TY - JOUR
T1 - Comprehensive Proteomics Analysis of Glycosomes from Leishmania donovani
AU - Jamdhade, Mahendra D.
AU - Pawar, Harsh
AU - Chavan, Sandip
AU - Sathe, Gajanan
AU - Umasankar, P. K.
AU - Mahale, Kiran N.
AU - Dixit, Tanwi
AU - Madugundu, Anil K.
AU - Prasad, T. S.Keshava
AU - Gowda, Harsha
AU - Pandey, Akhilesh
AU - Patole, Milind S.
N1 - Publisher Copyright:
© Copyright 2015, Mary Ann Liebert, Inc.
Copyright:
Copyright 2015 Elsevier B.V., All rights reserved.
PY - 2015/3
Y1 - 2015/3
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84924349824&partnerID=8YFLogxK
U2 - 10.1089/omi.2014.0163
DO - 10.1089/omi.2014.0163
M3 - Article
C2 - 25748437
AN - SCOPUS:84924349824
SN - 1536-2310
VL - 19
SP - 157
EP - 170
JO - OMICS: A Journal of Integrative Biology (OMICS)
JF - OMICS: A Journal of Integrative Biology (OMICS)
IS - 3
ER -