Instituto de Biomedicina de Sevilla (IBiS), Hospital Universitario Virgen del Rocio-CSIC-Universidad de Sevilla, Seville, Spain.
Departamento de Fisiología Médica y Biofísica, Universidad de Sevilla, Seville, Spain.
Glia. 2018 Jan;66(1):191-205. doi: 10.1002/glia.23237. Epub 2017 Oct 11.
Neuroinflammation mediated by chronically activated microglia, largely caused by abnormal accumulation of misfolded α-synuclein (αSyn) protein, is known to contribute to the pathophysiology of Parkinson's disease (PD). In this work, based on the immunomodulatory activities displayed by particular heat-shock proteins (HSPs), we tested a novel vaccination strategy that used a combination of αSyn and Grp94 (HSPC4 or Gp96) chaperone and a murine PD model. We used two different procedures, first, the adoptive transfer of splenocytes from αSyn/Grp94-immunized mice to recipient animals, and second, direct immunization with αSyn/Grp94, to study the effects in a chronic mouse MPTP-model of parkinsonism. We found that both approaches promoted a distinct profile in the peripheral system-supported by humoral and cellular immunity-consisting of a Th1-shifted αSyn-specific response accompanied by an immune-regulatory/Th2-skewed general phenotype. Remarkably, this mixed profile sustained by αSyn/Grp94 immunization led to strong suppression of microglial activation in the substantia nigra and striatum, pointing to a newly described positive effect of anti-αSyn Th1-responses in the context of PD. This strategy is the first to target αSyn and report the suppression of PD-associated microgliosis. Overall, we show that the αSyn/Grp94 combination supports a distinct and long-lasting immune profile in the peripheral system, which has an impact at the CNS level by suppressing chronic microglial activation in an MPTP model of PD. Furthermore, our study demonstrates that reshaping peripheral immunity by vaccination with appropriate misfolding protein/HSP combinations could be highly beneficial as a treatment for neurodegenerative misfolding diseases.
由慢性激活的小胶质细胞介导的神经炎症,主要由异常积累错误折叠的α-突触核蛋白(αSyn)蛋白引起,已知与帕金森病(PD)的病理生理学有关。在这项工作中,基于特定热休克蛋白(HSPs)显示的免疫调节活性,我们测试了一种新的疫苗接种策略,该策略使用了αSyn 和 Grp94(HSPC4 或 Gp96)伴侣蛋白的组合以及一种小鼠 PD 模型。我们使用了两种不同的程序,首先是从αSyn/Grp94 免疫小鼠中过继转移脾细胞至受体动物,其次是直接用αSyn/Grp94 进行免疫,以研究慢性 MPTP 帕金森病模型中的作用。我们发现,这两种方法都在周围系统中促进了一种独特的表型,这种表型由体液和细胞免疫支持,表现为 Th1 偏移的αSyn 特异性反应,并伴有免疫调节/Th2 倾斜的一般表型。值得注意的是,这种由αSyn/Grp94 免疫维持的混合表型导致黑质和纹状体中小胶质细胞激活的强烈抑制,表明在 PD 背景下抗-αSyn Th1 反应具有新描述的积极作用。该策略是第一个针对αSyn 的策略,并报道了抑制 PD 相关的小胶质细胞增生。总的来说,我们表明,αSyn/Grp94 组合在周围系统中支持独特且持久的免疫表型,通过抑制 PD 的 MPTP 模型中的慢性小胶质细胞激活,对中枢神经系统水平产生影响。此外,我们的研究表明,通过用适当的错误折叠蛋白/HSP 组合进行疫苗接种重塑外周免疫可能是治疗神经退行性错误折叠疾病的非常有益的方法。