In silico characterisation of a mitotic kinesin-related protein from Leishmania donovani KE16

Mitotic kinesin proteins have a significant role in eukaryotic cell mitosis. The kinesin motor domain of Leishmania donovani has been explored as a promising vaccine candidate due to its ability to generate strong immune responses. The current study aimed to fill the knowledge gap and to systematically identify the main characteristic of kinesin related protein in L. donavani strain KE16 (LdonKE16) (AAT40474.1) using TriTrypDB (kinetoplast genomics), NCBI and EMBL database tools. The study was carried out using in silico PCR analysis of LdonKE16 as a potential of mitotic kinesin protein. Amino acid sequence of the kinesin motor domain regions was detected by using BLASTp for AAT40474.1 and showed various identities with other Leishmania spp. The highest sequence identity with L. donovani K39 (98.10%), then with L. infantum (97.09%), and (97%) with L. chagasi, and L. braziliensis respectively. While L. mexicana showed low sequence identity (61%). The conserved domains KISc of this protein contains three typical domains, the N-terminal motor domain (11 to 399 aa), the coiled segment neck domain (429 to 622aa) and the tail region (681 to 858 aa). The current study revealed that the predicted functional structure of LdonKE16 has active state and inactive state by using bioinformatics tool I-TASSER. The PCR product confirmed the identification of the kinesin protein in LdonKE16. Sequence analysis demonstrated strong homology between LdonKE16 and kinesin K39 of visceral Leishmania species, aligning with the kinesin superfamily KIF13 found in parasites and humans. These findings suggest that LdonKE16 is a promising candidate for vaccine development and therapeutic interventions against leishmaniasis.