Grzych J M, Capron M, Lambert P H, Dissous C, Torres S, Capron A
Nature. 1985;316(6023):74-6. doi: 10.1038/316074a0.
Schistosomiasis is a parasitic infection of man which is widespread in tropical countries, and which so far has resisted attempts at control. We have been approaching the problem from an immunological angle. We have previously reported the production of a rat monoclonal IgG2a antibody against Schistosoma mansoni which exhibits marked cytoxicity for schistosomula in the presence of eosinophils and a high degree of protection by passive transfer in naive rats. This antibody, IPLSm1, was shown to bind specifically to a schistosomulum membrane target antigen defined as a glycoprotein of relative molecular mass 38,000 (38K), which is strongly immunogenic in schistosome infection of various animal species including man. Although theoretically the 38K protein represents an excellent candidate for a potential vaccine against schistosomiasis, the glycanic nature of the epitope recognized by IPLSm1 limits its production by DNA recombinant technology. It was, moreover, shown that, together with protective antibodies, the 38K molecule was able to induce the production of blocking IgG2c antibodies that inhibit the functional properties of IPLSm1 both in vitro and in vivo. Therefore, following Jerne's network theory, we considered an alternative approach, the possibility of immunization using anti-idiotype antibodies. In the present study, rat monoclonal anti-idiotype antibodies were produced against IPLSm1 (AB1). Anti-idiotype antibodies (AB2) were selected by their capacity to inhibit the binding of radioiodinated AB1 to its 38K target antigen. Sera from naive LOU rats immunized with a purified AB2 preparation contained specific anti-schistosome antibodies (AB3) which bound to 38K. AB3 antibodies were strongly cytotoxic for schistosomula in the presence of rat eosinophils and conferred highly significant protection by passive transfer. Most importantly, rats immunized with AB2 demonstrated marked protection (50-80%) to a challenge infection.
血吸虫病是一种在热带国家广泛传播的人类寄生虫感染病,迄今为止一直难以控制。我们一直从免疫学角度研究这个问题。我们之前报道过,制备了一种针对曼氏血吸虫的大鼠单克隆IgG2a抗体,该抗体在嗜酸性粒细胞存在的情况下对血吸虫幼虫表现出显著的细胞毒性,并且通过在未感染的大鼠中进行被动转移可提供高度保护。这种抗体IPLSm1被证明能特异性结合一种血吸虫幼虫膜靶抗原,该抗原被定义为相对分子质量为38,000(38K)的糖蛋白,在包括人类在内的各种动物物种的血吸虫感染中具有很强的免疫原性。虽然理论上38K蛋白是抗血吸虫病潜在疫苗的极佳候选物,但IPLSm1识别的表位的聚糖性质限制了其通过DNA重组技术生产。此外,研究表明,38K分子与保护性抗体一起,能够诱导产生阻断性IgG2c抗体,该抗体在体外和体内均能抑制IPLSm1的功能特性。因此,根据耶尔恩的网络理论,我们考虑了另一种方法,即使用抗独特型抗体进行免疫的可能性。在本研究中,制备了针对IPLSm1(AB1)的大鼠单克隆抗独特型抗体。通过抑制放射性碘化AB1与其38K靶抗原结合的能力来选择抗独特型抗体(AB2)。用纯化的AB2制剂免疫的未感染LOU大鼠的血清中含有与38K结合的特异性抗血吸虫抗体(AB3)。在大鼠嗜酸性粒细胞存在的情况下,AB3抗体对血吸虫幼虫具有很强的细胞毒性,并通过被动转移提供高度显著的保护。最重要的是,用AB2免疫的大鼠对攻击感染表现出显著的保护作用(50 - 80%)。