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Post‐translational modification of cellular proteins during Leishmania donovani differentiation
Author(s) -
Rosenzweig Doron,
Smith Derek,
Myler Peter J.,
Olafson Robert W.,
Zilberstein Dan
Publication year - 2008
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200701043
Subject(s) - acetylation , phagolysosome , leishmania donovani , intracellular , biochemistry , biology , amastigote , glycosylation , phosphorylation , leishmania , methylation , microbiology and biotechnology , gene , parasite hosting , genetics , phagosome , leishmaniasis , visceral leishmaniasis , world wide web , computer science
The pathogenic intracellular parasites Leishmania donovani cycle between sand fly gut and the human macrophage phagolysosome, differentiating from extracellular promastigotes to intracellular amastigote forms. Using isobaric tagging for relative and absolute quantifications (iTRAQ/LC‐MS/MS) proteomic methodology, we recently described the ordered gene expression changes during this process. While protein abundance changes in Leishmania were documented, little is known about their PTMs. Here we used iTRAQ to detect protein phosphorylation, methylation, acetylation, and glycosylation sites throughout differentiation. We found methylation of arginines, aspartic acids, glutamic acids, asparagines, and histidines. Detected acetylation sites included serines and protein N‐terminal acetylations on methionines, serines, alanines, and threonines. Phosphorylations were detected on serines and threonines, but not tyrosines. iTRAQ identified novel fucosylation sites as well as hexosylations. We observed quantity changes in some modifications during differentiation, suggesting a role in L. donovani intracellular development. This study is the first high‐throughput analysis of PTM sites dynamics during an intracellular parasitic development.