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A Novel Chaperone Function of Cycophilin from Leishmania Donovani: Mode of Intercation With its Client Protein.

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Title A Novel Chaperone Function of Cycophilin from Leishmania Donovani: Mode of Intercation With its Client Protein.
 
Creator Sen, Banibrata
 
Subject Structural Biology & Bioinformatics
 
Description Parasite, in order to evade the host defense mechanism, adopt a biologically much complicated physiology which in turn allow it to bypass the host immune response as well as enables it to resistance towards drugs. One of the major reasons behind slow progress of this field is the lack
of detail knowledge on parasite biology. Leishmania donovani an obligatory purine auxotrophic parasitic protozoa, causes visceral leishmaniasis or more popularly known as “Kala-azar” in human in the Indian as well as in African subcontinent. Being a purine auxotroph, the purine salvage pathway of this parasite reveal great importance. Initial finding suggested that differences in the properties of the parasite from its host counter part with respect to purine-metabolizing enzyme might be exploited in chemotherapy. Cyclophilin, a single domain chaperonic protein showing “peptidyl prolyl cis-trans isomerase
(PPIase)” activity, is involved in various physiological processes. Our serendipitious observation indicated that adenosine kinase of L donovani, cloned and purified from this laboratory, under homogeneous condition, form soluble aggregate. This ultimately leads to its inactivation. Cyclophilin can reactivate the AdK when it was included in assay condition. Surprisingly it was found that the PPIase
activity of CyP has no relation with the AdK reactivation process. Adenosine kinase (AdK), one of the key enzymes of purine salvage pathway, shows differential expressional pattern in the two stage of the parasite life cycle and displays several biochemical and biophysical properties distinct from its host counter part. This unorthodox chaperone function of cyclophilin which includes studies on its novel mechanism of action became the topic of the present work. The studies showed that this simgle domain
chaperonic protein (~18 KDa) reactivates oligomeric adenosine kinase. Furthermore the sites of interaction of AdK to CyP have been identified. The relavance of this interaction during cellular transformation of the parasite has been studied.
 
Date 2008
 
Type Thesis
NonPeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/1573/1/bani_thesis_final.pdf
Sen, Banibrata (2008) A Novel Chaperone Function of Cycophilin from Leishmania Donovani: Mode of Intercation With its Client Protein. PhD thesis, Jadavpur University.
 
Relation http://www.eprints.iicb.res.in/1573/