Data_Sheet_2_Structural and functional characterization of peste des petits ruminants virus coded hemagglutinin protein using various in-silico approaches.PDF

Peste des petits ruminants (PPR), a disease of socioeconomic importance has been a serious threat to small ruminants. The causative agent of this disease is PPR virus (PPRV) which belongs to the genus Morbillivirus. Hemagglutinin (H) is a PPRV coded transmembrane protein embedded in the viral envelope and plays a vital role in mediating the entry of virion particle into the cell. The infected host mounts an effective humoral response against H protein which is important for host to overcome the infection. In the present study, we have investigated structural, physiological and functional properties of hemagglutinin protein using various computational tools. The sequence analysis and structure prediction analysis show that hemagglutinin protein comprises of beta sheets as the predominant secondary structure, and may lack neuraminidase activity. PPRV-H consists of several important domains and motifs that form an essential scaffold which impart various critical roles to the protein. Comparative modeling predicted the protein to exist as a homo-tetramer that binds to its cognate cellular receptors. Certain amino acid substitutions identified by multiple sequence alignment were found to alter the predicted structure of the protein. PPRV-H through its predicted interaction with TLR-2 molecule may drive the expression of CD150 which could further propagate the virus into the host. Together, our study provides new insights into PPRV-H protein structure and its predicted functions.

小反刍兽疫（Peste des petits ruminants, PPR）是一种具有社会经济重要性的疫病，长期以来对小反刍动物构成严重威胁。该病的病原体为小反刍兽疫病毒（Peste des petits ruminants virus, PPRV），隶属于麻疹病毒属（Morbillivirus）。血凝素（Hemagglutinin, H）是PPRV编码的跨膜蛋白，嵌入病毒囊膜，在介导病毒粒子进入宿主细胞的过程中发挥关键作用。感染宿主会针对H蛋白产生有效的体液免疫应答，这对于宿主清除感染至关重要。本研究借助多种计算工具，对血凝素蛋白的结构、生理及功能特性展开了探究。序列分析与结构预测结果显示，血凝素蛋白以β折叠作为主要的二级结构，且可能不具备神经氨酸酶活性。PPRV-H包含多个重要的结构域与基序，这些元件构成了核心支架结构，赋予该蛋白多种关键功能。比较建模预测该蛋白以同源四聚体（homo-tetramer）的形式存在，并可与其同源细胞受体结合。通过多序列比对鉴定出的部分氨基酸替换，可改变该蛋白的预测结构。PPRV-H通过与Toll样受体2（TLR-2）的预测相互作用，可能介导CD150分子的表达，进而促进病毒在宿主体内的扩散。综上，本研究为PPRV-H蛋白的结构及其预测功能提供了全新的见解。