An evaluation of Fasciola hepatica HDM-1 mRNA expression in eggs, miracidia and adult flukes and simulation of its internalization pathway

Fascioliasis caused by parasitic flukes of the genus Fasciola. Here, the transcription of FhHDM-1(Fasciola hepatica Helminth Defense Molecule-1) was summarized to show its presence in the developmental stages of Fasciola hepatica (F.hepatica). Structural features were identified by bioinformatics tools as a bioactive-immunomodulator molecule-based therapy. We also simulated peptide initialization by the Linux operating system using GROningen MAchine for Chemical Simulations (GROMACS) and Coarse-grained molecular dynamics (CGMD) Simulation. The final structure of the peptide was extracted from the last frame of the simulation and used as the initial structure for the simulation of protein initialization into the plasma membrane. All HDM clade sequences showed amino acid sequence identity in the sequence part of HDMs, consisting of an N-terminal signal peptide, an α-helical secondary structure, and a C-terminal amphipathic motif when compared with orthologues from other trematodes in databases. The bioinformatics analysis provided stereochemical structures and biochemical features of peptides, showing a relatively appropriate quality for protein biological expression systems. Our findings revealed the presence of FhHDM-1 mRNA in F. hepatica adult flukes and the lack of mRNA in its eggs and miracidia, indicating its central role in the evolution of the parasitic life cycle. The internalization of the peptide into the plasma membrane lipid rafts by the polar heads of lipid molecules and interaction with phospholipids, in turn, results in creating curvature, leading to endocytosis pathways. The possible presenting antigens by MHC classes I and II were identified as overlapping fragments throughout the protein sequence.