Identification and characterization of a cathepsin L-like cysteine protease from Taenia solium metacestode

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• 作者：Ai Hua Li ; Sung-Ung Moon ; Yun-Kyu Park ; Byoung-Kuk Na ; Myung-Gi Hwang ; Chang-Mi Oh ; Shin-Hyeong Cho ; Yoon Kong ; Tong-Soo Kim and Pyung-Rim Chung
• 关键词：Taenia solium metacestode ; Cysteine protease ; Recombinant protein
• 刊名：Veterinary Parasitology
• 出版年：2006
• 出版时间：5 November 2006
• 年：2006
• 卷：141
• 期：3-4
• 页码：251-259
• 全文大小：1186 K

文摘

Taenia solium metacestode, a larval pork tapeworm, is a causative agent of neurocysticercosis, one of the most common parasitic diseases in the human central nervous system. In this study, we identified a cDNA encoding for a cathepsin L-like cysteine protease from the T. solium metacestode (TsCL-1) and characterized the biochemical properties of the recombinant enzyme. The cloned cDNA of 1216 bp encoded 339 amino acids with an approximate molecular weight of 37.6 kDa which containing a typical signal peptide sequence (17 amino acids), a pro-domain (106 amino acids), and a mature domain (216 amino acids). Sequence alignments of TsCL-1 showed low sequence similarity of 27.3–44.6 to cathepsin L-like cysteine proteases from other helminth parasites, but the similarity was increased to 35.9–55.0 when compared to mature domains. The bacterially expressed recombinant protein (rTsCL-1) did not show enzyme activity; however, the rTsCL-1 expressed in Pichia pastoris showed typical biochemical characteristics of cysteine proteases. It degraded human immunoglobulin G (IgG) and bovine serum albumin (BSA), but not collagen. Western blot analysis of the rTsCL-1 showed antigenicity against the sera from patients with cysticercosis, sparganosis or fascioliasis, but weak or no antigenicity against the sera from patients with paragonimiasis or clonorchiasis.