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Cloning, expression and dynamic simulation of TRYP6 from Leishmania major (MRHO/IR/75/ER)
1Department of Parasitology and Mycology, Shahid Sadoughi University of Medical Sciences, 8916188/35, Yazd, Iran. eslami_g2000@yahoo.com
Abstract:
Leishmania, a digenetic protozoan parasite causes severe diseases in human and animals. Efficient evasion of toxic microbicidal molecules, such as reactive oxygen species and reactive nitrogen species is crucial for Leishmania to survive and replicate in the host cells. Tryparedoxin peroxidase, a member of peroxiredoxins family, is vital for parasite survival in the presence of antioxidant, hence it is one of the most important molecules in Leishmania viability and then, it may be an appropriate goal for challenging against leishmaniasis. After cloning and sub-cloning of TRYP6 from Leishmania major (MRHO/IR/75/ER), homology modeling of the LmTRYP6 was proposed to predict some functional property of this protein. The refined model showed that the core structure consists of a seven β stranded β-sheet and five α helices which are organized as a central 7-stranded β2-β1-β5-β4-β3-β6-β7 surrounded by 2-stranded β-hairpin, α helices A and D on one side, and α helices B, C and E on the other side. The peroxidatic active site is located in a pocket formed by the residue Pro45, Met46, Thr49, Val51, Cys52, Arg128, Met147 and Pro 148. The catalytic Cys52, located in the first turn of helix αB, is in van der Waals with a Pro45, a Thr49 and an Arg128 that are absolutely conserved in all known Prx sequences. In this study, an attractive molecular target was studied. These results might be used in designing of drugs to fight an important human pathogen.
Insights
Tryparedoxin peroxidase (TRYP6) is crucial for Leishmania parasite survival. Researchers modeled LmTRYP6, revealing its structure and active site, offering a potential target for new anti-leishmaniasis drugs.
Area of Science:
- Parasitology
- Structural Biology
- Drug Discovery
Background:
- Leishmania parasites cause severe diseases and evade host defenses using antioxidant enzymes.
- Tryparedoxin peroxidase (Prx) is vital for Leishmania survival against toxic molecules.
- Leishmania viability relies on Prx, making it a key target for leishmaniasis treatment.
Purpose of the Study:
- To investigate the structure and functional properties of Tryparedoxin peroxidase 6 (LmTRYP6) from Leishmania major.
- To identify potential drug targets for combating leishmaniasis.
Main Methods:
- Cloning and sub-cloning of the TRYP6 gene from Leishmania major.
- Homology modeling to predict the 3D structure of LmTRYP6.
- Analysis of the protein's core structure and active site residues.
Main Results:
- A refined homology model of LmTRYP6 was generated, detailing its seven β-stranded β-sheet and five α-helices.
- The peroxidatic active site pocket was identified, highlighting key residues like Cys52.
- Conserved residues in the active site suggest functional importance and potential for drug interaction.
Conclusions:
- LmTRYP6 possesses a conserved structural framework typical of peroxiredoxins.
- The identified active site and conserved residues provide a basis for rational drug design.
- Targeting LmTRYP6 could lead to novel therapeutic strategies against leishmaniasis.
