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热休克蛋白(hsp70)普通存在于原核、真核细胞生物内。该蛋白在不同生物之间呈现高度保守性,提示寄生虫的hsp70抗体有可能与宿主hsp70有交叉反应。hsp70在血吸虫、利什曼原虫、锥虫、盘尾丝虫和疟原虫等寄生虫感染中是主要的免疫原;已证实hsp70在其它免疫性疾病中是自身免疫的靶蛋白。本文用hsp70作模式蛋白,研究与包虫病患者自身抗原同源的细粒棘球蚴(E.g)抗原的免疫活性,进而探讨包虫的免疫逃避机制。
Heat shock protein (hsp70) is commonly found in prokaryotic and eukaryotic organisms. The protein is highly conserved among different organisms, suggesting that the parasite hsp70 antibody may cross-react with the host hsp70. hsp70 is the major immunogen in parasitic infections such as schistosomes, Leishmania, trypanosomes, onchocerciasis and malaria parasites; hsp70 has been shown to be the target of autoimmunity in other immunological diseases. In this paper, with hsp70 as a model protein to study the e antigenic activity of Echinococcus granulosus (E.g) with the e antigen of echinococcosis patients, and then explore the hydatid immune evasion mechanism.