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Project #2249
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#2249 : Phylogenetic analysis of the Leishmania HSP70 protein family
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Name of Applicant : Gerald Spaeth
Date of application : 18-06-2015
Unit : Molecular Parasitology and Signaling
Location : Calmette 2nd floor room 17
Phone : 0140613858
@ Mail : gspaeth@pasteur.fr

Project context and summary :

Across bacterial, archaeal and eukaryotic kingdoms, heat shock proteins (HSPs) are defined as a class of highly conserved chaperone proteins that are rapidly induced in response to temperature increase through dedicated heat shock transcription factors. While this transcriptional response governs cellular adaptation of fungal, plant and animal cells to thermic shock and other forms of stress, early-branching eukaryotes of the kinetoplastid order, including trypanosomatid parasites, lack classical mechanisms of transcriptional regulation and show largely constitutive expression of HSPs, thus raising important questions on the function of HSPs in the absence of stress and the regulation of their chaperone activity in response to environmental adversity. Understanding parasite-specific mechanisms of stress-response regulation is especially relevant for protozoan parasites of the genus Leishmania that are adapted for survival inside highly toxic phagolysosomes of host macrophages causing the various immuno-pathologies of leishmaniasis. To gain first insight into the role the heat shock repsonse for Leishmania differentiation and pathogenicity, we are studying the evolution and function of members of the HSP70 protein family combining bio-informatics and transgenics apporahces.


Related team publications :
Späth GF, Drini S, Rachidi N. A touch of Zen: post-translational regulation of the Leishmania stress response. Cell Microbiol. 2015 May;17(5):632-8. doi: 10.1111/cmi.12440. Epub 2015 Apr 8. PubMed PMID: 25801803.
Morales MA, Watanabe R, Dacher M, Chafey P, Osorio y Fortéa J, Scott DA, Beverley SM, Ommen G, Clos J, Hem S, Lenormand P, Rousselle JC, Namane A, Späth GF. Phosphoproteome dynamics reveal heat-shock protein complexes specific to the Leishmania donovani infectious stage. Proc Natl Acad Sci U S A. 2010 May
Yau WL, Pescher P, MacDonald A, Hem S, Zander D, Retzlaff S, Blisnick T, Rotureau B, Rosenqvist H, Wiese M, Bastin P, Clos J, Späth GF. The Leishmania donovani chaperone cyclophilin 40 is essential for intracellular infection independent of its stage-specific phosphorylation status. Mol Microbiol. 2014 Jul;93(1):80-97. doi: 10.1111/mmi.12639. Epub 2014 May 23. PubMed PMID: 24811325.
Service Delivery
Project Manager : pierre.lechat@pasteur.fr
Project Type : Short
Status : Closed
Publication : 10.1093/gbe/evw140
Global Satisfaction for this application : Excellent (5/5)


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