Résumé
Aim: This work focused on the sequence homology studies of the enzyme, phospholipase A2 (PLA2), in Trypanosoma brucei obtained from the blood of bull in Federe, Plateau State, Nigeria, West Africa Place and Duration of Study: Department of Biochemistry, University of Jos, Nigeria; Department of Biochemistry, Ahmadu Bello University, Zaria, Nigeria, Department of Biotechnology, NVRI, Vom, Nigeria; between June 2009 and September 2011. Methodology: T. brucei grown in rats were harvested and separated using diethyl amino ethyl (DEAE) cellulose chromatography. From the parasites’ genomic DNA the PLA2-like gene was amplified using consensus primers. The amplicon was cloned unto pMal-2cE vector and confirmed using direct PCR and restriction enzyme analyses. The PLA2 gene and translated protein sequences were studied using National Center for Biotechnology Information (NCBI) Conserved Domain Search Tool and Conserved Domain Architectural Retrieval Tool Results: Analyses of the 1344bp gene sequence using bioinformatics tools showed that it is very closely related to PLA2 sequences of T. brucei (TREU 927) and T. b. gambiense. Motifs that are unique to PLA2 (FSHGL) and lipases (GHSFG) were found to be present in the query sequence. The domains present in the studied sequence agreed closely with those of the human platelet activating factor acetyl hydrolase (PAF-AH). There was also a good sequence resemblance with PLA2s from T. cruzi, Metarhizium amisop, Metarphizium acridu and PAF-AH in terms of architecture. Conclusion: The PLA2-like gene isolated from the blood stream form of Trypanosoma brucei and studied was found to posses the domains and motifs unique to PLA2s and lipases and so homology was established among the proteins.