Ghosh Pratik, Bhattacharya Manojit, Patra Prasanta, Sharma Garima, Patra Bidhan Chandra, Lee Sang-Soo, Sharma Ashish Ranjan, Chakraborty Chiranjib
Department of Zoology, Vidyasagar University, Midnapore, West Bengal 721102 India.
Department of Zoology, Fakir Mohan University, Vyasa Vihar, Balasore, Odisha 756020 India.
Int J Pept Res Ther. 2022;28(1):5. doi: 10.1007/s10989-021-10322-9. Epub 2021 Nov 29.
and its serogroup can cause several diseases in humans, cattle, ruminants, and birds. The viral M-polyprotein helps the virus to enter the host body. Therefore, this protein might serve as a potential vaccine target against . The present study applied the immunoinformatics technique to design an epitopic vaccine component that could protect against infection. Phylogenetic analysis revealed the presence of conserved patterns of M-polyprotein within the viral serogroup. Three epitopes common for both B-cell and T-cell were identified, i.e., YQPTELTRS, YKAHDKEET, and ILGTGTPKF merged with a specific linker peptide to construct an active vaccine component. The low atomic contact energy value of docking complex between human TLR4 (TLR4/MD2 complex) and vaccine construct confirms the elevated protein-protein binding interaction. Molecular dynamic simulation and normal mode analysis illustrate the docking complex's stability, especially by the higher Eigenvalue. In silico cloning of the vaccine construct was applied to amplify the desired vaccine component. Structural allocation of both the vaccine and epitopes also show the efficacy of the developed vaccine. Hence, the computational research design outcomes support that the peptide-based vaccine construction is a crucial drive target to limit the infection of to an extent.
The online version contains supplementary material available at 10.1007/s10989-021-10322-9.
其血清群可在人类、牛、反刍动物和鸟类中引发多种疾病。病毒的M多聚蛋白有助于病毒进入宿主体内。因此,这种蛋白可能是针对[病毒名称未明确]的潜在疫苗靶点。本研究应用免疫信息学技术设计一种可预防[病毒名称未明确]感染的表位疫苗成分。系统发育分析揭示了病毒血清群内M多聚蛋白存在保守模式。鉴定出两个B细胞和T细胞共有的三个表位,即YQPTELTRS、YKAHDKEET和ILGTGTPKF,与特定连接肽融合以构建活性疫苗成分。人TLR4(TLR4/MD2复合物)与疫苗构建体之间对接复合物的低原子接触能值证实了蛋白质-蛋白质结合相互作用增强。分子动力学模拟和正常模式分析表明对接复合物的稳定性,尤其是较高的本征值。应用疫苗构建体的电子克隆来扩增所需的疫苗成分。疫苗和表位的结构分配也显示了所开发疫苗的功效。因此,计算研究设计结果支持基于肽的疫苗构建在一定程度上是限制[病毒名称未明确]感染的关键驱动靶点。
在线版本包含可在10.1007/s10989-021-10322-9获取的补充材料。