Bour S P, Aberham C, Perrin C, Strebel K
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892-0460, USA.
J Virol. 1999 Jan;73(1):778-82. doi: 10.1128/JVI.73.1.778-782.1999.
In addition to its role in receptor binding, the envelope glycoprotein of certain human immunodeficiency virus type 2 (HIV-2) isolates, including ROD10, exhibits a biological activity that enhances the release of HIV-2, HIV-1, and simian immunodeficiency virus particles from infected cells. The present study aims at better defining the functional domains involved in this biological activity. To this end, we have characterized the envelope protein of the ROD14 isolate of HIV-2, which, despite 95% homology with the ROD10 envelope at the amino acid level, is unable to enhance viral particle release. Site-directed mutagenesis showed that the presence of a truncation in the cytoplasmic tail of the ROD14 envelope was not responsible for the lack of activity, as previously reported for the HIV-2 ST isolate (G. D. Ritter, Jr., G. Yamshchikov, S. J. Cohen, and M. J. Mulligan, J. Virol. 70:2669-2673, 1996). Similarly, several modifications of the length of the ROD10 envelope cytoplasmic tail did not impair its ability to enhance particle release, suggesting that, in the case of the HIV-2 ROD isolate, particle release activity is not regulated by the length of the cytoplasmic tail.
除了在受体结合中的作用外，某些2型人类免疫缺陷病毒（HIV-2）毒株（包括ROD10）的包膜糖蛋白还具有一种生物活性，可增强HIV-2、HIV-1和猿猴免疫缺陷病毒颗粒从受感染细胞中的释放。本研究旨在更好地确定参与这种生物活性的功能域。为此，我们对HIV-2的ROD14毒株的包膜蛋白进行了表征，该毒株尽管在氨基酸水平上与ROD10包膜具有95%的同源性，但无法增强病毒颗粒的释放。定点诱变表明，ROD14包膜细胞质尾部的截断并非缺乏活性的原因，这与之前关于HIV-2 ST毒株的报道不同（G. D. Ritter, Jr., G. Yamshchikov, S. J. Cohen, and M. J. Mulligan, J. Virol. 70:2669-2673, 1996）。同样，对ROD10包膜细胞质尾部长度的几种改变并没有损害其增强颗粒释放的能力，这表明，就HIV-2 ROD毒株而言，颗粒释放活性不受细胞质尾部长度的调节。
