Abstract
For virulence and transmission, the protozoan parasite Leishmania must assemble a complex glycolipid on the cell surface, the lipophosphoglycan (LPG). Functional complementation identified the gene LPG2, which encodes an integral Golgi membrane protein implicated in intracellular compartmentalization of LPG biosynthesis. Ipg2- mutants lack only characteristic disaccharide-phosphate repeats, normally present on both LPG and other surface or secreted molecules considered critical for infectivity. In contrast, a related yeast gene, VAN2/VRG4, is essential and required for general Golgi function. These results suggest that LPG2 participates in a specialized virulence pathway, which may offer an attractive target for chemotherapy.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Carbohydrate Sequence
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Cell Compartmentation
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Genes, Fungal
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Genes, Protozoan*
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Genetic Complementation Test
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Glycosphingolipids / biosynthesis*
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Glycosphingolipids / chemistry
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Glycosphingolipids / genetics
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Glycosphingolipids / physiology*
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Glycosylation
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Golgi Apparatus / metabolism*
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Leishmania donovani / genetics
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Leishmania donovani / metabolism
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Leishmania donovani / pathogenicity*
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Membrane Proteins / chemistry
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Membrane Proteins / genetics
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Membrane Proteins / physiology*
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Molecular Sequence Data
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Protozoan Proteins / chemistry
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Protozoan Proteins / genetics
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Protozoan Proteins / physiology*
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Virulence / genetics
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Yeasts / genetics
Substances
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Glycosphingolipids
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LPG2 protein, Leishmania
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Membrane Proteins
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Protozoan Proteins
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lipophosphonoglycan