Identification and characterisation of the gene encoding an amastine-like surface protein (ALSP) in the Leishmania donovani genome: a putative anti-leishmanial drug target [article]

Bapi Biswas, Bhakti Laha, Monidipa Ghosh
2020 bioRxiv   pre-print
The host-parasite interaction is a complex molecular cross-talk between the host and its parasites, where the parasite employs a repertoire of surface and secretory effector molecules for host cell manipulation and successful parasitism. Identification and functional analysis of such parasite specific effectors is an efficient approach to understand the molecular basis of host-parasite interaction which provides us a potential drug target against the parasitic diseases. The current study
more » ... zes an Amastine like Surface Protein (ALSP), present and expressed in abundant amount in intracellular amastigotes form of Leishmania donovani, the causative agent of visceral leishmaniasis. In-silico analysis indicates that this protein is localized in the cytosol of the amastigotes. Characterization of the protein is performed through Indirect ELISA, Immunoprecipitation, MALDI-TOF, MALDI-TOF-MS-MS analysis and subcellular localization. MALDI-TOF MS analysis reveals that the molecular mass of the protein is 10.147 kDa. Following digestion with trypsin, MALDI-TOF-MS-MS analysis using peptide fragments of the purified native protein in amastigotes shows 100% identity with the leishmanial ALSP. Prediction of its presence and expression was done by localization and transcript level studies. Based on in-silico study, ALSP is 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.
doi:10.1101/2020.07.23.218107 fatcat:yolorxisijddrggyofjrmdejcq