Immunoinformatics-aided rational design of multiepitope-based peptide vaccine (MEBV) targeting human parainfluenza virus 3 (HPIV-3) stable proteins

• Published in: Journal of Genetic Engineering and Biotechnology Vol. 21; no. 1; p. 162
• Main Authors: Hossen, Md Sakib, Hasan, Md. Nazmul, Haque, Munima, Al Arian, Tawsif, Halder, Sajal Kumar, Uddin, Md. Jasim, Abdullah-Al-Mamun, M., Shakil, Md Salman
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer Berlin Heidelberg 06.12.2023; Springer Nature B.V
• Subjects: Amino acids; Antigens; Bioinformatics; Biomedical Engineering and Bioengineering; Biotechnology; Cloning; Cloning vectors; Cytotoxicity; DNA-directed RNA polymerase; Engineering; Epitopes; Exo-a-sialidase; Genetic Engineering; Genetics and Genomics; Hemagglutinins; Homology; Immune response; Immune system; Immunology; Infections; Lymphocytes; Lymphocytes B; Lymphocytes T; Matrix protein; Parainfluenza; Peptides; Proteins; Proteomes; Proteomics; Respiratory tract infection; RNA polymerase; RNA viruses; RNA-directed RNA polymerase; TLR3 protein; TLR4 protein; Toll-like receptors; Toxicity; Vaccines; Viral infections; Viruses; pET32a ( +) vector; Multiepitope vaccine; Molecular dynamics simulation; Human parainfluenza virus 3; Molecular docking
• ISSN: 1687-157X; 2090-5920
• DOI: 10.1186/s43141-023-00623-5

Background Human parainfluenza viruses (HPIVs) are common RNA viruses responsible for respiratory tract infections. Human parainfluenza virus 3 (HPIV-3) is particularly pathogenic, causing severe illnesses with no effective vaccine or therapy available. Results The current study employed a systematic immunoinformatic/reverse vaccinology approach to design a multiple epitope-based peptide vaccine against HPIV-3 by analyzing the virus proteome. On the basis of a number of therapeutic features, all three stable and antigenic proteins with greater immunological relevance, namely matrix protein, hemagglutinin neuraminidase, and RNA-directed RNA polymerase L, were chosen for predicting and screening suitable T-cell and B-cell epitopes. All of our desired epitopes exhibited no homology with human proteins, greater population coverage (99.26%), and high conservancy among reported HPIV-3 isolates worldwide. All of the T- and B-cell epitopes are then joined by putative ligands, yielding a 478-amino acid-long final construct. Upon computational refinement, validation, and thorough screening, several programs rated our peptide vaccine as biophysically stable, antigenic, allergenic, and non-toxic in humans. The vaccine protein demonstrated sufficiently stable interaction as well as binding affinity with innate immune receptors TLR3, TLR4, and TLR8. Furthermore, codon optimization and virtual cloning of the vaccine sequence in a pET32a ( +) vector showed that it can be readily expressed in the bacterial system. Conclusion The in silico designed HPIV-3 vaccine demonstrated potential in evoking an effective immune response. This study paves the way for further preclinical and clinical evaluation of the vaccine, offering hope for a future solution to combat HPIV-3 infections.