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鉴定和描述巨肾虫(Dioctophyme renale)主要假体腔蛋白。

Identification and characterization of the major pseudocoelomic proteins of the giant kidney worm, Dioctophyme renale.

机构信息

Instituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), Facultad de Ciencias Médicas, Universidad Nacional de La Plata, La Plata, Argentina.

Institute of Biodiversity, Animal Health and Comparative Medicine, University of Glasgow, G12 8QQ, Glasgow, UK.

出版信息

Parasit Vectors. 2017 Sep 27;10(1):446. doi: 10.1186/s13071-017-2388-x.

DOI:10.1186/s13071-017-2388-x
PMID:28954629
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5615634/
Abstract

BACKGROUND

The giant kidney worm, Dioctophyme renale, is a debilitating and potentially lethal parasite that inhabits and destroys, typically host's right kidney, and may also be found in ectopic sites. It is circumglobally distributed, mainly in dogs, and is increasingly regarded as a threat to other domestic animals and humans. There is little information on the parasite's true incidence, or immune responses to it, and none on its biochemistry and molecular biology.

RESULTS

We characterised the soluble proteins of body wall, intestine, gonads and pseudocelomic fluid (PCF) of adult parasites. Two proteins, P17 and P44, dominate the PCF of both male and females. P17 is of 16,622 Da by mass spectrometry, and accounts for the intense red colour of the adult parasites. It may function to carry or scavenge oxygen and be related to the 'nemoglobins' found in other nematode clades. P44 is of 44,460 Da and was found to associate with fatty acids by thin layer chromatography. Using environment-sensitive fluorescent lipid probes, P44 proved to be a hydrophobic ligand-binding protein with a binding site that is highly apolar, and competitive displacement experiments showed that P44 binds fatty acids. It may therefore have a role in distributing lipids within the parasites and, if also secreted, might influence local inflammatory and tissue responses. N-terminal and internal peptide amino-acid sequences of P44 indicate a relationship with a cysteine- and histidine-rich protein of unknown function from Trichinella spiralis.

CONCLUSIONS

The dominant proteins of D. renale PCF are, like those of large ascaridids, likely to be involved in lipid and oxygen handling, although there is evidence of strong divergence between the two groups.

摘要

背景

巨肾虫,Dioctophyme renale,是一种衰弱且潜在致命的寄生虫,它栖息并破坏宿主的右肾,也可能在异位部位发现。它在全球范围内分布,主要在狗中,并越来越被认为是对其他家畜和人类的威胁。关于寄生虫的真实发病率或对其的免疫反应,以及关于其生物化学和分子生物学的信息很少。

结果

我们对成虫体壁、肠、性腺和假体腔液(PCF)的可溶性蛋白进行了特征描述。两种蛋白,P17 和 P44,主导着雌雄成虫 PCF。P17 通过质谱法测定分子量为 16622Da,它解释了成虫的强烈红色。它可能具有携带或清除氧气的功能,并与在其他线虫类群中发现的“血绿蛋白”有关。P44 的分子量为 44460Da,通过薄层层析发现它与脂肪酸有关。使用环境敏感荧光脂质探针,P44 被证明是一种疏水性配体结合蛋白,其结合位点高度非极性,竞争置换实验表明 P44 结合脂肪酸。因此,它可能在寄生虫内分配脂质方面发挥作用,如果也分泌出来,可能会影响局部炎症和组织反应。P44 的 N 端和内部肽氨基酸序列表明它与旋毛虫中一种未知功能的富含半胱氨酸和组氨酸的蛋白质有关。

结论

D. renale PCF 的主要蛋白质,与大型蛔虫的蛋白质一样,可能参与脂质和氧气处理,尽管两组之间存在明显的差异。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/27c9/5615634/250792e866b1/13071_2017_2388_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/27c9/5615634/489a6c920592/13071_2017_2388_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/27c9/5615634/0df2b67ed9b5/13071_2017_2388_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/27c9/5615634/69d528539eac/13071_2017_2388_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/27c9/5615634/45f264669f47/13071_2017_2388_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/27c9/5615634/5244b2234b52/13071_2017_2388_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/27c9/5615634/250792e866b1/13071_2017_2388_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/27c9/5615634/489a6c920592/13071_2017_2388_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/27c9/5615634/0df2b67ed9b5/13071_2017_2388_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/27c9/5615634/69d528539eac/13071_2017_2388_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/27c9/5615634/45f264669f47/13071_2017_2388_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/27c9/5615634/5244b2234b52/13071_2017_2388_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/27c9/5615634/250792e866b1/13071_2017_2388_Fig6_HTML.jpg

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