No abstract

The host-parasite interaction is a complex molecular cross-talk, where the parasite employs a repertoire of surface and secretory effector molecules for host cell manipulation and successful parasitism. The current study identifies an Amastine like Surface Protein (ALSP), expressed in abundant amount in the intracellular amastigotes form of Leishmania donovani, the causative agent of visceral leishmaniasis. Characterization and subcellular localization of the protein indicates its stage specific presence in the cytosol of the amastigotes. MALDI-TOF MS analysis reveals its molecular mass to be 10.147 kDa. The trypsin digested purified native protein shows 100% identity with the leishmanial ALSP through MALDI-TOF-MS-MS peptide analysis. Prediction of its presence and expression was done by immunolocalization and transcript level observations. Based on in-silico study, ALSP has been hypothesized to serve as a source of energy for the intracellular parasite during parasitism by conversion of triglycerides into glycerol and fatty acid, assigning a role in virulence through triglyceride lipase activity. The intracellular survival of the parasite with the intervention of the target protein may help in harnessing the candidate molecule, as an appealing target for design of novel chemotherapeutics against visceral leishmaniasis in future.