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旋毛虫新型半胱氨酸蛋白酶抑制剂抑制巨噬细胞介导的炎症反应。

A novel cystatin derived from Trichinella spiralis suppresses macrophage-mediated inflammatory responses.

机构信息

Department of Helminthology, Faculty of Tropical Medicine, Mahidol University, Bangkok, Thailand.

Department of Infection Biology, Institute of Infection and Global Health, University of Liverpool, Liverpool, United Kingdom.

出版信息

PLoS Negl Trop Dis. 2020 Apr 1;14(4):e0008192. doi: 10.1371/journal.pntd.0008192. eCollection 2020 Apr.

Abstract

Trichinella spiralis can modulate host immune responses to retain a suitable environment for its long-term survival. Incidentally, the parasite elicits regulatory effects through immunomodulatory molecule release, which can suppress host inflammation and may be used for the treatment of unrelated inflammatory diseases in someday. Here we identified and characterized a novel T. spiralis cystatin (TsCstN), which inhibits inflammation mediated by LPS-treated macrophages.Proteins contained in the excretory-secretory (ES) product of muscle-stage T. spiralis (ES-L1) were fractionated, and each was treated with mouse bone marrow-derived macrophages (mBMDMs) before LPS stimulation. The fractions that exhibited high immunomodulatory property by decreasing pro-inflammatory cytokines or increasing anti-inflammatory cytokines were identified by mass spectrometry. Incidentally, the conserved hypothetical protein (Tsp_04814) was selected for further characterization as it presented the most significant MS score. An annotation of Tsp_04814 using protein structural homology comparison suggested that it has high structural similarity to human cystatin E/M (TM score 0.690). The recombinant T. spiralis novel cystatin (rTsCstN) was expressed in Escherichia coli at a molecular weight of approximately 13 kDa. Mouse anti-rTsCstN polyclonal antibody (pAb) could detect native TsCstN in crude worm antigens (CWA) and ES-L1 and be predominantly localized in the stichosome and subcuticular cells. rTsCstN inhibited cysteine proteases in vitro, especially cathepsin L, at an optimal pH of 6. Besides, rTsCstN could be internalized into mBMDMs, which were mostly distributed in the cytoplasm and lysosome both before and after LPS stimulation. To evaluate the rTsCstN immunomodulatory properties on mBMDMs, rTsCstN was incubated with mBMDM before LPS stimulation; this demonstrated that rTsCstN suppressed pro-inflammatory cytokine production and MHC class II expression.T. spiralis L1-derived TsCstN was characterized as a novel cysteine protease inhibitor. The protein elicits an anti-inflammatory property by suppressing pro-inflammatory cytokines and interfering with the antigen presentation process through depletion of MHC class II expression.

摘要

旋毛虫可以调节宿主的免疫反应,为其长期生存提供适宜的环境。此外,寄生虫通过释放免疫调节分子来发挥调节作用,这些分子可以抑制宿主的炎症反应,也许有朝一日可以用于治疗与炎症无关的疾病。在这里,我们鉴定并描述了一种新型旋毛虫半胱氨酸蛋白酶抑制剂(TsCstN),它可以抑制脂多糖处理的巨噬细胞介导的炎症。将旋毛虫肌幼虫期的排泄分泌产物(ES)进行分离,并在 LPS 刺激前用小鼠骨髓来源的巨噬细胞(mBMDMs)处理每个部分。通过质谱分析,鉴定出具有降低促炎细胞因子或增加抗炎细胞因子的高免疫调节特性的部分。偶然的是,选择保守的假设蛋白(Tsp_04814)进行进一步表征,因为它的 MS 评分最高。使用蛋白质结构同源性比较对 Tsp_04814 进行注释表明,它与人半胱氨酸蛋白酶抑制剂 E/M 具有高度结构相似性(TM 评分 0.690)。重组旋毛虫新型半胱氨酸蛋白酶抑制剂(rTsCstN)在大肠杆菌中以约 13 kDa 的分子量表达。小鼠抗 rTsCstN 多克隆抗体(pAb)可以检测粗虫抗原(CWA)和 ES-L1 中的天然 TsCstN,主要定位于口囊和皮下细胞。rTsCstN 在体外抑制半胱氨酸蛋白酶,尤其是组织蛋白酶 L,最佳 pH 值为 6。此外,rTsCstN 可以被内化到 mBMDMs 中,在 LPS 刺激前后,rTsCstN 主要分布在细胞质和溶酶体中。为了评估 rTsCstN 对 mBMDMs 的免疫调节特性,将 rTsCstN 与 LPS 刺激前的 mBMDM 孵育;结果表明 rTsCstN 抑制了促炎细胞因子的产生和 MHC Ⅱ类的表达。旋毛虫 L1 衍生的 TsCstN 被鉴定为一种新型的半胱氨酸蛋白酶抑制剂。该蛋白通过抑制促炎细胞因子的产生和通过 MHC Ⅱ类表达的耗竭干扰抗原呈递过程来发挥抗炎作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fa9b/7153903/f1e0bda572c4/pntd.0008192.g001.jpg

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