人类I型T细胞白血病病毒包膜糖蛋白与人类白细胞介素-2中涉及与β受体结合的区域之间的免疫和结构同源性。

Kohtz D S, Altman A, Kohtz J D, Puszkin S

Department of Pathology, Mount Sinai School of Medicine, City University of New York, New York 10029.

J Virol. 1988 Feb;62(2):659-62. doi: 10.1128/JVI.62.2.659-662.1988.

The N-terminal segment of human interleukin-2 (hIL-2) appears to mediate binding of the beta hIL-2 receptor (R. Robb, C. Rusk, J. Yodoi, and W. Greene, Proc. Natl. Acad. Sci. USA 84:2002-2006, 1987). An affinity-purified antibody prepared against this peptide segment (p81) is shown here to cross-react with a homologous region of the human T-cell leukemia virus type I (HTLV-I) envelope glycoprotein, raising the interesting possibility that the envelope glycoprotein of HTLV-I can interact with the beta hIL-2 receptor.

人白细胞介素-2（hIL-2）的N端片段似乎介导了β型hIL-2受体的结合（R.罗布、C.拉斯克、J.与登井、W.格林，《美国国家科学院院刊》84:2002 - 2006，1987年）。本文显示，针对该肽段（p81）制备的亲和纯化抗体与人I型T细胞白血病病毒（HTLV-I）包膜糖蛋白的同源区域发生交叉反应，这引发了一个有趣的可能性，即HTLV-I的包膜糖蛋白可能与β型hIL-2受体相互作用。