摘要
ICP22作为单纯疱疹病毒进入细胞后最早表达的蛋白之一,对于病毒的复制具有重要的调节功能,由于抗原表位的同源性,使用完整的ICP22蛋白作为抗原难以获得特异性的抗体。通过氨基酸序列预测,ICP22蛋白1～36位氨基酸具有较强的抗原性,将ICP22蛋白1-36位氨基酸偶联于GTS蛋白作为抗原免疫小鼠,所制备抗体能够特异性识别具有正常生理构象的ICP22蛋白。抗体检测结果显示,ICP22不但定位于细胞核内,而且还能够形成特殊的点状结构。
As one of the viral proteins expressed in the immediate-early phase of HSVI infection, ICP22 functions in the regulation of viral replication. However, it is difficult to produce specific antibody against ICP22 protein with homology of antigenicity in this protein. Based upon prediction of antigenicity of ICP22, a peptide of 1-36 amino acids was thought to possess a specific antigenic epitope, which was expressed as a fusion protein with GST. The antibody, raised in mice immunized with a purified fusion protein, was able to recognize ICP22 expressed in eukaryotic cells. Analysis with this antibody suggested a nuclear locatization of ICP22 and specific punctuative structure in cells.
出处
《中国病毒学》
CSCD
2006年第3期221-225,共5页
Virologica Sinica
基金
国家自然科学基金资助项目(30370065
30570081)
