A broadly active fucosyltransferase LmjFUT1 whose mitochondrial localization and catalytic activity is essential in the parasitic protozoan Leishmania
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References
Protein O-fucosyltransferase 2 adds O-fucose to thrombospondin type 1 repeats.
Post-translational modification of cellular proteins during Leishmania donovani differentiation
Function and assembly of the Leishmania surface coat.
Clinical pleiomorphism in human leishmaniases, with special mention of asymptomatic infection.
Ether phospholipids and glycosylinositolphospholipids are not required for amastigote virulence or for inhibition of macrophage activation by Leishmania major.
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Frequently Asked Questions (2)
Q2. What have the authors stated for future works in "A broadly active fucosyltransferase lmjfut1 whose mitochondrial localization and catalytic activity is essential in the parasitic protozoan leishmania" ?
Future studies will address this possibility. Future studies will be necessary to resolve the nature of the GDP-Fucose and FUT1dependent product ( s ) in trypanosomatids, which genetic and biochemical data strongly predict must nonetheless exist. Potentially, trypanosomatid mitochondrial FUT1s may offer a facile system in the future for probing mitochondrial glycosylation in a setting uncomplicated by multiple isoforms targeted to diverse compartments, and its essentiality renders it an attractive target for chemotherapy of trypanosomatid parasites. L. donovani expresses a mannose-fucose conjugate whose structure has not been definitively established ( 33 ), and several L. donovani proteins exhibited MS/MS signatures suggestive of fucosylation ( 34 ).