[feed] Atom [feed] RSS 1.0 [feed] RSS 2.0

Jamdhade, M.D. and Pawar, H. and Chavan, S. and Sathe, S. and Umasankar, P.K. and Mahale, K.N. and Dixit , T. and Madugundu, A.K. and Prasad, T.S. and Gowda, H. and Pandey , A. and Patole, M.S. (2015) Comprehensive proteomics analysis of glycosomes from Leishmania donovani. OMICS: A Journal of Integrative Biology, 19 (3). pp. 157-170. ISSN March 2015, 19(3): 157-170

Full text not available from this repository. (Request a copy)

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.

Item Type: Article
Subjects: Insect Molecular Biology
Depositing User: Mr. Rameshwar Nema
Date Deposited: 27 May 2016 03:31
Last Modified: 27 May 2016 03:31
URI: http://nccs.sciencecentral.in/id/eprint/247

Actions (login required)

View Item View Item