Sui Hongyan, Wiscovitch-Russo Rosana, Cachaco Silvia, Yang Jun, Bruchey Whitney, Laverdure Sylvain, Chen Qian, Imamichi Tomozumi
Laboratory of Human Retrovirology and Immunoinformatics, Frederick National Laboratory, Frederick, MD, 21702.
bioRxiv. 2025 Aug 23:2025.08.20.671272. doi: 10.1101/2025.08.20.671272.
We previously reported that manganese (Mn) enhances innate immune responses to viral infection by inducing phosphorylation of TANK-binding kinase 1 (TBK1) in an Ataxia-telangiectasia mutated (ATM)-dependent manner. However, the underlying mechanism by which how Mn induces TBK1 phosphorylation remained unclear. Here, we show that Mn dose-dependently induced TBK1 phosphorylation in the presence of ATM across multiple cell lines, as well as in primary human macrophages and T cells. This phosphorylation was abolished in ATM-deficient cells, and we identified cytoplasmic ATM as a key mediator. Immunoprecipitation assays revealed that Mn promoted ATM phosphorylation at Ser1893, Ser1981, and Ser2996. TBK1 interacted with phosphorylated ATM at early stages, but upon phosphorylation, TBK1 dissociated from the ATM-TBK1 complex. This dissociation coincided with enhanced antiviral cytokine production. Furthermore, Mn dose-dependently suppressed HIV replication by inducing multiple antiviral host factors and cytokines. Together, these findings identify a cytoplasmic ATM-TBK1 phosphorylation cycle as a critical regulator of antiviral innate immunity and suggest Mn supplementation as a potential therapeutic approach against HIV and other viral infections.
我们之前报道过,锰(Mn)通过以共济失调毛细血管扩张症突变基因(ATM)依赖的方式诱导TANK结合激酶1(TBK1)磷酸化,增强对病毒感染的先天免疫反应。然而,锰诱导TBK1磷酸化的潜在机制仍不清楚。在此,我们表明,在多种细胞系以及原代人巨噬细胞和T细胞中,锰在存在ATM的情况下剂量依赖性地诱导TBK1磷酸化。这种磷酸化在ATM缺陷细胞中被消除,并且我们确定细胞质ATM是关键介质。免疫沉淀分析显示,锰促进ATM在Ser1893、Ser1981和Ser2996位点的磷酸化。TBK1在早期与磷酸化的ATM相互作用,但磷酸化后,TBK1从ATM-TBK1复合物中解离。这种解离与抗病毒细胞因子产生增加相一致。此外,锰通过诱导多种抗病毒宿主因子和细胞因子剂量依赖性地抑制HIV复制。总之,这些发现确定细胞质ATM-TBK1磷酸化循环是抗病毒先天免疫的关键调节因子,并表明补充锰作为对抗HIV和其他病毒感染的潜在治疗方法。