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Comprehensive Proteomics Analysis of Glycosomes from Leishmania Donovani

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Journal OMICS
Date 2015 Mar 10
PMID 25748437
Citations 11
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Abstract

Leishmania donovani is a kinetoplastid protozoan that causes a severe and fatal disease kala-azar, or visceral leishmaniasis. L. donovani infects human host after the phlebotomine sandfly takes a blood meal and resides within the phagolysosome of infected macrophages. Previous studies on host-parasite interactions have not focused on Leishmania organelles and the role that they play in the survival of this parasite within macrophages. Leishmania possess glycosomes that are unique and specialized subcellular microbody organelles. Glycosomes are known to harbor most peroxisomal enzymes and, in addition, they also possess nine glycolytic enzymes. In the present study, we have carried out proteomic profiling using high resolution mass spectrometry of a sucrose density gradient-enriched glycosomal fraction isolated from L. donovani promastigotes. This study resulted in the identification of 4022 unique peptides, leading to the identification of 1355 unique proteins from a preparation enriched in L. donovani glycosomes. Based on protein annotation, 566 (41.8%) were identified as hypothetical proteins with no known function. A majority of the identified proteins are involved in metabolic processes such as carbohydrate, lipid, and nucleic acid metabolism. Our present proteomic analysis is the most comprehensive study to date to map the proteome of L. donovani glycosomes.

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References
1.
Opperdoes F, Baudhuin P, Coppens I, De Roe C, Edwards S, Weijers P . Purification, morphometric analysis, and characterization of the glycosomes (microbodies) of the protozoan hemoflagellate Trypanosoma brucei. J Cell Biol. 1984; 98(4):1178-84. PMC: 2113209. DOI: 10.1083/jcb.98.4.1178. View

2.
Petriv O, Tang L, Titorenko V, Rachubinski R . A new definition for the consensus sequence of the peroxisome targeting signal type 2. J Mol Biol. 2004; 341(1):119-34. DOI: 10.1016/j.jmb.2004.05.064. View

3.
KROGH A, Larsson B, von Heijne G, Sonnhammer E . Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol. 2001; 305(3):567-80. DOI: 10.1006/jmbi.2000.4315. View

4.
Dietrich D, Seiler F, Essmann F, Dodt G . Identification of the kinesin KifC3 as a new player for positioning of peroxisomes and other organelles in mammalian cells. Biochim Biophys Acta. 2013; 1833(12):3013-3024. DOI: 10.1016/j.bbamcr.2013.08.002. View

5.
Hasan S, Platta H, Erdmann R . Import of proteins into the peroxisomal matrix. Front Physiol. 2013; 4:261. PMC: 3781343. DOI: 10.3389/fphys.2013.00261. View