Wang Dai, Bresnahan Wade, Shenk Thomas
Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
Proc Natl Acad Sci U S A. 2004 Nov 23;101(47):16642-7. doi: 10.1073/pnas.0407233101. Epub 2004 Nov 9.
The human cytomegalovirus pUL21.5 protein is a small, secreted glycoprotein whose mRNA is packaged into virions. We demonstrate that pUL21.5 protein is a soluble CC chemokine receptor that functions as a decoy to modulate the host immune response to infection. In contrast to other viral chemokine-binding proteins, which interact promiscuously with multiple chemokines, pUL21.5 selectively binds RANTES (regulated upon activation, normal T cell expressed and secreted) with high affinity. By binding RANTES, pUL21.5 blocks RANTES interaction with its cellular receptors. We propose that human cytomegalovirus directs the synthesis of a secreted, virus-coded protein that modulates the host antiviral response even before the newly infecting viral genome becomes transcriptionally active.
人类巨细胞病毒pUL21.5蛋白是一种小型分泌性糖蛋白，其mRNA被包装进病毒粒子中。我们证明pUL21.5蛋白是一种可溶性CC趋化因子受体，作为诱饵发挥作用，调节宿主对感染的免疫反应。与其他能与多种趋化因子随意相互作用的病毒趋化因子结合蛋白不同，pUL21.5以高亲和力选择性结合RANTES（活化时调节、正常T细胞表达和分泌）。通过结合RANTES，pUL21.5阻断RANTES与其细胞受体的相互作用。我们提出，人类巨细胞病毒指导合成一种分泌性的、病毒编码的蛋白，该蛋白甚至在新感染的病毒基因组转录激活之前就调节宿主的抗病毒反应。
