Wang Hao, Strandin Tomas, Hepojoki Jussi, Lankinen Hilkka, Vaheri Antti
Department of Virology, Haartman Institute, PO Box 21, FIN-00014 University of Helsinki, Finland.
J Gen Virol. 2009 Dec;90(Pt 12):2995-3001. doi: 10.1099/vir.0.012179-0. Epub 2009 Aug 12.
The cytoplasmic tails of envelope glycoprotein Gn of pathogenic hantaviruses but not of the apathogenic Prospect Hill virus (PHV) were recently reported to be proteasomally degraded in simian COS7 cells. Here, we show that the cytoplasmic tails of the glycoproteins of the apathogenic hantaviruses Tula virus (TULV) and PHV are also degraded through the ubiquitin-proteasome pathway, both in human HEK-293 and in simian Vero E6 cells. TULV Gn tails formed aggresomes in cells with proteasomal inhibitors. We conclude that degradation upon aggregation of Gn tails, which may represent a general cellular response to misfolded protein used by hantaviruses to control maturation of virions, is unrelated to pathogenicity.
最近有报道称，致病性汉坦病毒包膜糖蛋白Gn的细胞质尾巴在猿猴COS7细胞中会被蛋白酶体降解，但无致病性的展望山病毒（PHV）则不会。在此，我们表明，无致病性的汉坦病毒图拉病毒（TULV）和PHV糖蛋白的细胞质尾巴在人胚肾293细胞和猿猴Vero E6细胞中也通过泛素-蛋白酶体途径被降解。在存在蛋白酶体抑制剂的细胞中，TULV Gn尾巴会形成聚集体。我们得出结论，Gn尾巴聚集时的降解可能代表细胞对错误折叠蛋白的一种普遍反应，汉坦病毒利用这种反应来控制病毒粒子的成熟，而这与致病性无关。
