Clonorchis sinensis: molecular cloning and localization of myosin regulatory light chain.
One cDNA clone was purified from an adult Clonorchis sinensis cDNA library, and its deduced polypeptide sequence was found to be homologous with myosin regulatory light chain (MRLC) of invertebrates and vertebrates. Two amino-acid residues, Thr and Ser, were conserved at the phosphorylation sites that regulate the function of MRLCs. Recombinant C. sinensis MRLC (rCsMRLC) protein was produced and purified from Escherichia coli, and mouse anti-CsMRLC immune sera recognized a protein of molecular weight 24 kDa from a soluble protein preparation of C. sinensis. The CsMRLC protein was immunohistochemically localized to the muscle fibers of the subtegumental muscle layer and to the muscles of oral and ventral suckers. However, the rCsMRLC protein proved to be less useful antigen for the serodiagnosis of human clonorchiasis.
Kwon
Yeong-Deok
YD
Department of Parasitology, Chung-Ang University College of Medicine, Tongjak-gu, Seoul 156-756, Republic of Korea.
Cho
Pyo Yun
PY
Hong
Sung-Jong
SJ
D000595:Amino Acid Sequence; D000818:Animals; D000909:Antibodies, Helminth; D001483:Base Sequence; D003001:Cloning, Molecular; D003004:Clonorchis sinensis / Q000235:genetics*; D017124:Conserved Sequence; D006801:Humans; D007150:Immunohistochemistry; D008969:Molecular Sequence Data; D018485:Muscle Fibers, Skeletal / Q000737:chemistry; D018994:Myosin Light Chains / Q000032:analysis* / Q000737:chemistry / Q000235:genetics*; D016366:Open Reading Frames; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
D000909:Antibodies, Helminth; D018994:Myosin Light Chains