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已知模型抗原卵白蛋白(OVA)能用化学方法与小热休克蛋白(sHsp)笼相结合,笼的结构类似于病毒样颗粒(VLPs)。OVA-sHsp的结合效率取决于所用小分子接头的长度和化学计量及其在sHsp笼上的粘着位置。当OVA-sHsp结合物鼻内用于首次受试的小鼠时,对OVA的免疫应答加速了且强化了,1剂免疫后的5 d内有明显的OVA特异性IgG1应答,说明它可用于疫苗的开发。如果动物在OVA-sHsp结合物免疫前用不同的VLP、P22C(非复制性噬菌体衣壳)预处理,初次接触OVA的小鼠在1剂免后的第4 d就已有明显的OVA特异性IgG1应答。另外,用P22预处理的小鼠产生了高滴度的的黏膜IgA和同族型改变的OVA特异性血清IgG。
It is known that the model antigen ovalbumin (OVA) can be chemically bound to a small heat shock protein (sHsp) cage that is structurally similar to virus-like particles (VLPs). The binding efficiency of OVA-sHsp depends on the length and stoichiometry of the small molecule linker used and its location on the sHsp cage. When the OVA-sHsp conjugate was used intranasally in na [iota] ve mice, the immune response to OVA was accelerated and intensified with a clear OVA-specific IgGl response within 5 days after one dose of immunization, indicating that it can be used in Vaccine development. If animals were pre-treated with different VLPs, P22C (non-replicating phage capsid) prior to OVA-sHsp conjugate immunization, naive OVA-exposed mice had significant OVA specificity at day 4 after 1 dose IgG1 response. In addition, mice pre-treated with P22 produced high-titer mucosal IgA and congeneric-altered OVA-specific serum IgG.