Molecular characterization and expression of the MYND-ZF gene from Clonorchis sinensis

• Published in: Parasitology research (1987) Vol. 107; no. 5; pp. 1249 - 1255
• Main Authors: Wang, Lexun, Yu, Xinbing, Yang, Yabo, Chen, Jingfang, Hu, Dong, Deng, Chuanhuan, Yang, Xiao, Hu, Xuchu, Xu, Jin
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Berlin/Heidelberg : Springer-Verlag 01.10.2010; Springer-Verlag; Springer
• Subjects: Amino Acid Sequence; Amino acids; Animals; Biological and medical sciences; Biomedical and Life Sciences; Biomedicine; Cloning, Molecular; Clonorchis sinensis; Clonorchis sinensis - chemistry; Clonorchis sinensis - genetics; DNA, Complementary - genetics; DNA, Complementary - isolation & purification; DNA, Helminth - genetics; DNA, Helminth - isolation & purification; Escherichia coli; Escherichia coli - genetics; Fundamental and applied biological sciences. Psychology; Gene Expression; General aspects; General aspects and techniques. Study of several systematic groups. Models; Helminth Proteins - analysis; Helminth Proteins - genetics; Immunohistochemistry; Immunology; Invertebrates; Medical Microbiology; Microbiology; Molecular Sequence Data; Open Reading Frames; Original Paper; Protein Structure, Tertiary; Protein-protein interactions; Proteins; Recombinant Proteins - biosynthesis; Recombinant Proteins - immunology; Recombinant Proteins - isolation & purification; Sequence Alignment; Sequence Homology, Amino Acid; Zinc Fingers - genetics; Adult Worm; Zinc Finger Domain; Bile Duct; Zinc Finger; Esophageal Squamous Cell Carcinoma; Gene; Helmintha; Plathelmintha; Parasite; Clonorchis sinensis; Invertebrata; Trematoda
• ISSN: 0932-0113; 1432-1955
• DOI: 10.1007/s00436-010-1995-7

The MYND-type zinc finger protein (MYND-ZF) is a large group of proteins containing the MYND domain which play an important role in protein-protein interactions. A cDNA clone encoding a novel MYND-ZF was isolated and identified from a Clonorchis sinensis (C. sinensis) adult cDNA library. The open reading frame of this novel cDNA sequence contains 1,440 base pairs with a putative protein of 479 amino acids showing a high homology with the MYND-ZF identified from other species. Recombinant CsMYND-ZF was expressed and purified from Escherichia coli BL21 (DE3). CsMYND-ZF transcripts were detected in the cDNA of adult worms and metacercariae but not in eggs of C. sinensis. Immunohistochemistry results revealed that CsMYND-ZF was deposited at the tegument of adult worms and metacercariae C. sinensis using anti-recombinant CsMYND-ZF serum. These findings may contribute to the development of a reliable diagnostic method.