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Identification and characterization of a cathepsin L-like cysteine protease from Taenia solium metacestode
Li, Ai Hua; Moon, Sung-Ung; Park, Yun-Kyu; Na, Byoung-Kuk; Hwang, Myung-Gi; Oh, Chang-Mi; Cho, Shin-Hyeong; Kong, Yoon; Kim, Tong-Soo; Chung, Pyung-Rim; Chung, PR, Inha Univ, Coll Med, Dept Parasitol, Inchon 400712, South Korea
2006-11-05
Source PublicationVETERINARY PARASITOLOGY
ISSN0304-4017
Volume141Issue:3-4Pages:251-259
AbstractTaenia 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. (c) 2006 Published by Elsevier B.V.; 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. (c) 2006 Published by Elsevier B.V.
SubtypeArticle
KeywordTaenia Solium Metacestode Cysteine Protease Recombinant Protein
DepartmentInha Univ, Coll Med, Dept Parasitol, Inchon 400712, South Korea; Korea Ctr Dis Control & Prevent, Natl Inst Hlth, Dib Malaria & Parasit Dis, Seoul 122701, South Korea; Chinese Acad Sci, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan 430072, Peoples R China; Gyeongsang Natl Univ, Coll Med, Dept Parasitol, Jinju 660751, South Korea; Gyeongsang Natl Univ, Coll Med, Inst Hlth Sci, Jinju 660751, South Korea; Sungkyunkwan Univ, Sch Med, Suwon 440746, South Korea; Samsung Biomed Res Inst, Dept Mol Parasitol, Suwon 440746, South Korea; Samsung Biomed Res Inst, Ctr Mol Med, Suwon 440746, South Korea
Subject AreaParasitology ; Veterinary Sciences
DOI10.1016/j.vetpar.2006.05.015
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
Indexed BySCI
Language英语
WOS Research AreaParasitology ; Veterinary Sciences
WOS SubjectParasitology ; Veterinary Sciences
WOS IDWOS:000241720000007
WOS KeywordPARAGONIMUS-WESTERMANI ; PROTEINASE
Citation statistics
Cited Times:23[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ihb.ac.cn/handle/152342/8802
Collection期刊论文
Corresponding AuthorChung, PR, Inha Univ, Coll Med, Dept Parasitol, Inchon 400712, South Korea
Affiliation1.Inha Univ, Coll Med, Dept Parasitol, Inchon 400712, South Korea
2.Korea Ctr Dis Control & Prevent, Natl Inst Hlth, Dib Malaria & Parasit Dis, Seoul 122701, South Korea
3.Chinese Acad Sci, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan 430072, Peoples R China
4.Gyeongsang Natl Univ, Coll Med, Dept Parasitol, Jinju 660751, South Korea
5.Gyeongsang Natl Univ, Coll Med, Inst Hlth Sci, Jinju 660751, South Korea
6.Sungkyunkwan Univ, Sch Med, Suwon 440746, South Korea
7.Samsung Biomed Res Inst, Dept Mol Parasitol, Suwon 440746, South Korea
8.Samsung Biomed Res Inst, Ctr Mol Med, Suwon 440746, South Korea
Recommended Citation
GB/T 7714
Li, Ai Hua,Moon, Sung-Ung,Park, Yun-Kyu,et al. Identification and characterization of a cathepsin L-like cysteine protease from Taenia solium metacestode[J]. VETERINARY PARASITOLOGY,2006,141(3-4):251-259.
APA Li, Ai Hua.,Moon, Sung-Ung.,Park, Yun-Kyu.,Na, Byoung-Kuk.,Hwang, Myung-Gi.,...&Chung, PR, Inha Univ, Coll Med, Dept Parasitol, Inchon 400712, South Korea.(2006).Identification and characterization of a cathepsin L-like cysteine protease from Taenia solium metacestode.VETERINARY PARASITOLOGY,141(3-4),251-259.
MLA Li, Ai Hua,et al."Identification and characterization of a cathepsin L-like cysteine protease from Taenia solium metacestode".VETERINARY PARASITOLOGY 141.3-4(2006):251-259.
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