In Silico Physicochemical, Structural, and Immunoinformatic Characterization of MPV510 Fab Light Chain as a Potential Vaccine Candidate Against Human Metapneumovirus

Human metapneumovirus (HMPV) is a respiratory virus of high clinical significance, particularly in children and immunocompromised patients all over the world. There are no currently available vaccines for HMPV that are still under development and hence require new vaccine candidates. This study used computational methods to assess the suitability of MPV510 Fab light chain protein as a vaccine candidate against HMPV. Protein sequence (107 amino acids, accession 9PDY_I) was acquired from the NCBI database and analysed using computational methods. The results showed desirable properties such as low molecular weight (11,771.21 Da), optimal pI (9.51) and good solubility (hydrophilicity index = GRAVY = -0.445). PSIPRED analysis demonstrated the protein contains an equal amount of ordered and disordered amino acid residues as observed in functional proteins. DiANNA analysis of the protein confirmed the existence of predicted disulfide bonds. The AllerTOP evaluation confirmed the protein to be a putative non-allergen, making it safe for use in human immunizations. The three-dimensional structure analysis carried out by trROSETTA ensured that high confidence results were generated. As a result, the correct prediction of the structure was obtained, along with the accessibility of the epitopes that could be used to target the vaccine. The entire computational analysis pipeline consisting of physicochemical analysis, structure prediction, and immunoinformatics proves that the Fab light chain of MPV510 protein has various characteristics that make it ideal for vaccination.