Analyses of Trypanosoma brucei Phospholipase A2 Structure and Function Using Bioinformatics Approach
Journal Title: Journal of Advances in Biology & Biotechnology - Year 2016, Vol 8, Issue 4
Abstract
Aim: Studying Phospholipase A2 is increasingly needful because of the enzyme’s biotechnological potentials and involvement in the pathogenicity of Trypanosoma species. This work was therefore designed to study some of the structural features of putative PLA2 from T. brucei. Place and Duration of Study: Department of Biotechnology, National Veterinary research Institute, Vom and Department of Parasitology, National Institute of Trypanosomiasis Research, Vom, Nigeria, between July 2015 and May 2016. Methodology: Bloodstream rat adapted strain of T. brucei was grown in rats and separated using DEAE cellulose chromatography. Genomic DNA of the parasites was isolated and the PLA2 gene amplified and sequenced (GenBank DB accession number: JN603736). The translated protein structure prediction server PSIPRED, Phyre2 web portal for protein modeling, prediction and analysis, (ProSA) -web, RAMPAGE server, 3DLigandSite and PSI-Blast tool were used to analyse the T. brucei PLA2 translated protein sequence. Results: The analyses of the PLA2 protein with 447 peptide sequence revealed its secondary structure; 3D structure showing amino acid residues that lie in a helix, strand or coil; ProSA-web z-scores with an overall model quality value of -7.01; the Ramachandran plot that among the 447 residues, 433 (96.86%) were in favoured region; ligand binding site at position 235 (Trp) and its transmembrane helices and membrane topology. Conclusion: A good quality structural model of Trypanosoma brucei PLA2 was determined and found to be closely related to that of Platelet-activating factor acetylhydrolase.
Authors and Affiliations
Ishaya Yohanna Longdet
Keywords
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- EP ID EP351809
- DOI 10.9734/JABB/2016/28443
- Views 64
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