REEP5/TRAM1 复合物结合 SARS-CoV-2 NSP3 并促进病毒复制。

Department of Biochemistry and Molecular Pharmacology, New York University Grossman School of Medicine , New York, New York, USA.

Laura and Isaac Perlmutter NYU Cancer Center, New York University Grossman School of Medicine , New York, New York, USA.

J Virol. 2023 Oct 31;97(10):e0050723. doi: 10.1128/jvi.00507-23. Epub 2023 Sep 28.

Generation of virus-host protein-protein interactions (PPIs) maps may provide clues to uncover SARS-CoV-2-hijacked cellular processes. However, these PPIs maps were created by expressing each viral protein singularly, which does not reflect the life situation in which certain viral proteins synergistically interact with host proteins. Our results reveal the host-viral protein-protein interactome of SARS-CoV-2 NSP3, NSP4, and NSP6 expressed individually or in combination. Furthermore, REEP5/TRAM1 complex interacts with NSP3 at ROs and promotes viral replication. The significance of our research is identifying virus-host interactions that may be targeted for therapeutic intervention.

生成病毒-宿主蛋白-蛋白相互作用（PPIs）图谱可能为揭示 SARS-CoV-2 劫持细胞过程提供线索。然而，这些 PPIs 图谱是通过单独表达每种病毒蛋白创建的，这并不能反映某些病毒蛋白与宿主蛋白协同相互作用的生命状态。我们的结果揭示了 SARS-CoV-2 NSP3、NSP4 和 NSP6 单独或组合表达时的宿主-病毒蛋白-蛋白相互作用组。此外，REEP5/TRAM1 复合物在 RO 上与 NSP3 相互作用并促进病毒复制。我们研究的意义在于鉴定可能成为治疗干预目标的病毒-宿主相互作用。