Molecular characterization of EcCLP1, a new putative cathepsin L protease from Echinococcus canadensis.

IF 2.3 2区 医学 Q2 PARASITOLOGY Parasite Pub Date : 2024-01-01 Epub Date: 2024-07-09 DOI:10.1051/parasite/2024036
Ariel Naidich, Ariana M Gutierrez, Federico Camicia
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Abstract

Echinococcus granulosus sensu lato is a platyhelminth parasite and the etiological cause of cystic echinococcosis (CE), a zoonotic and neglected disease that infects animals and humans worldwide. As a part of the biological arsenal of the parasite, cathepsin L proteases are a group of proteins that are believed to be essential for parasite penetration, immune evasion, and establishment in the tissues of the host. In this work, we have cloned and sequenced a new putative cathepsin L protease from Echinococcus canadensis (EcCLP1). The bioinformatic analysis suggests that EcCLP1 could be synthesized as a zymogen and activated after proteolytic cleavage. The multiple sequence alignment with other cathepsin proteases reveals important functional conserved features like a conserved active site, an N-linked glycosylation residue, a catalytic triad, an oxyanion hole, and three putative disulfide bonds. The phylogenetic analysis suggests that EcCLP1 could indeed be a cathepsin L cysteine protease from clade 1 as it grouped with cathepsins from other species in this clade. Modeling studies suggest that EcCLP1 has two domains forming a cleft where the active site is located and an occluding role for the propeptide. The transcriptomic analysis reveals different levels of cathepsin transcript expression along the different stages of the parasite life cycle. The whole-mount immunohistochemistry shows an interesting superficial punctate pattern of staining which suggests a secretory pattern of expression. The putative cathepsin L protease characterized here may represent an interesting tool for diagnostic purposes, vaccine design, or a new pharmacological target for antiparasitic intervention.

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EcCLP1 的分子特征,ECLP1 是一种来自犬棘球蚴的新的推定 cathepsin L 蛋白酶。
普通棘球蚴是一种扁形动物寄生虫,也是囊性棘球蚴病(CE)的病原体,这是一种人畜共患且被忽视的疾病,世界各地的动物和人类都会感染这种疾病。作为寄生虫生物武库的一部分,螯合蛋白 L 蛋白酶是一组被认为对寄生虫的渗透、免疫逃避和在宿主组织中的建立至关重要的蛋白质。在这项工作中,我们克隆并测序了一种来自犬棘球蚴的新的假定性 cathepsin L 蛋白酶(EcCLP1)。生物信息学分析表明,ECCLP1 可以作为一种酶原合成,并在蛋白水解裂解后被激活。与其他酪蛋白蛋白酶的多重序列比对显示了重要的功能保守特征,如一个保守的活性位点、一个N-连接的糖基化残基、一个催化三元组、一个氧阴离子孔和三个假定的二硫键。系统进化分析表明,EcCLP1 确实可能是来自第一支系的一种半胱氨酸蛋白酶,因为它与该支系中其他物种的蛋白酶归为一类。建模研究表明,EcCLP1 有两个结构域,形成一个活性位点所在的裂隙,并对前肽起闭锁作用。转录组分析显示,在寄生虫生命周期的不同阶段,螯合蛋白转录本的表达水平不同。整装免疫组化显示了一种有趣的表层点状染色模式,表明这是一种分泌型表达模式。这里描述的假定的钙蛋白 L 蛋白酶可能是一种有趣的工具,可用于诊断、疫苗设计或抗寄生虫干预的新药理靶点。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Parasite
Parasite 医学-寄生虫学
CiteScore
5.50
自引率
6.90%
发文量
49
审稿时长
3 months
期刊介绍: Parasite is an international open-access, peer-reviewed, online journal publishing high quality papers on all aspects of human and animal parasitology. Reviews, articles and short notes may be submitted. Fields include, but are not limited to: general, medical and veterinary parasitology; morphology, including ultrastructure; parasite systematics, including entomology, acarology, helminthology and protistology, and molecular analyses; molecular biology and biochemistry; immunology of parasitic diseases; host-parasite relationships; ecology and life history of parasites; epidemiology; therapeutics; new diagnostic tools. All papers in Parasite are published in English. Manuscripts should have a broad interest and must not have been published or submitted elsewhere. No limit is imposed on the length of manuscripts, but they should be concisely written. Papers of limited interest such as case reports, epidemiological studies in punctual areas, isolated new geographical records, and systematic descriptions of single species will generally not be accepted, but might be considered if the authors succeed in demonstrating their interest.
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