The dynamics of interactions of viral proteins with their host are pivotal in establishing a successful infection and ensuring systemic spread. To uncover these, an in silico analysis of the interactions between the coat protein (CP) of Sesbania mosaic virus (SeMV), a group IV virus with single-stranded positive-sense RNA genome was carried out with the known crystal structures of proteins belonging to the Fabaceae family, which is its natural host. SeMV is an isometric plant virus which infects Sesbania grandiflora, a member of Fabaceae, and causes mosaic symptoms. Earlier results have indicated that the assembly and disassembly events of SeMV favor the formation of CP dimers. Hence, the ability and strength of interactions of CP dimer with the host proteins were assessed using in silico protein–protein docking approaches. A set of 61 unique crystal structures of native proteins belonging to Fabaceae were downloaded from the Protein Data Bank (PDB) and docked with the CP dimer of SeMV. From the docking scores and interaction analysis, the host proteins were ranked according to their strength and significance of interactions with the CP dimers. The leads that were identified present themselves as strong candidates for developing antivirals against not only SeMV but also other related viruses that infect Fabaceae. The study is a prototype to understand host protein interactions in viruses and hosts.

病毒蛋白与其宿主的相互作用动力学对于建立成功的感染和确保系统性传播至关重要。为了揭示这些，对Sesbania花叶病毒（SeMV）的外壳蛋白（CP）之间的相互作用进行了计算机分析，该蛋白是具有单链正义RNA基因组的IV组病毒，具有已知的蛋白质晶体结构在豆科植物家族，这是它的自然宿主。SeMV是一种等距的植物病毒，可感染Fabaceae的成员Sesbania grandiflora ，并导致马赛克症状。较早的结果表明，SeMV的组装和拆卸事件有利于CP二聚体的形成。因此，使用计算机模拟蛋白质-蛋白质对接方法评估了CP二聚体与宿主蛋白质相互作用的能力和强度。从蛋白质数据库（PDB）下载了一组属于豆科的天然蛋白质的61个独特的晶体结构，并与SeMV的CP二聚体对接。从对接分数和相互作用分析，根据宿主蛋白的强度和与CP二聚体相互作用的重要性对宿主蛋白进行排名。鉴定出的线索本身是开发抗SeMV以及对抗Fabaceae的其他相关病毒的抗病毒剂的强大候选者。 该研究是了解病毒和宿主中宿主蛋白相互作用的原型。