The decoding of genome sequences of camel and its pathogens will help in speeding up the discovery of new drug targets of pathogens. In this context, Trypanosoma evansi (T. evansi) constitutes the major health hazard with confirmed broad host range and zoonotic infections of humans. Discovery of a drug target in T. evansi deoxyuridine 5'- triphosphate (dUTP) pathways by comparing dUTP metabolizing enzymes in dromedary camels and the parasite. The pyrimidine pathways were investigated and the enzymes involved in the metabolism of deoxyuridine 5'- triphosphate (dUTP) in camel and T. evansi were investigated by bioinformatics tools. T. evansi was devoid of deoxycytidine triphosphate deaminase rendering the source of dUTP under metabolic stress. There were interesting differences in predicted structure and function of dUTPase between the camel and T. evansi. The camel dUTPase is a trimeric enzyme of 165 amino acids highly similar to other vertebrates’ enzyme, mw of 18 kDa and form trimers without multiple domain constituents. In comparison, T. evansi dUTPase is a dimeric enzyme with a higher mw of 32 kDa resembling bacterial and some protozoal enzyme and bearing multiple domain content of dUTPase-2 family, as well as a broad-spectrum nucleotide-binding domain. Additionally, both enzymes have different catalytic attacks at the nucleotide phosphates. Owing to the described structural and catalytic differences, dUTPase could be a useful target for anti-Trypanosoma drug discovery research.

To Cite This Article: Kandeel M and Al-Taher A, 2021. Molecular landscapes of deoxyuridine 5'-triphosphatase (dUTPase) as a drug target against camel Trypanosoma evansi. Pak Vet J, 41(2): 235-241. http://dx.doi.org/10.29261/pakvetj/2021.015