| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 3417941 | Parasitology International | 2012 | 5 Pages |
A cathepsin B-like cysteine protease belonging to family C1 is abundantly expressed in the transcriptome and proteome of the carcinogenic liver fluke of humans, Opisthorchis viverrini. This enzyme is present in excretory/secretory (ES) products released by parasites cultured in vitro. This study evaluated the performance of recombinant O. viverrini cathepsin B1 (rOv-CB-1) as an antigen for immunodiagnosis of opisthorchiasis. The full length Ov-CB-1 cDNA was cloned and recombinant protein was produced in catalytically active form in Pichia pastoris. The recombinant Ov-CB-1 (rOv-CB-1) was affinity purified via nickel-NTA chromatography and tested in enzyme-linked immunosorbent assays (ELISA) with human sera from an opisthorchiasis endemic area. Sera from egg-positive O. viverrini infections produced a strong IgG antibody response to rOv-CB-1 both in ELISA and immunoblot analysis. The sensitivity and specificity of the ELISA test was 67% and 81%, respectively. These findings support the feasibility of using recombinant Ov-CB-1 in ELISA for the serodiagnosis of human opisthorchiasis.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideResearch highlights► A cathepsin protease of Opisthorchis viverrini produced in yeast ► The recombinant protease, rOv-CB-1 recognized by sera from O. viverrini infected persons ► Using ELISA, rOv-CB-1 showed 67% sensitivity and 81% specificity for human opisthorchiasis.
