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Role of TbALG3 in N‐linked glycosylation of Trypanosoma brucei
Author(s) -
Manthri Sujatha,
Ferguson Michael Anthony
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a513-c
Subject(s) - trypanosoma brucei , glycosylation , biology , endoplasmic reticulum , glycoprotein , gene , antigenic variation , trypanosoma , immune system , innate immune system , microbiology and biotechnology , biochemistry , genetics
Trypanosoma brucei is a parasitic protozoan that causes African sleeping sickness in sub‐Saharan Africa. The bloodstream form has an outer coat of variant surface glycoprotein (VSG). The VSG coat acts as a defensive barrier to the host innate immune system and allows the parasite to evade the host immune system by sequential expression of different VSG genes (antigenic variation). VSGs are homodimers of ~50kDa monomers that contain 1‐3 N‐linked glycans and are attached to the plasma membrane by glycosylphosphotidylinositol membrane anchors. The N‐glycosylation pathway in the T.brucei has several unique features that might provide suitable targets for chemotherapy. Many of the enzymes that participate in N‐glycosylation pathway in the ER have been identified by bioinformatics and/or enzymology. The ALG3 gene encodes the enzyme Dol‐ P ‐Man:Man 5 GlcNAc 2 ‐ PP ‐Dol ∞‐mannosyl transferase which converts Man 5 GlcNAc 2 ‐Dol‐ PP to Man 6 GlcNAc 2 ‐Dol‐ PP . This occurs in the lumenal side of the endoplasmic reticulum. We have deleted the T.brucei ALG3 gene ( TbALG3 ) and studied the effects of this mutation on the glycosylation of the VSG glycoprotein.