Ferreira A M, Würzner R, Hobart M J, Lachmann P J
Molecular Immunopathology Unit, MRC Centre, Cambridge, UK.
Parasite Immunol. 1995 May;17(5):245-51. doi: 10.1111/j.1365-3024.1995.tb01022.x.
In the present study we have investigated the fluid phase activation of the complement (C) alternative pathway by Echinococcus granulosus sheep hydatid cyst fluid (SHCF) and its higher molecular weight fraction (SHCF-I) by quantitating the formation of both the terminal C intermediary C5b6 complex and the terminal C complex (TCC). Our results show that in vitro C activation progresses beyond the C5 step suggesting that potentially lytic complexes may be generated in vivo. In addition, SHCF and SHCF-I glucidic moieties are probably involved in C activation since 80% and 86% of SHCF and SHCF-I activity respectively was destroyed by periodate oxidation. Furthermore, partial deglycosylation with Peptide N-Glycosidase F of SHCF-I which had been digested with Pronase E, released an active fraction (MW < 14 KDa) which bound to Soybean agglutinin, suggesting that N-linked oligosaccharides containing alpha- or beta-linked N-acetyl galactosamine play a role in C activation by SHCF.
在本研究中，我们通过定量终末补体中间产物C5b6复合物和终末补体复合物（TCC）的形成，研究了细粒棘球绦虫绵羊包虫囊液（SHCF）及其高分子量组分（SHCF-I）对补体（C）替代途径的液相激活作用。我们的结果表明，体外补体激活在C5步骤之后仍继续进行，这表明体内可能会产生潜在的溶解复合物。此外，SHCF和SHCF-I的糖部分可能参与补体激活，因为经高碘酸盐氧化后，SHCF和SHCF-I的活性分别有80%和86%被破坏。此外，用肽N-糖苷酶F对经链霉蛋白酶E消化的SHCF-I进行部分去糖基化处理后，释放出一个与大豆凝集素结合的活性组分（分子量<14 kDa），这表明含有α-或β-连接的N-乙酰半乳糖胺的N-连接寡糖在SHCF激活补体过程中发挥作用。
