Posttranslational features of Phospholipase A2 like Protein from blood stream form Trypanosoma brucei brucei

Posttranslational modifications (PTMs) of proteins are crucial for understanding their dynamics and the various signaling pathways or networks in cells. The interest in phospholipase A2 was because of its biotechnological potentials and involvement in the pathogenicity of Trypanosoma species. Bloodstream rat adapted strain of T. brucei brucei was grown in rats and separated using DEAE cellulose chromatography. Genomic DNA of the parasites was isolated and the PLA2-like gene amplified. The gene sequence gave a 1344bp length. The protein translation of the PLA2 like gene using BLASTX gave a 447 peptide sequence. This translated protein sequence analysed using bioinformatics tools for posttranslational modifications revealed transmembrane helices; 13 phosphorylation sites; 6 methylation sites and an O-glycosylation site. The electronically detected features in this report agree with those characterized and their potentials in the sequence were discussed.