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sparganosis/l cystein
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14 Ergebnisse
Serodiagnosis of sparganosis by ELISA using recombinant cysteine protease of Spirometra erinaceieuropaei spargana.
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The Spirometra erinaceieuropaei cysteine protease (SeCP) gene encoding a 36 kDa protein was expressed in Escherichia coli, and the potential of recombinant SeCP protein (rSeCP) as an antigen for the serodiagnosis of sparganosis was investigated by ELISA and compared with those of ELISA with
Diagnostic efficacy of a recombinant cysteine protease of Spirometra erinacei larvae for serodiagnosis of sparganosis.
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The mature domain of a cysteine protease of Spirometra erinacei plerocercoid larva (i.e., sparganum) was expressed in Escherichia coli, and its value as an antigen for the serodiagnosis of sparganosis was investigated. The recombinant protein (rSepCp-1) has the molecular weight of 23.4 kDa, and
Characterization of Spirometra erinaceieuropaei Plerocercoid Cysteine Protease and Potential Application for Serodiagnosis of Sparganosis.
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BACKGROUND
Sparganosis is a neglected but important food-borne parasitic zoonosis. Clinical diagnosis of sparganosis is difficult because there are no specific manifestations. ELISA using plerocercoid crude or excretory-secretory (ES) antigens has high sensitivity but has cross-reactions with other
A cysteine protease from Spirometra erinaceieuropaei plerocercoid is a critical factor for host tissue invasion and migration.
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Sparganosis in humans caused by the plerocercoid larvae of Spirometra erinaceieuropaei is found worldwide, especially in Eastern Asia and the Far East. Previous studies have suggested that dissolution of plerocercoid body, plerocercoid invasion of host tissue, and migration are important processes
Differential expression of the 27 kDa cathepsin L-like cysteine protease in developmental stages of Spirometra erinacei.
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The 27 kDa cathepsin L-like cysteine protease of Spirometra erinacei plerocercoid is known to play an important function in tissue penetration, nutrient uptake and immune modulation in human sparganosis. In the present study, the expression of this enzyme was examined at different developmental
Purification and partial characterization of cysteine proteinase from Spirometra mansoni plerocercoids.
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Spirometra mansoni plerocercoids were dissected from the tissues of naturally infected snakes (Natrix trigrialateralia). Fresh plerocercoids were incubated in medium, and excretory-secretory products (E-S) were collected. In addition, soluble proteins from lyophilized plerocercoids (10 mg/ml) were
Cloning and characterization of a new cysteine proteinase secreted by Paragonimus westermani adult worms.
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The cysteine proteinases of Paragonimus westermani are known to play important roles in invasion and pathogenesis to hosts and in immune modulation and nutrient uptake. In this study, we have cloned a new cysteine proteinase of P. westermani, PwCP2, from adult worms and tested its diagnostic
Isolation and partial characterization of cysteine proteinase from sparganum.
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A proteolytic enzyme was purified from the tissue extract of spargana (plerocercoids of Spirometra erinacei) by DEAE-Trisacryl M ion exchange chromatography and thiopropyl-sepharose affinity chromatography resulted in a 21-fold purification. The proteinase activity was assayed with a synthetic
Identification and characterization of a cathepsin L-like cysteine protease from Taenia solium metacestode.
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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)
Expression of cysteine proteinase of Clonorchis sinensis and its use in serodiagnosis of clonorchiasis.
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A gene encoding cysteine proteinase from Clonorchis sinensis has been cloned and expressed in Escherichia coli. The cysteine proteinase cDNA fragment was amplified by reverse transcription-polymerase chain reaction using degenerate oligonucleotide primers derived from conserved active site of
Molecular cloning and characterization of plerocercoid-immunosuppressive factor from Spirometra erinaceieuropaei.
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A platyhelminth, Spirometra erinaceieuropaei, belonging to the class Cestoda, causes human sparganosis, and infection with its larva results in subtle inflammation in the body of its host. We previously reported the purification of a glycoprotein, plerocercoid-immunosuppressive factor (P-ISF) from
Identification of early diagnostic antigens from Spirometra erinaceieuropaei sparganum soluble proteins using immunoproteomics.
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In order to identify early specific diagnostic antigens of Spirometra erinaceieuropaei (syn. S. erinacei or S. mansoni) sparganum, soluble proteins were analyzed by two-dimensional electrophoresis (2-DE) and western blotting probed with immune sera from infected mice at 14 days post-infection. From
Immunoproteomic Analysis of the Excretory-Secretory Proteins from Spirometra mansoni Sparganum.
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BACKGROUND
Sparganosis is caused by the invasion of Spirometra sparganum into various tissues/organs. Subcutaneous sparganosis can be diagnosed by biopsy, while visceral/cerebral sparganosis is not easy to be diagnosed. The diagnosis depends largely on the detection of specific anti-sparganum
Cystatin capture enzyme-linked immunosorbent assay for serodiagnosis of human clonorchiasis and profile of captured antigenic protein of Clonorchis sinensis.
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Enzyme-linked immunosorbent assay (ELISA) with crude extracts of adult Clonorchis sinensis has been reported to have a high degree of sensitivity with a moderate degree of specificity for the serodiagnosis of clonorchiasis. The cystatin capture ELISA was investigated for its usefulness for the
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