Identification of the fusion domain in the visna virus transmembrane protein.
Identification of the fusion domain in the visna virus transmembrane protein.
复制标题
维斯纳病毒跨膜蛋白融合结构域的鉴定。
DOI：
10.1016/0042-6822(91)90805-l
复制
发表时间：
1991
期刊：
影响因子：
3.7
通讯作者：
Clements,JE
中科院分区：
文献类型：
--
作者：
Crane,SE;Kanda,P;Clements,JE
Visna病毒是一种绵羊慢病毒，可导致敏感细胞融合。先前已经证明融合是由病毒包膜糖蛋白介导的。Visna病毒的跨膜蛋白在其氨基末端含有一个疏水区。该区域与正粘病毒和副粘病毒的融合表位相似。该区域位于HIV-1和SIV跨膜蛋白中融合表位的位置。为了确定该疏水区域在Visna病毒诱导的细胞融合中的作用，我们合成了与该区域相对应的24个氨基酸的多肽。这种多肽本身就能诱导山羊细胞融合。这种多肽的抗体抑制病毒诱导的细胞融合和山羊细胞中的多肽融合。此外，这种多肽与细胞的直接融合是一个独特的观察结果，可能有助于研究其他慢病毒的融合表位。因此，这个疏水区似乎是Visna病毒诱导细胞融合的一个表位。
Visna virus, a lentivirus of sheep, causes fusion of susceptible cells. Fusion has previously been shown to be mediated by the viral envelope glycoprotein. The transmembrane protein of visna virus contains a hydrophobic region at its amino terminus. This region is similar to the fusion epitopes of the orthomyxoviruses and paramyxoviruses. This region is located in a position similar to that of the fusion epitopes in the transmembrane proteins of HIV-1 and SIV. To determine the role of this hydrophobic region in visna virus-induced cell fusion, a peptide of 24 amino acids corresponding to this region was synthesized. The peptide alone induces fusion of goat cells. Antibodies to this peptide inhibit both viral-induced cell fusion and peptide fusion in goat cells. Further, the direct fusion of cells by this peptide is a unique observation and may be useful for studying the fusion epitopes of other lentiviruses. Thus, this hydrophobic region appears to be one epitope responsible for visna virus-induced cell fusion.