Mocarski E S, Pereira L, McCormick A L
Department of Microbiology and Immunology, Stanford University School of Medicine, California 94305.
J Gen Virol. 1988 Oct;69 ( Pt 10):2613-21. doi: 10.1099/0022-1317-69-10-2613.
We employed a murine monoclonal antibody (CH41) and a lambda gt11 library of human cytomegalovirus (CMV) DNA fragments to map the gene for a viral protein, denoted infected cell protein (ICP) 22, to the HWLF1 open reading frame in the S component of the CMV genome (0.92 to 0.93 map units). By using antibody CH41 in immunofluorescence, immunoprecipitation and immunoblotting analyses, ICP22 was readily detected as a beta (delayed early) gene product during viral growth. The cellular localization of this protein was found to be nuclear by immunofluorescence analysis; however, it partitioned with the cytoplasm when cells were fractionated with non-ionic detergents. Analysis of cell-free medium showed that a proportion of ICP22 was released from cells as a soluble protein at both early (24 h) and late (72 to 120h) times in infection. The function of this protein which has such diverse characteristics remains unknown.
我们使用了一种鼠单克隆抗体(CH41)和一个人巨细胞病毒(CMV)DNA片段的λgt11文库,将一种病毒蛋白(称为感染细胞蛋白(ICP)22)的基因定位到CMV基因组S成分中的HWLF1开放阅读框(0.92至0.93个图距单位)。通过在免疫荧光、免疫沉淀和免疫印迹分析中使用抗体CH41,在病毒生长过程中很容易将ICP22检测为一种β(延迟早期)基因产物。通过免疫荧光分析发现该蛋白的细胞定位是细胞核;然而,当用非离子去污剂对细胞进行分级分离时,它与细胞质一起分离。对无细胞培养基的分析表明,在感染的早期(24小时)和晚期(72至120小时),一定比例的ICP22作为可溶性蛋白从细胞中释放出来。这种具有多种特性的蛋白的功能仍然未知。