A 7-kDa protein was purified from extracts of adult Clonorchis sinensis by a combination of ammonium sulfate precipitation, anion exchange chromatography, cation exchange chromatography, gel-filtration chromatography, and reversed-phase FPLC. The 7-kDa protein exists in the excretory–secretory products of adult C. sinensis, but not in extracts of adult Paragonimus westermani. Also, the 7-kDa protein reacted with the sera of patients with clonorchiasis but not with paragonimiasis or normal human sera. To observe the localization of the 7-kDa protein in the tissue of adult C. sinensis, an immunogold labeling method was followed using anti-7-kDa antibody. The gold particles were observed in the basal layer below the tegumental syncytium, in the interstitial matrix of the parenchyma, and in the content of the uterus. The 7-kDa cDNA was obtained through reverse transcription-polymerase chain reaction using a primer designed from N-terminal sequence analysis. Rapid amplification of cDNA ends (5′-RACE) was used to obtain the complete protein coding sequence. The sequence encodes a 90-amino acid polypeptide. The deduced amino acid sequence of the 7-kDa protein revealed no homology with proteins of different organisms reported so far. These results suggest that the 7-kDa protein is a fluid antigen and may be valuable as a tool for the immunodiagnosis of clonorchiasis.
PURIFICATION AND CHARACTERIZATION OF A 7-KDA PROTEIN FROM CLONORCHIS SINENSIS ADULT WORMS
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Hye-Jeong Lee, Chang-Seok Lee, Beom-Su Kim, Kyoung-Hwan Joo, Joon-Sang Lee, Tong-Soo Kim, Hak R. Kim; PURIFICATION AND CHARACTERIZATION OF A 7-KDA PROTEIN FROM CLONORCHIS SINENSIS ADULT WORMS. J Parasitol 1 June 2002; 88 (3): 499–504. doi: https://doi.org/10.1645/0022-3395(2002)088[0499:PACOAK]2.0.CO;2
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