In Silico Design of Multimeric HN-F Antigen as a Highly Immunogenic Peptide Vaccine Against Newcastle Disease Virus

• Published in: International journal of peptide research and therapeutics Vol. 20; no. 2; pp. 179 - 194
• Main Authors: Motamedi, Mohammad Javad, Amani, Jafar, Shahsavandi, Shahla, Salmanian, Ali Hatef
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Netherlands 01.06.2014; Springer Nature B.V
• Subjects: Animal Anatomy; Antigens; Biochemistry; Biomedical and Life Sciences; Glycoproteins; Histology; Life Sciences; Molecular biology; Molecular Medicine; Morphology; Newcastle disease virus; Peptides; Pharmaceutical Sciences/Technology; Pharmacology/Toxicology; Polymer Sciences; Viral infections; Epitope mapping; Peptide vaccine; Newcastle disease virus; Codon optimization
• DOI: 10.1007/s10989-013-9380-x
• ISSN: 1573-3149

Application of molecular biology techniques to the production of new vaccines against different strains of the Newcastle disease virus (NDV) has been the subject of recent research reports. Development of improved techniques for genome sequencing has led to the recognition of protective mechanisms and the identification of possible candidate antigens. Such procedures could generate meaningful results regarding the virulence determinants of NDV. This study proposed an in silico approach by assembling potential and conserved epitopic regions of hemagglutinin–neuraminidase (HN) and fusion (F) glycoproteins of NDV to induce multiepitopic responses against the virus. Epitope predictions showed that the hypothetical synthetic construct could induce immature B and T cell epitopes that expect a high immune response because of their location in four distinct parts of the construct, namely the head, stalk and the heptad repeated regions known as the HRA and HRB domains. Most regions of the chimeric construct were found to have high antigenic propensity and surface accessibility, which further confirmed the strategy for selection of precise continuous and discontinuous epitopes of HN and F antigens. Thermodynamic folding of mRNA structures revealed correct folding of the RNA construct, indicating good stability of the mRNA to increase the efficiency of translation in the target host. The three-dimensional structure of the native HN-F chimeric protein was successfully generated and validated as a proper model which may define reliability, structural quality and conformation.