Department of Hybrid Microbiosystems Engineering, Nalecz Institute of Biocybernetics and Biomedical Engineering, Polish Academy of Sciences, Ks. Trojdena 4 St., 02-109 Warsaw, Poland.
Department of Biomedical Sciences, Faculty of Medicine, Collegium Medicum, Cardinal Stefan Wyszynski University, Wóycickiego 1/3, 01-938 Warsaw, Poland.
Int J Mol Sci. 2024 Nov 10;25(22):12079. doi: 10.3390/ijms252212079.
Alpha-synuclein (α-syn) is a 140-amino-acid, intrinsically disordered, soluble protein that is abundantly present in the brain. It plays a crucial role in maintaining cellular structures and organelle functions, particularly in supporting synaptic plasticity and regulating neurotransmitter turnover. However, for reasons not yet fully understood, α-syn can lose its physiological role and begin to aggregate. This altered α-syn disrupts dopaminergic transmission and causes both presynaptic and postsynaptic dysfunction, ultimately leading to cell death. A group of neurodegenerative diseases known as α-synucleinopathies is characterized by the intracellular accumulation of α-syn deposits in specific neuronal and glial cells within certain brain regions. In addition to Parkinson's disease (PD), these conditions include dementia with Lewy bodies (DLBs), multiple system atrophy (MSA), pure autonomic failure (PAF), and REM sleep behavior disorder (RBD). Given that these disorders are associated with α-syn-related neuroinflammation-and considering that SARS-CoV-2 infection has been shown to affect the nervous system, with COVID-19 patients experiencing neurological symptoms-it has been proposed that COVID-19 may contribute to neurodegeneration in PD and other α-synucleinopathies by promoting α-syn misfolding and aggregation. In this review, we focus on whether SARS-CoV-2 could act as an environmental trigger that facilitates the onset or progression of α-synucleinopathies. Specifically, we present new evidence on the potential role of SARS-CoV-2 in modulating α-syn function and discuss the causal relationship between SARS-CoV-2 infection and the development of parkinsonism-like symptoms.
α-突触核蛋白(α-syn)是一种含有 140 个氨基酸的、无规则结构的可溶性蛋白,在大脑中大量存在。它在维持细胞结构和细胞器功能方面起着至关重要的作用,特别是在支持突触可塑性和调节神经递质周转方面。然而,由于一些尚未完全了解的原因,α-syn 可能会失去其生理功能并开始聚集。这种改变的 α-syn 会破坏多巴胺能传递,并导致突触前和突触后功能障碍,最终导致细胞死亡。一组被称为 α-突触核蛋白病的神经退行性疾病的特征是特定脑区的特定神经元和神经胶质细胞内 α-syn 沉积的细胞内积累。除了帕金森病(PD)之外,这些病症还包括路易体痴呆(DLB)、多系统萎缩症(MSA)、单纯自主神经衰竭(PAF)和 REM 睡眠行为障碍(RBD)。鉴于这些疾病与 α-syn 相关的神经炎症有关——并且考虑到 SARS-CoV-2 感染已被证明会影响神经系统,COVID-19 患者会出现神经系统症状——有人提出 COVID-19 可能通过促进 α-syn 错误折叠和聚集,导致 PD 和其他 α-突触核蛋白病的神经退行性变。在这篇综述中,我们重点讨论了 SARS-CoV-2 是否可以作为促进 α-突触核蛋白病发病或进展的环境触发因素。具体来说,我们提出了 SARS-CoV-2 调节 α-syn 功能的潜在作用的新证据,并讨论了 SARS-CoV-2 感染与帕金森样症状发展之间的因果关系。