Hemolytic activity and developmental expression of pore-forming peptide, clonorin.
Peptides pore-forming in cell membrane have been identified from a wide range of animals. A putative pore-forming peptide deduced from a cDNA clone of Clonorchis sinensis (clonorin) was predicted to consist of four amphipathic alpha-helices. Clonorin contained six invariably conserved cysteine residues, identified to form three disulfide bonds. These predicted structural features are highly homologous with pore-forming peptides, the amoebapores. Recombinant clonorin showed hemolytic activity toward rabbit erythrocytes. The hemolytic activity of C. sinensis extract increased dose-dependently and was inhibited by anti-clonorin immune sera. The clonorin was expressed developmentally in juvenile and adult flukes and localized in the intestinal epithelium of adult flukes. It is proposed that, through lysing host cellular components, clonorin could enhance proteolytic digestion in the intestine of C. sinensis.
Department of Parasitology, Chung-Ang University College of Medicine, Tongjak-gu, 156-756, Seoul, Republic of Korea.
Ji-Yun
JY
Lee
Pyo-Yun
PY
Cho
Tae Yun
TY
Kim
Shin-Yong
SY
Kang
Kye-Yong
KY
Song
Sung-Jong
SJ
Hong
D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D003004:Clonorchis sinensis / Q000254:growth & development* / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D015801:Helminth Proteins / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology*; D006460:Hemolysin Proteins / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology*; D006461:Hemolysis; D007413:Intestinal Mucosa / Q000737:chemistry; D008969:Molecular Sequence Data; D010455:Peptides / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology; D017433:Protein Structure, Secondary; D011817:Rabbits; D011993:Recombinant Fusion Proteins / Q000494:pharmacology; D016415:Sequence Alignment
C406725:FHAP protein, Fasciola hepatica; D015801:Helminth Proteins; D006460:Hemolysin Proteins; D010455:Peptides; D011993:Recombinant Fusion Proteins