Diagnostic efficacy of a recombinant cysteine protease of Spirometra erinacei larvae for serodiagnosis of sparganosis.
S M Mazidur RahmanJae-Hwan KimSung-Tae HongMin-Ho ChoiPublished in: The Korean journal of parasitology (2014)
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 strongly reacted with the sparganum positive human or mice sera but not with negative sera by immunoblotting. ELISA with rSepCp-1 protein or sparganum crude antigen (SeC) was evaluated for the serodiagnosis of sparganosis using patient's sera. The sensitivity and specificity of ELISA using rSepCp-1 protein were 95.0% (19/20) and 99.1% (111/112), respectively. In contrast, the sensitivity and specificity of ELISA with SeC were 100% (20/20) and 96.4% (108/112), respectively. Moreover, in experimentally infected mice, the sensitivity and specificity of both ELISA assays were 100% for the detection of anti-sparganum IgG. It is suggested that the rSepCp-1 protein-based ELISA could provide a highly sensitive and specific assay for the diagnosis of sparganosis.
Keyphrases
- escherichia coli
- protein protein
- amino acid
- monoclonal antibody
- binding protein
- high throughput
- endothelial cells
- magnetic resonance
- fluorescent probe
- living cells
- metabolic syndrome
- type diabetes
- adipose tissue
- staphylococcus aureus
- biofilm formation
- induced pluripotent stem cells
- heat shock protein
- cystic fibrosis
- quantum dots
- insulin resistance
- pluripotent stem cells
- wild type
- single molecule