Wadhawan Mohit, Tiwari Savitri, Sharma Shweta, Rathaur Sushma
Department of Biochemistry, Institute of Science, Banaras Hindu University, Varanasi, India.
Department of Biochemistry, Institute of Science, Banaras Hindu University, Varanasi, India.
Biochem Biophys Res Commun. 2018 Jan 15;495(3):2235-2241. doi: 10.1016/j.bbrc.2017.12.093. Epub 2017 Dec 19.
A 75 kDa serine protease having prolyl oligopeptidase activity has been purified from Setaria cervi, a bovine filarial parasite. The MALDI-MS/MS analysis of the purified protein revealed 6 peptides showing nearest match S9A (prolyl oligopeptidase) family protein from Plesiocystis pacifica. The ScPOP was found to be unique compared to mammalian POP with respect to its kinetic properties. To elucidate its role, filarial parasites were exposed to specific inhibitor of POP, Z-Pro-prolinal (ZPP) for 8 h. The inhibition of POP induced calcium signaling via phospholipase c stimulation which further triggered mitochondrial mediated apoptosis in filarial parasites.
一种具有脯氨酰寡肽酶活性的75 kDa丝氨酸蛋白酶已从牛丝状寄生虫鹿丝状线虫中纯化出来。对纯化蛋白的基质辅助激光解吸电离串联质谱（MALDI-MS/MS）分析显示，有6种肽与太平洋近囊虫的S9A（脯氨酰寡肽酶）家族蛋白最为匹配。与哺乳动物的脯氨酰寡肽酶相比，鹿丝状线虫脯氨酰寡肽酶（ScPOP）的动力学特性具有独特性。为阐明其作用，将丝状寄生虫暴露于脯氨酰寡肽酶的特异性抑制剂Z-脯氨酰-脯氨醛（ZPP）中8小时。脯氨酰寡肽酶的抑制通过磷脂酶c刺激诱导钙信号传导，进而触发丝状寄生虫中线粒体介导的细胞凋亡。
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