Kusov Y Y, Probst C, Jecht M, Jost P D, Gauss-Müller V
Institute of Medical Microbiology, Medical University of Lübeck, Germany.
Arch Virol. 1998;143(5):931-44. doi: 10.1007/s007050050343.
The direct function of hepatitis A virus (HAV) protein 2C, a putative NTPase, is not known, yet genetic evidence obtained from chimeric viruses carrying the 2C genomic region of different HAV variants indicates that it plays a pivotal role in viral replication. In a first assessment of its potential function(s), membrane and RNA binding properties of HAV 2C were studied after expressing the protein in various recombinant systems. In contrast to poliovirus 2C, expression of HAV 2C was inhibitory to the growth and protein synthesis of bacteria. Deletion of the N-terminal amphipathic helix of 2C abrogated this effect and the ability of 2C to associate with eukaryotic membranes. Both, purified 2C and the N-terminally truncated protein were shown to bind RNA in vitro. Our data taken together suggest that HAV 2C is a multifunctional protein.
甲型肝炎病毒（HAV）的蛋白2C是一种假定的NTP酶，其直接功能尚不清楚，但从携带不同HAV变体2C基因组区域的嵌合病毒获得的遗传学证据表明，它在病毒复制中起关键作用。在对其潜在功能的首次评估中，在各种重组系统中表达该蛋白后，研究了HAV 2C的膜结合和RNA结合特性。与脊髓灰质炎病毒2C不同，HAV 2C的表达对细菌的生长和蛋白质合成具有抑制作用。删除2C的N端两亲性螺旋消除了这种作用以及2C与真核细胞膜结合的能力。纯化的2C和N端截短的蛋白均显示在体外能结合RNA。综合我们的数据表明，HAV 2C是一种多功能蛋白。
