Sakaguchi Suehiro, Arakawa Takeshi
Division of Molecular Cytology, The Institute for Enzyme Research, The University of Tokushima, 3-18-15 Kuramoto-cho, Tokushima 770-8503, Japan.
Expert Rev Vaccines. 2007 Feb;6(1):75-85. doi: 10.1586/14760584.6.1.75.
Bovine spongiform encephalopathy in cattle is highly suspected to be orally transmitted to humans through contaminated food, causing new variant Creutzfeldt-Jakob disease. However, no prophylactic procedures against these diseases, such as vaccines, in particular those stimulating mucosal protective immunity, have been established. The causative agents of these diseases, termed prions, consist of the host-encoded prion protein (PrP). Therefore, prions are immunologically tolerated, inducing no host antibody responses. This immune tolerance to PrP has hampered the development of vaccines against prions. We and others recently reported that the immune tolerance could be successfully broken and mucosal immunity could be stimulated by mucosal immunization of mice with PrP fused with bacterial enterotoxin or delivered using an attenuated Salmonella strain, eliciting significantly higher immunoglobulin A and G antibody responses against PrP. In this review, we will discuss these reports.
牛海绵状脑病极有可能通过受污染的食物经口传播给人类，引发新型变异型克雅氏病。然而，尚未确立针对这些疾病的预防性措施，如疫苗，尤其是那些能刺激黏膜保护性免疫的疫苗。这些疾病的病原体被称为朊病毒，由宿主编码的朊病毒蛋白（PrP）组成。因此，朊病毒在免疫上具有耐受性，不会诱导宿主产生抗体反应。这种对PrP的免疫耐受性阻碍了抗朊病毒疫苗的研发。我们和其他研究团队最近报告称，通过用与细菌肠毒素融合的PrP对小鼠进行黏膜免疫，或使用减毒沙门氏菌菌株递送PrP，可以成功打破免疫耐受性并刺激黏膜免疫，从而引发针对PrP的显著更高的免疫球蛋白A和G抗体反应。在这篇综述中，我们将讨论这些报告。
