In Silico Design and 3D Structural Data for a Multi-Epitope Vaccine Construct targeting Tilapia Parvovirus (TiPV)

Research HypothesisThe central hypothesis of this study is that a rationally engineered, 58-amino acid Multi-Epitope Vaccine Construct (MEVC) integrating highly conserved B-cell and T-cell epitopes from the Tilapia Parvovirus (TiPV) VP1 capsid protein with an N-terminal Tuftsin adjuvant will form a thermodynamically stable, high-affinity complex with the teleost Toll-Like Receptor 3 (TLR3) to trigger a robust innate and adaptive immune cascade.What the Data Shows and Notable FindingsThe provided dataset contains the raw viral sequences, multiple sequence alignments, 3D structural coordinate files (.pdb), and the final docked receptor-ligand complex. Structural validation data confirms the de novo modeled vaccine construct possesses optimal stereochemical geometry, with 100% of residues situated in Ramachandran favored or allowed regions. Molecular docking and thermodynamic profiling data show a highly spontaneous binding affinity (ΔG = -21.5 kcal/mol) and a sub-femtomolar dissociation constant (1.6 x 10^-16M). Interface analysis of the docked .pdb complex reveals a massive 2074.4 Ų contact area stabilized by 9 intermolecular hydrogen bonds. Furthermore, kinetic data from Normal Mode Analysis (NMA) yields an eigenvalue of 4.498936 x 10^-7, indicating exceptional dynamic stability of the receptor-vaccine complex under simulated physiological motion. Finally, the dataset includes a 174 bp DNA sequence demonstrating perfect in silico codon optimization (CAI = 1.0, GC = 50.57%) for Escherichia coli K12 expression.How the Data Can Be Interpreted and UsedThis computational dataset serves as a mathematically validated structural blueprint. Researchers can directly download the provided .pdb coordinate files to conduct independent, long-duration Molecular Dynamics (MD) simulations or execute comparative molecular docking against other teleost pattern recognition receptors (PRRs). Additionally, the provided consensus sequences and codon-optimized E. coli DNA files can be directly utilized by wet-lab researchers and molecular biologists to physically synthesize the gene, transitioning this design into in vitro recombinant mass production and subsequent in vivo biological challenge trials in Oreochromis species.