Hennessy K, Fennewald S, Hummel M, Cole T, Kieff E
Proc Natl Acad Sci U S A. 1984 Nov;81(22):7207-11. doi: 10.1073/pnas.81.22.7207.
The nucleotide sequence of an Epstein-Barr virus gene expressed in latently infected growth-transformed cells is known to include a long open reading frame containing a 33-base-pair repeat element. A bacterial fusion protein constructed from a portion of the reading frame and Escherichia coli beta-galactosidase was used to produce sera in rabbits against the previously unidentified gene product. The viral protein detected with these sera in latently infected cells varies in size with the number of copies of the DNA repeat element. Translation of the RNA in vitro yields a protein of similar size. As expected from its primary sequence, the protein is a membrane protein. Immunofluorescence studies with the rabbit antisera suggest that the protein is in the plasma membrane. Thus, this protein could be the lymphocyte-determined membrane antigen (LYDMA) responsible for the generation of T-cell immunity to latently infected cells.
已知在潜伏感染的生长转化细胞中表达的爱泼斯坦-巴尔病毒基因的核苷酸序列包含一个长开放阅读框，该阅读框含有一个33个碱基对的重复元件。由该阅读框的一部分与大肠杆菌β-半乳糖苷酶构建的细菌融合蛋白被用于在兔中产生针对先前未鉴定的基因产物的血清。用这些血清在潜伏感染细胞中检测到的病毒蛋白大小随DNA重复元件的拷贝数而变化。该RNA的体外翻译产生大小相似的蛋白质。从其一级序列预期，该蛋白质是一种膜蛋白。用兔抗血清进行的免疫荧光研究表明该蛋白质存在于质膜中。因此，这种蛋白质可能是负责产生针对潜伏感染细胞的T细胞免疫的淋巴细胞决定的膜抗原（LYDMA）。
