Sialic Acid-Binding Protein-1 (SABP1) of : Preliminary Computer-Based Epitope Mapping for Enhanced Vaccine Design.

() infects one third of the human population globally, presenting serious consequences especially in pregnant women or immunosuppressed patients. This study characterized sialic acid-binding protein-1 (SABP1) to determine its physicochemical, antigenic, and structural properties as well as immunogenic epitopes using bioinformatics predictions. The amino acid sequence for SABP1 was analyzed using ProtParam (physicochemical properties), VaxiJen v2.0 (antigenicity prediction), AllergenFP v1.0 and AllerTOP v2.0 (allergenicity prediction), NetSurfP-6.0 (secondary structure), Robetta (tertiary structure), IEDB, IFNepitope, and IL4pred (immunogenic epitopes). The subcellular prediction was made using signal peptide, transmembrane domain, posttranslational modifications (PTMs) and protein localization). The SABP1 protein (315 residues; 33.73 kDa) possessed antigenicity (0.46), high solubility (0.783), hydrophilicity (GRAVY: -0.335), and an aliphatic index of 69.33. It was shown to be nonallergen. SABP1 is located in the cytoplasm and has no signal peptide or transmembrane domain. Importantly, there were many B- and T-cell epitopes predicted to be immunogenic, which could be beneficial for designing multiepitope vaccines to prevent infection. Further validation of these epitopes using wet experiments is needed.