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Research Paper | Biochemistry Science | Kenya | Volume 5 Issue 7, July 2016

A Functional Comparison of the Archaeon Tricorn Protease and Selected Serine Proteases from Trypanosoma brucei brucei

Ng'ong'a F.A | Wamunyokoli F | Nyanjom S. R. G

Abstract: Trypanosomes are protozoan parasites causing African trypanosomiasis, a neglected tropical disease in Africa affecting humans and animals. Current control methods have focused on the use of drugs which have adverse effects and develop resistance and with no available conventional vaccine. Proteolysis is a key process in trypanosome survival in the mammalian host hence identification of other parasitic factors would lead to the development of new chemotherapeutic agents. This study investigated archaeon tricorn protease functional analogs in Trypanosoma brucei brucei through bioinformatics approaches. The protein sequences were retrieved from NCBI (http//www. ncbi. nlm. nih. gov/protein/) and position specific iterated basic local sequence alignment (PSI-BLAST) was performed using default parameters to determine patterns of conservation which aid in the recognition of distant similarities. The 3D models of the putative proteins were constructed using T. acidophilum tricorn protease. The constructed models were analyzed based on percentage identity, e-value and bit-score. Structural alignment was done using MATRAS (http//strcomp. protein. osaka-u. ac. jp/matras/) and PyMOL Molecular Graphics System, Version 1.8 Schrdinger, LLC (https//www. pymol. org/) was used for viewing and structural analysis. The bioinformatics analysis revealed similarities in the catalytic core elements as well as the beta sheets serving as substrate entry and exit route to and from the catalytic chamber. Therefore, based on these similarities, this study reports the identification tricorn protease functional analogs in Trypanosoma brucei brucei.

Keywords: Tricorn protease, trypanosomiasis, protein homology, serine peptidases, proteolysis

Edition: Volume 5 Issue 7, July 2016,

Pages: 556 - 559

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