Institute of Molecular Virology and Cell Biology, Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Südufer 10, 17493 Greifswald-Insel Riems, Germany.
Viruses. 2024 Sep 17;16(9):1478. doi: 10.3390/v16091478.
The African swine fever virus (ASFV) is a large and complex DNA virus that causes a highly lethal disease in swine, for which no antiviral drugs or vaccines are currently available. Studying viral-host protein-protein interactions advances our understanding of the molecular mechanisms underlying viral replication and pathogenesis and can facilitate the discovery of antiviral therapeutics. In this study, we employed affinity tagging and purification mass spectrometry to characterize the interactome of VPS39, an important cellular factor during the early phase of ASFV replication. The interaction network of VPS39 revealed associations with mitochondrial proteins involved in membrane contact sites formation and cellular respiration. We show that the ASFV proteins CP204L and A137R target VPS39 by interacting with its clathrin heavy-chain functional domain. Furthermore, we elaborate on the potential mechanisms by which VPS39 may contribute to ASFV replication and prioritize interactions for further investigation into mitochondrial protein function in the context of ASFV infection.
非洲猪瘟病毒(ASFV)是一种大型且复杂的 DNA 病毒,可导致猪的高度致命疾病,目前尚无抗病毒药物或疫苗。研究病毒-宿主蛋白-蛋白相互作用可以增进我们对病毒复制和发病机制的分子机制的理解,并有助于发现抗病毒治疗药物。在这项研究中,我们采用亲和标记和纯化质谱法来表征 VPS39 的互作组,VPS39 是 ASFV 复制早期阶段的一个重要的细胞因子。VPS39 的相互作用网络揭示了与参与膜接触位点形成和细胞呼吸的线粒体蛋白的关联。我们表明,ASFV 蛋白 CP204L 和 A137R 通过与 VPS39 的网格蛋白重链功能域相互作用来靶向 VPS39。此外,我们详细阐述了 VPS39 可能有助于 ASFV 复制的潜在机制,并优先考虑了进一步研究 ASFV 感染背景下线粒体蛋白功能的相互作用。