ISSN 2320-5407 International Journal of Advanced Research (2015), Volume 3, Issue 12, 1049 – 1054 1049 Journal homepage: http://www.journalijar.com INTERNATIONAL JOURNAL OF ADVANCED RESEARCH RESEARCH ARTICLE Posttranslational features of Phospholipase A 2 like Protein from blood stream form Trypanosoma brucei brucei I.Y. LONGDET 1 * B. YAKUBU 2 H.M. INUWA 3 I.A. UMAR 3 and A.J. NOK 3 1.Department of Biochemistry, University of Jos, Nigeria; 2.Department of Biotechnology, NVRI, Vom, Nigeria, 3.Department of Biochemistry, Ahmadu Bello University, Zaria, Nigeria Manuscript Info Abstract Manuscript History: Received: 18 October 2015 Final Accepted: 22 November 2015 Published Online: December 2015 Key words: Trypanosoma brucei brucei, Phospholipase A 2, transmembrane helix, phosphorylation, methylation, glycosylation *Corresponding Author I.Y. LONGDET Posttranslational modifications (PTMs) of proteins are crucial for understanding their dynamics and the various signaling pathways or networks in cells. The interest in phospholipase A 2 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 PLA 2 -like gene amplified. The gene sequence gave a 1344bp length. The protein translation of the PLA 2 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. Copy Right, IJAR, 2015,. All rights reserved INTRODUCTION Phospholipase A 2 (3.1.1.4) belongs to a superfamily of enzymes that hydrolyse glycerophoshospholipids at the sn-2 position giving rise to free fatty acids and lysophospholipids. This group of enzymes has been described in a variety of organisms such as vertebrates (mammals, lizards and snake venoms), insects (bees, wasp and scorpions) and parasites (Trypanosoma spp). We had reported the presence and sequence homology studies of PLA 2 like gene from Trypanosoma brucei (Longdet and Yakubu, 2014; Longdet et al., 2014) . All the members of the PLA 2 superfamily carry a consensus sequence GXSXG which is common to many other lipases (Balsinde et al., 1999) despite some differences that are the basis for the various patterns of classification. The PLA 2 from Trypanosoma species has not found inclusion in the several classes of the enzymes reported in literature possibly due to the scarcity of literature on its studies. Therefore, this work was designed to study the enzyme, PLA 2 , in blood stream form of T. b. brucei. During protein biosynthesis, the polypeptide chains created undergo a series of activities, such as cutting, folding, and posttranslational modification (PTM) (Qiu et al., 2014). Since understanding PTMs in proteins is crucial for dynamic proteome analysis of various diseases and epigenetic inheritance, the analyses of posttranslational features of phospholipase A 2 like Protein was considered imperative.