|Budget Amount *help
¥2,300,000 (Direct Cost : ¥2,300,000)
Fiscal Year 1996 : ¥1,000,000 (Direct Cost : ¥1,000,000)
Fiscal Year 1995 : ¥1,300,000 (Direct Cost : ¥1,300,000)
Recombinant DNA technology is increasingly being applied to the isolation and identification of parasite antigens. Although cysteine protease has been reported as the major antigen of Paragonimus, characteristics of the other antigens have remained unclear. We reported four cathepsin L-like proteins as antigens from cDNA library of adult P.miyazakii using molecular biology technique. Three clones were isolated from P.miyazakii cDNA library with IgG of infected rat in addition to 4 cDNAs of cysteine protease in the present investigation. These clones were 1,095-1,552 bp with poly (A) tail and lacked their 5' ends. These clones are related to heat-shock protein 70 family, especially heat-shock cognate 70 protein. These three clones are related to cytoplasmic heat-shock protein 70 homologs and have no KDEL sequence which is C terminal endoplasmic reticulum retention sequence. Heat-shock protein 70 recent has their importance in normal cellular processes such as protein folding, assembly, disassembly and degradation. Heat-shock protein also plays a major role in the immune response to variety of parasitic infections, i.e. trypanosomiasis, leishmaniasis, malaria, giardiaisis, toxoplasmosis, filariasis, schistosomiasis, mesocestoidiasis. One possible role of heat-shock proteins is repair or removal of damaged parasite proteins caused by various immune mediators.