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α-突触核蛋白在神经元和脑组织中支持 I 型干扰素信号转导。

Alpha-synuclein supports type 1 interferon signalling in neurons and brain tissue.

机构信息

Department of Immunology and Microbiology, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.

Division of Infectious Diseases, Department of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.

出版信息

Brain. 2022 Oct 21;145(10):3622-3636. doi: 10.1093/brain/awac192.

Abstract

The protein alpha-synuclein is predominantly expressed in neurons and is associated with neurodegenerative diseases like Parkinson's disease and dementia with Lewy bodies. However, the normal function of alpha-synuclein in neurons is not clearly defined. We have previously shown that mice lacking alpha-synuclein expression exhibit markedly increased viral growth in the brain, increased mortality and increased neuronal cell death, implicating alpha-synuclein in the neuronal innate immune response. To investigate the mechanism of alpha-synuclein-induced immune responses to viral infections in the brain, we challenged alpha-synuclein knockout mice and human alpha-synuclein knockout dopaminergic neurons with RNA virus infection and discovered that alpha-synuclein is required for neuronal expression of interferon-stimulated genes. Furthermore, human alpha-synuclein knockout neurons treated with type 1 interferon failed to induce a broad range of interferon stimulated genes, implying that alpha-synuclein interacts with type 1 interferon signalling. We next found that alpha-synuclein accumulates in the nucleus of interferon-treated human neurons after interferon treatment and we demonstrated that interferon-mediated phosphorylation of STAT2 is dependent on alpha-synuclein expression in human neurons. Next, we found that activated STAT2 co-localizes with alpha-synuclein following type 1 interferon stimulation in neurons. Finally, we found that brain tissue from patients with viral encephalitis expresses increased levels of phospho-serine129 alpha-synuclein in neurons. Taken together, our results show that alpha-synuclein expression supports neuron-specific interferon responses by localizing to the nucleus, supporting STAT2 activation, co-localizing with phosphorylated STAT2 in neurons and supporting expression of interferon-stimulated genes. These data provide a novel mechanism that links interferon activation and alpha-synuclein function in neurons.

摘要

蛋白α-突触核蛋白主要在神经元中表达,与帕金森病和路易体痴呆等神经退行性疾病有关。然而,α-突触核蛋白在神经元中的正常功能尚不清楚。我们之前曾表明,缺乏α-突触核蛋白表达的小鼠在大脑中的病毒生长明显增加,死亡率增加,神经元细胞死亡增加,这表明α-突触核蛋白参与神经元固有免疫反应。为了研究α-突触核蛋白对大脑中病毒感染的免疫反应的机制,我们用 RNA 病毒感染了α-突触核蛋白敲除小鼠和人α-突触核蛋白敲除多巴胺能神经元,发现α-突触核蛋白是神经元表达干扰素刺激基因所必需的。此外,用 1 型干扰素处理的人α-突触核蛋白敲除神经元未能诱导广泛的干扰素刺激基因,这意味着α-突触核蛋白与 1 型干扰素信号通路相互作用。接下来,我们发现α-突触核蛋白在干扰素处理后在干扰素处理的人神经元的核内积累,并且我们证明了干扰素介导的 STAT2 磷酸化依赖于人神经元中α-突触核蛋白的表达。接下来,我们发现激活的 STAT2 在神经元中经 1 型干扰素刺激后与α-突触核蛋白共定位。最后,我们发现病毒性脑炎患者的脑组织中神经元中磷酸化丝氨酸 129 位的α-突触核蛋白表达增加。总之,我们的结果表明,α-突触核蛋白的表达通过定位于核内来支持神经元特异性干扰素反应,支持 STAT2 激活,与磷酸化 STAT2 在神经元中共定位,并支持干扰素刺激基因的表达。这些数据提供了一个新的机制,将干扰素激活与神经元中的α-突触核蛋白功能联系起来。

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