Heat shock protein 70 of Trypanosoma evansi is phylogenitically closer to salivaria than stercoraria homologs

Trypanosomioisis is an economically significant disease affecting a wide range of animals in tropics and subtropics. Heat shock proteins (HSPs) play an important role in trypanosomes by altering parasite’s physiology and adaptability as its life cycle alternates between the poikilothermic invertebrate vector and the homoeothermic vertebrate hosts. The aim of the present study was find out the phylogenetic relationship between T. evansi and other trypanosomes using HSP 70 gene. HSP 70 of Trypanosoma evansi was cloned, characterized, and phylogenitically analyzed with HSP 70 sequences of other trypanosomes. Results revealed that HSP 70 is a highly conserved molecule in trypanosomes. It showed 100% identity with other sequences of T. evansi and T. equiperdum. Alongside, it showed much higher identities with sequences of trypanosomes of anterior station group than those of posterior station group. Hence, it was concluded that HSP 70 of T. evansi is phylogenitically closer to salivaria than stercoraria homologs. The finding is important from evolutionary point of view.