Two distinct oxysterol binding protein-related proteins in the parasitic protist Cryptosporidium parvum (Apicomplexa).
Two distinct oxysterol binding protein-related proteins in the parasitic protist Cryptosporidium parvum (Apicomplexa).
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寄生原生生物隐孢子虫（Apicomplexa）中两种不同的氧甾醇结合蛋白相关蛋白。
DOI：
10.1016/j.bbrc.2006.05.165
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发表时间：
2006
影响因子：
3.1
通讯作者：
Zhu,Guran
中科院分区：
文献类型：
--
作者：
Zeng,Bin;Zhu,Guran
从寄生原生生物微小隐孢子虫（Cryptosporidium parvum）中鉴定出两种不同的氧固醇结合蛋白（OSBP）相关蛋白（CpORP 1和CpORP 2）。短型CpOPR 1仅包含配体结合（LB）结构域，而长型CpORP 2包含Pleckstrin同源性（PH）和LB结构域。使用重组蛋白的脂质-蛋白质重叠分析显示，CpORP 1和CpORP 2可以特异性地结合磷脂酸（PA），各种磷脂酰肌醇磷酸（PIP），和硫苷脂，但不与其他类型的简单的头部的脂质。胆固醇不是这两种蛋白质的配体。CpOPR 1主要分布在寄生虫空泡膜（PVM）上，提示CpOPR 1可能参与了寄生虫和宿主肠腔之间的脂质转运。虽然隐孢子虫有两个氧化还原酶，其他apicomplexans包括疟原虫，弓形虫，艾美耳球虫只有一个长型氧化还原酶，这表明这个家族的蛋白质可能发挥不同的作用apicomplexans。
Two distinct oxysterol binding protein (OSBP)-related proteins (ORPs) have been identified from the parasitic protist Cryptosporidium parvum (CpORP1 and CpORP2). The short-type CpOPR1 contains only a ligand binding (LB) domain, while the long-type CpORP2 contains Pleckstrin homology (PH) and LB domains. Lipid–protein overlay assays using recombinant proteins revealed that CpORP1 and CpORP2 could specifically bind to phosphatidic acid (PA), various phosphatidylinositol phosphates (PIPs), and sulfatide, but not to other types of lipids with simple heads. Cholesterol was not a ligand for these two proteins. CpOPR1 was found mainly on the parasitophorous vacuole membrane (PVM), suggesting that CpORP1 is probably involved in the lipid transport across this unique membrane barrier between parasites and host intestinal lumen. Although Cryptosporidium has two ORPs, other apicomplexans including Plasmodium, Toxoplasma, and Eimeria possess only a single long-type ORP, suggesting that this family of proteins may play different roles among apicomplexans.