paragonimiasis/l cisteină

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Protein A immunocapture assay detecting antibodies to fluke cysteine proteinases for immunodiagnosis of human paragonimiasis and fascioliasis.

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Enzyme-linked immunosorbent assays (ELISAs) which detect specific antibodies to fluke cysteine proteinases have provided good sensitivity and specificity for the immunodiagnosis of trematode diseases. To detect specific antibodies without the need for purified proteinase antigens, an immunocapture

Enzyme-linked immunosorbent assay using cysteine proteinase antigens for immunodiagnosis of human paragonimiasis.

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An enzyme-linked immunsorbent assay (ELISA) using worm extract antigens from lung flukes of Paragonimus westermani provided good sensitivity to sera from patients with paragonimiasis westermani but high cross-reactivity with sera from most fascioliasis patients and some patients with onchocerciasis

Cysteine protease secreted by Paragonimus westermani attenuates effector functions of human eosinophils stimulated with immunoglobulin G.

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An immunoglobulin G (IgG)-coated surface, such as that found on helminth parasites, is one of the most effective physiologic stimuli for eosinophil activation. The cysteine proteases secreted by tissue-invasive helminth larvae play an important role in evasion of the immune response by degrading the

[Cloning, expression and evaluation on effect in serological diagnosis of cysteine protease of Clonorchis sinensis].

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OBJECTIVE To clone and express the cysteine protease of Clonorchis sinensis and evaluate its effect on immunodiagnosis of human clonorchiasis. METHODS Based on a cysteine protease gene fragment of C. sinensis (CS-CP, GenBank accession: AF093242), a pair of primers were designed and amplified from

Proteolytic activity of cysteine protease in excretory-secretory product of Paragonimus westermani newly excysted metacercariae pivotally regulates IL-8 production of human eosinophils.

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This study investigated the effect of the excretory-secretory product (ESP) of Paragonimus westermani newly excysted metacercariae (PwNEM) on IL-8 production of human mature eosinophils. Treatment of eosinophils with lower concentrations (0.3 and 1 microg/ml) of the ESP significantly (P < 0.01)

Structural and immunological characteristics of a 28-kilodalton cruzipain-like cysteine protease of Paragonimus westermani expressed in the definitive host stage.

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A complete cDNA sequence encoding a 28-kDa cruzipain-like cysteine protease of adult Paragonimus westermani, termed Pw28CCP, was isolated from an adult cDNA library. The cDNA contained a single open reading frame of 975 bp encoding 325 amino acids, which exhibited the structural motif and domain

Molecular and biochemical characterization of hemoglobinase, a cysteine proteinase, in Paragonimus westermani.

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The mammalian trematode Paragonimus westermani is a typical digenetic parasite, which can cause paragonimiasis in humans. Host tissues and blood cells are important sources of nutrients for development, growth and reproduction of P. westermani. In this study, a cDNA clone encoding a 47 kDa

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

Characterization of a cysteine proteinase from adult worms of Paragonimus westermani.

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Paragonimus westermani, the lung fluke, is known to migrate to the pulmonary tissue of mammalian hosts and causes pathological changes in the lungs. An acidic thiol-dependent proteinase with a molecular weight of approximately 20,000 daltons was purified to homogeneity using ion-exchange

Characterization and classification of five cysteine proteinases expressed by Paragonimus westermani adult worm.

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Three new members of the cysteine proteinase gene family of Paragonimus westermani have been isolated and classified. Comparisons of the predicted amino acid sequences of PwCP2 (U69121), PwCP4 (U56958), and PwCP5 (U33215) were performed with those of the previously reported PwCP1 (U69120) and PwCP3

Cystatin capture enzyme-linked immunosorbent assay for immunodiagnosis of human paragonimiasis and fascioliasis.

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An ELISA was developed using chicken cystatin as a capture agent for the immunodiagnosis of paragonimiasis and fascioliasis. The assay detected specific antibodies to fluke cysteine proteinases without the need for purified proteinases. An ELISA plate was sensitized with chicken egg white cystatin,

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)

A 27 kDa cysteine protease secreted by newly excysted Paragonimus westermani metacercariae induces superoxide anion production and degranulation of human eosinophils.

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Eosinophil degranulation plays a crucial role in tissue inflammatory reactions associated with helminth parasitic infections and allergic diseases. Paragonimus westermani, a lung fluke causing human paragonimiasis, secretes a large amount of cysteine proteases, which are involved in nutrient uptake,

Cloning and expression of a cysteine proteinase gene from Paragonimus westermani adult worms.

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A gene encoding a cysteine proteinase from Paragonimus westermani has been cloned and expressed in Escherichia coli. The cysteine proteinase cDNA fragment was amplified by reverse transcription-polymerase chain reaction (RT-PCR) using degenerate oligonucleotide primers derived from the conserved

Molecular and immunological characterization of cathepsin L-like cysteine protease of Paragonimus pseudoheterotremus.

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Cathepsin L is a cysteine protease belonging to the papain family. In parasitic trematodes, cathepsin L plays essential roles in parasite survival and host-parasite interactions. In this study, cathepsin L of the lung fluke Paragonimus pseudoheterotremus (PpsCatL) was identified and its molecular

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