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A lysosomal hydrolase receptor, CPBF2, is associated with motility and invasion of the enteric protozoan parasite Entamoeba histolytica.
Molecular and Biochemical Parasitology ( IF 1.5 ) Pub Date : 2020-07-21 , DOI: 10.1016/j.molbiopara.2020.111299
Kumiko Nakada-Tsukui 1 , Konomi Marumo 2 , Tomoyoshi Nozaki 3
Affiliation  

Proper targeting and secretion of lysosomal hydrolases are regulated by transporting receptors. Entamoeba histolytica, the enteric protozoan parasite responsible for human amebiasis, has a unique family of lysosomal hydrolase receptors, cysteine protease binding protein family, CPBF. CPBFs, consisting of 11 members with conserved domain organization, bind to a wide range of cargos including cysteine proteases and glycosidases, which are also known to be involved in pathogenesis of this parasite. In this study, we characterized one of CPBFs, CPBF2, which is involved in cell motility and extracellular matrix invasion. Unexpectedly, these roles of CPBF were not related to its cargo, α-amylase. This is the first demonstration that a putative hydrolase receptor is involved in cell motility and invasion in parasitic protozoa.



中文翻译:

溶酶体水解酶受体,CPBF2,与肠原生动物寄生虫组织型变形杆菌的运动性和侵袭性有关。

溶酶体水解酶的正确靶向和分泌受转运受体的调节。溶组织性变形虫负责人类阿米巴病的肠道原生动物寄生虫,具有独特的溶酶体水解酶受体家族,半胱氨酸蛋白酶结合蛋白家族CPBF。CPBF由11个具有保守域结构的成员组成,可与多种货物结合,包括半胱氨酸蛋白酶和糖苷酶,它们也已知与该寄生虫的发病机理有关。在这项研究中,我们表征了CPBF之一CPBF2,它参与细胞运动和细胞外基质的侵袭。出乎意料的是,CPBF的这些作用与其货物α-淀粉酶无关。这是第一个证明推定的水解酶受体参与寄生虫原生动物的细胞运动和侵袭的证明。

更新日期:2020-07-21
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