Ouaissi M A, Auriault C, Santoro F, Capron A
J Immunol. 1981 Oct;127(4):1556-9.
It was previously reported that Schistosoma mansoni schistosomula in the presence of IgG activate complement through the classical pathway (CCP). In the present work we have demonstrated that schistosomula incubated with IgG peptides resulting from IgG hydrolysis by schistosomula proteases are able to initiate complement activation through CCP, since a marked consumption of C1, C4, and C2 was observed. Our results eliminate an eventual direct action of the substances released by schistosomula on the activation of CCP. The first step of CCP activation required the preliminary binding of IgG peptides on the schistosomula surface. This interaction induced an increase in the C1q uptake by schistosomula. Since the involvement of the Fc portion of IgG molecules has been clearly evidenced, in this case the peripheral globular subunits of C1q recognize the CH2 region on IgG peptides or intact IgG molecules. By this mechanism, the local consumption of complement around schistosomula could contribute to its survival in the host.
先前有报道称,曼氏血吸虫童虫在存在IgG的情况下通过经典途径(CCP)激活补体。在本研究中,我们证明,与曼氏血吸虫童虫蛋白酶水解IgG产生的IgG肽一起孵育的童虫能够通过CCP启动补体激活,因为观察到C1、C4和C2有显著消耗。我们的结果排除了童虫释放的物质对CCP激活的最终直接作用。CCP激活的第一步需要IgG肽预先结合在童虫表面。这种相互作用导致童虫对C1q摄取增加。由于IgG分子的Fc部分的参与已得到明确证实,在这种情况下,C1q的外周球形亚基识别IgG肽或完整IgG分子上的CH2区域。通过这种机制,童虫周围补体的局部消耗可能有助于其在宿主体内存活。