Taenia solium, like other
helminthic
parasites, lacks key components of cellular machinery required for
endogenous lipid biosynthesis. This deficiency compels the parasite
to obtain all of its lipid requirements from its host. The passage
of lipids across the cell membrane is tightly regulated. To facilitate
effective lipid transport, the cestode parasite utilizes certain lipid
binding proteins called FABPs. These FABPs bind with the lipid ligands
and allow the transport of lipids across the membranes and into the
cytosol. Here, by integrating a computational with homology protein
prediction tools, we had identified five FABPs in the T. solium proteome. We confirmed their presence by
RNA expression analysis of respective genes from the parasite’s
cysticerci transcript. During the molecular modeling and MD simulation
studies, two of them, TsM_000544100 and TsM_001185100, were most stable.
Furthermore, they had a robust interaction with the IgG1 molecule,
as evidenced by MD simulation. In addition, by employing in
silico screening, we had identified potential ligand interacting
residues that are present on the probable druggable site. In combination
with in vitro cysticidal assays, enalaprilat dihydrate
showed efficacy against cysticerci, which suggests that FABPs play
a significant role in the cysticercus life cycle. Together, we provided
a detailed distribution of all FABPs expressed by T.
solium cysticerci and the critical role of TsM_001185100
in cysticercus viability.