Everett R, O'Hare P, O'Rourke D, Barlow P, Orr A
Medical Research Council Virology Unit, Glasgow, Scotland.
J Virol. 1995 Nov;69(11):7339-44. doi: 10.1128/JVI.69.11.7339-7344.1995.
Herpes simplex virus type 1 immediate-early protein Vmw110 (also known as ICP0) has been implicated in the control of the balance between the lytic and latent states, but the precise mechanisms by which it exerts its effects are unknown. Vmw110 includes a characteristic zinc binding domain, termed the C3HC4 domain or RING finger, which is essential for its function. The solution structure of a related herpesvirus RING finger domain suggested that an amphipathic alpha helix might be an important functional component of the RING finger. In this paper, we show that the equivalent region of Vmw110 is important for virus growth in tissue culture and for the normal interaction of Vmw110 with nuclear structures which include the PML protein.
单纯疱疹病毒I型立即早期蛋白Vmw110(也称为ICP0)与裂解状态和潜伏状态之间平衡的控制有关,但其发挥作用的确切机制尚不清楚。Vmw110包含一个特征性的锌结合结构域,称为C3HC4结构域或环指结构域,这对其功能至关重要。一种相关疱疹病毒环指结构域的溶液结构表明,两亲性α螺旋可能是环指结构域的重要功能成分。在本文中,我们表明Vmw110的等效区域对于病毒在组织培养中的生长以及Vmw110与包括PML蛋白在内的核结构的正常相互作用很重要。