Bennett R P, Wills J W
Department of Microbiology and Immunology, Pennsylvania State University College of Medicine, Hershey, Pennsylvania 17033, USA.
J Virol. 1999 Mar;73(3):2045-51. doi: 10.1128/JVI.73.3.2045-2051.1999.
Rous sarcoma virus (RSV) and murine leukemia virus (MLV) are examples of distantly related retroviruses that normally do not encounter one another in nature. Their Gag proteins direct particle assembly at the plasma membrane but possess very little sequence similarity. As expected, coexpression of these two Gag proteins did not result in particles that contain both. However, when the N-terminal membrane-binding domain of each molecule was replaced with that of the Src oncoprotein, which is also targeted to the cytoplasmic face of the plasma membrane, efficient copackaging was observed in genetic complementation and coimmunoprecipitation assays. We hypothesize that the RSV and MLV Gag proteins normally use distinct locations on the plasma membrane for particle assembly but otherwise have assembly domains that are sufficiently similar in function (but not sequence) to allow heterologous interactions when these proteins are redirected to a common membrane location.
劳氏肉瘤病毒（RSV）和鼠白血病病毒（MLV）是关系较远的逆转录病毒的例子，它们在自然界中通常不会相遇。它们的Gag蛋白在质膜处指导病毒颗粒组装，但序列相似性非常低。不出所料，这两种Gag蛋白的共表达并未产生同时包含两者的病毒颗粒。然而，当每个分子的N端膜结合结构域被同样靶向质膜胞质面的Src癌蛋白的结构域取代时，在基因互补和共免疫沉淀试验中观察到了有效的共包装。我们推测，RSV和MLV的Gag蛋白通常在质膜上使用不同的位置进行病毒颗粒组装，但除此之外，它们具有功能（而非序列）足够相似的组装结构域，以便当这些蛋白被重定向到共同的膜位置时能够进行异源相互作用。
