Laboratorio de Inmunomodulación y Desarrollo de Vacunas, Departamento de Inmunobiología, Facultad de Medicina, Universidad de La República, Montevideo, Uruguay.
Unidad de Biología Molecular, Institut Pasteur Montevideo, Montevideo, Uruguay.
Immunology. 2021 May;163(1):46-59. doi: 10.1111/imm.13302. Epub 2021 Jan 25.
Trypanosoma cruzi cytosolic tryparedoxin peroxidase (c-TXNPx) is a 2-Cys peroxiredoxin (Prx) with an important role in detoxifying host cell oxidative molecules during parasite infection. c-TXNPx is a virulence factor, as its overexpression enhances parasite infectivity and resistance to exogenous oxidation. As Prxs from other organisms possess immunomodulatory properties, we studied the effects of c-TXNPx in the immune response and analysed whether the presence of the peroxidatic cysteine is necessary to mediate these properties. To this end, we used a recombinant c-TXNPx and a mutant version (c-TXNPxC52S) lacking the peroxidatic cysteine. We first analysed the oligomerization profile, oxidation state and peroxidase activity of both proteins by gel filtration, Western blot and enzymatic assay, respectively. To investigate their immunological properties, we analysed the phenotype and functional activity of macrophage and dendritic cells and the T-cell response by flow cytometry after injection into mice. Our results show that c-TXNPx, but not c-TXNPxC52S, induces the recruitment of IL-12/23p40-producing innate antigen-presenting cells and promotes a strong specific Th1 immune response. Finally, we studied the cellular and humoral immune response developed in the context of parasite natural infection and found that only wild-type c-TXNPx induces proliferation and high levels of IFN-γ secretion in PBMC from chronic patients without demonstrable cardiac manifestations. In conclusion, we demonstrate that c-TXNPx possesses pro-inflammatory properties that depend on the presence of peroxidatic cysteine that is essential for peroxidase activity and quaternary structure of the protein and could contribute to rational design of immune-based strategies against Chagas disease.
克氏锥虫细胞质硫氧还蛋白过氧化物酶 (c-TXNPx) 是一种 2-Cys 过氧化物酶 (Prx),在寄生虫感染过程中对清除宿主细胞氧化分子具有重要作用。c-TXNPx 是一种毒力因子,因为其过表达增强了寄生虫的感染力和对外源氧化的抵抗力。由于来自其他生物体的 Prx 具有免疫调节特性,我们研究了 c-TXNPx 在免疫反应中的作用,并分析了过氧物酶半胱氨酸的存在是否有必要介导这些特性。为此,我们使用重组 c-TXNPx 和突变体版本 (c-TXNPxC52S) 缺乏过氧物酶半胱氨酸。我们首先通过凝胶过滤、Western blot 和酶促测定分别分析了这两种蛋白质的寡聚化谱、氧化状态和过氧化物酶活性。为了研究它们的免疫特性,我们通过流式细胞术分析了注射到小鼠体内后巨噬细胞和树突状细胞的表型和功能活性以及 T 细胞反应。我们的结果表明,c-TXNPx 但不是 c-TXNPxC52S 诱导产生 IL-12/23p40 的先天抗原呈递细胞的募集,并促进强烈的特异性 Th1 免疫反应。最后,我们研究了在寄生虫自然感染背景下发展的细胞和体液免疫反应,发现只有野生型 c-TXNPx 诱导来自慢性患者的 PBMC 增殖和高水平 IFN-γ 分泌,而这些患者没有明显的心脏表现。总之,我们证明 c-TXNPx 具有依赖于过氧物酶半胱氨酸的促炎特性,而过氧物酶半胱氨酸对于过氧化物酶活性和蛋白质的四级结构是必需的,这可能有助于对抗恰加斯病的基于免疫的策略的合理设计。