Analysis of Leishmania phosphoprotein isoforms
EMSL Project ID
38206
Abstract
Our laboratory applies quantitative phosphoproteomics to investigate signaling networks underlying the pathogenicity of the protozoan parasite Leishmania, which causes severe human diseases around the world. Utilizing 2D differential electrophoresis we revealed that 40% of the parasite phosphoproteome shows statistically significant differences between the promastigote insect stage and the infective amastigote stage. 43% of the identified phosphoproteins were represented by protein isoforms, some of which showed stage-specific distribution, including HSP90 and HSP70. Phosphatase treatment had no effect on the distribution of these isoforms, which consequently arise from unknown modifications independent of protein phosphorylation. This proposal aims to determine the elusive protein modifications of Leishmania HSP90 and HSP70, which may be implicated in regulation of the parasite heat shock response and thus directly linked to heat-induced development of the pathogenic amastigote stage. The data are part of a manuscript in revision that will be resubmitted to Science Magazine. We are currently working on a revised version and the support through the EMSL Rapid Access proposal and EMLS mass spectrometry capabilities will be instrumental to obtain crucial data required for a successful re-submission.
Project Details
Project type
Limited Scope
Start Date
2010-02-08
End Date
2010-04-10
Status
Closed
Released Data Link
Team
Principal Investigator