in procyclic form trypanosomes. The first branching point in the GPI anchor side-chain is produced by TbGT8, a GlcNAc-transferase that acts on the terminal digalactose moiety of the GPI anchor (Izquierdo, Nakanishi, et al. 2009; Nakanishi et al. 2014). The resulting GPI structure can be further substituted either by (i) TbGT3 Gal-transferase, described in this paper, that adds a Gal residue to the non-reducing–t-GlcNAc or (ii) an unknown Gal-transferase, labelled as “??”, that adds a Gal-terminal residue to the α1,2-linked mannose.
Mentions: With respect to the GPI anchor modifying activity of TbGT3, we postulate that it acts on the product of TbGT8, either directly or after the action of an unknown α1-3 Gal-transferase (Figure 7).Fig. 7.

Bottom Line: Under nonpermissive conditions, the normal glycosylation of the major glycoprotein of bloodstream form T. brucei, the variant surface glycoprotein and the absence of major alterations in lectin binding to other glycoproteins suggested that the major function of TbGT3 occurs in the procyclic form of the parasite.Consistent with this, the major surface glycoprotein of the procyclic form, procyclin, exhibited a marked reduction in molecular weight due to changes in glycosylphosphatidylinositol (GPI) anchor side chains.Despite the alterations in GPI anchor side chains, TbGT3 conditional mutants remained infectious to tsetse flies under nonpermissive conditions.

View Article: PubMed Central - PubMed

Affiliation: Division of Biological Chemistry and Drug Discovery, The College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK Barcelona Centre for International Health Research, CRESIB, Hospital Clínic-Universitat de Barcelona, Barcelona 08036, Spain.

Show MeSH
Related in: MedlinePlus